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Conserved domains on  [gi|15147348|ref|NP_149354|]
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fibroblast growth factor 8 isoform E precursor [Homo sapiens]

Protein Classification

fibroblast growth factor( domain architecture ID 10445583)

fibroblast growth factor (FGF) is a mitogen that stimulates growth or differentiation of cells of mesodermal or neuroectodermal origin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_FGF8 cd23322
FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; ...
 52-196 9.66e-103

FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; FGF8, also called androgen-induced growth factor (AIGF), or heparin-binding growth factor 8 (HBGF8), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It is required for normal brain, eye, ear, and limb development during embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. It plays a role in neurite outgrowth in hippocampal cells. FGF8 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF8 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


:

Pssm-ID: 467008  Cd Length: 147  Bit Score: 293.82  E-value: 9.66e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  52 QHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKK 131
Cdd:cd23322   3 QHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKKINAMAEDGDPHAKLIVETDTFGSRVRIKGAETGYYICMNKK 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15147348 132 GKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRL 196
Cdd:cd23322  83 GKLIGKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRL 147
 
Name Accession Description Interval E-value
beta-trefoil_FGF8 cd23322
FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; ...
 52-196 9.66e-103

FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; FGF8, also called androgen-induced growth factor (AIGF), or heparin-binding growth factor 8 (HBGF8), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It is required for normal brain, eye, ear, and limb development during embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. It plays a role in neurite outgrowth in hippocampal cells. FGF8 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF8 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467008  Cd Length: 147  Bit Score: 293.82  E-value: 9.66e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  52 QHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKK 131
Cdd:cd23322   3 QHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKKINAMAEDGDPHAKLIVETDTFGSRVRIKGAETGYYICMNKK 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15147348 132 GKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRL 196
Cdd:cd23322  83 GKLIGKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRL 147
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 70-193 1.38e-59

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organizms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organizms.


Pssm-ID: 425498  Cd Length: 124  Bit Score: 183.52  E-value: 1.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348    70 RTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGsRVRVRGAETGLYICMNKKGKLIAKSNGKgKDCVFTE 149
Cdd:pfam00167   1 RVRRLYCRTGGFHLQILPDGKVDGTGEDGSPYSILEIESVSVG-VVRIKGVESGLYLAMNKKGRLYGSKNFT-DECVFKE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 15147348   150 IVLENNYTALQNAKY--EGWYMAFTRKGRPRKGSKTRQHQREVHFM 193
Cdd:pfam00167  79 RLLENNYNTYASAKYsgRGWYVGLNKKGRPKRGSKTKPGQKAAHFL 124
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
 69-195 8.51e-40

Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The family play essential roles in patterning and differentiation during vertebrate embryogenesis, and have neurotrophic activities.


Pssm-ID: 214665  Cd Length: 126  Bit Score: 133.15  E-value: 8.51e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348     69 IRTYQLYSRTsGKHVQVLANKRINAMAEDGDPFakLIVETDTFG-SRVRVRGAETGLYICMNKKGKLIAKSNgKGKDCVF 147
Cdd:smart00442   2 KRLRQLYCRN-GQHLQILPDGTVDGTRDESSSF--TILEIIAVAvGVVAIKGVASCRYLCMNKCGKLYGSKN-FTEDCVF 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 15147348    148 TEIVLENNYTALQNAKYEG-WYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:smart00442  78 REEMEENGYNTYASAKYRKrWYVALNKKGRPRRGQKTKPLQKASHFLPR 126
 
Name Accession Description Interval E-value
beta-trefoil_FGF8 cd23322
FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; ...
 52-196 9.66e-103

FGF domain, beta-trefoil fold, found in fibroblast growth factor 8 (FGF8) and similar proteins; FGF8, also called androgen-induced growth factor (AIGF), or heparin-binding growth factor 8 (HBGF8), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It is required for normal brain, eye, ear, and limb development during embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. It plays a role in neurite outgrowth in hippocampal cells. FGF8 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF8 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467008  Cd Length: 147  Bit Score: 293.82  E-value: 9.66e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  52 QHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKK 131
Cdd:cd23322   3 QHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKKINAMAEDGDPHAKLIVETDTFGSRVRIKGAETGYYICMNKK 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15147348 132 GKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRL 196
Cdd:cd23322  83 GKLIGKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRL 147
beta-trefoil_FGF17 cd23323
FGF domain, beta-trefoil fold, found in fibroblast growth factor 17 (FGF17) and similar ...
 70-196 1.17e-73

FGF domain, beta-trefoil fold, found in fibroblast growth factor 17 (FGF17) and similar proteins; FGF17 plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. It is required for normal brain development. FGF17 interacts with fibroblast growth factor receptors, FGFR3 and FGFR4. FGF17 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467009  Cd Length: 126  Bit Score: 219.47  E-value: 1.17e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTSGKHVQVlANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTE 149
Cdd:cd23323   1 RVYQLYSRTSGKHVQV-TGRRVSATAEDGNKFAKLIVETDTFGSRVRIKGAESGKYICMNKRGKLVGKPNGKSKDCIFTE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15147348 150 IVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRL 196
Cdd:cd23323  80 IVLENNYTAFQNARHEGWFMAFTRKGRPRKASKTRQNQREVHFIKRL 126
beta-trefoil_FGF18 cd23324
FGF domain, beta-trefoil fold, found in fibroblast growth factor 18 (FGF18) and similar ...
 70-195 9.37e-66

FGF domain, beta-trefoil fold, found in fibroblast growth factor 18 (FGF18) and similar proteins; FGF18, also called zFGF5, plays an important role in the regulation of cell proliferation, cell differentiation, and cell migration. It is required for normal ossification and bone development. It stimulates hepatic and intestinal proliferation. FGF18 interacts with fibroblast growth factor receptors, FGFR3 and FGFR4. FGF18 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467010  Cd Length: 126  Bit Score: 199.41  E-value: 9.37e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTSGKHVQVLAnKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTE 149
Cdd:cd23324   1 RLYQLYSRTSGKHIQVLG-RRISARGEDGDKYAQLLVETDTFGSQVRIKGKETDFYLCMNRKGKLVGKPDGTSKECVFIE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15147348 150 IVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:cd23324  80 KVLENNYTALMSAKYSGWYVGFTKKGRPRKGPKTRENQQDVHFMKR 125
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
 70-193 1.38e-59

Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in growth and differentiation in a wide range of contexts. They are found in a wide range of organizms, from nematodes to humans. Most share an internal core region of high similarity, conserved residues in which are involved in binding with their receptors. On binding, they cause dimerization of their tyrosine kinase receptors leading to intracellular signalling. There are currently four known tyrosine kinase receptors for fibroblast growth factors. These receptors can each bind several different members of this family. Members of this family have a beta trefoil structure. Most have N-terminal signal peptides and are secreted. A few lack signal sequences but are secreted anyway; still others also lack the signal peptide but are found on the cell surface and within the extracellular matrix. A third group remain intracellular. They have central roles in development, regulating cell proliferation, migration and differentiation. On the other hand, they are important in tissue repair following injury in adult organizms.


Pssm-ID: 425498  Cd Length: 124  Bit Score: 183.52  E-value: 1.38e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348    70 RTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGsRVRVRGAETGLYICMNKKGKLIAKSNGKgKDCVFTE 149
Cdd:pfam00167   1 RVRRLYCRTGGFHLQILPDGKVDGTGEDGSPYSILEIESVSVG-VVRIKGVESGLYLAMNKKGRLYGSKNFT-DECVFKE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 15147348   150 IVLENNYTALQNAKY--EGWYMAFTRKGRPRKGSKTRQHQREVHFM 193
Cdd:pfam00167  79 RLLENNYNTYASAKYsgRGWYVGLNKKGRPKRGSKTKPGQKAAHFL 124
beta-trefoil_FGF8-like cd23307
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The ...
 70-195 2.87e-54

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 8 (FGF8)-like family; The FGF8-like family includes FGF8, FGF17 and FGF18. FGF8, also called androgen-induced growth factor (AIGF), or heparin-binding growth factor 8 (HBGF8), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It is required for normal brain, eye, ear,, and limb development during embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. It plays a role in neurite outgrowth in hippocampal cells. FGF8 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. FGF17 plays an important role in the regulation of embryonic development and as signaling molecule in the induction and patterning of the embryonic brain. It is required for normal brain development. FGF17 interacts with FGFR3 and FGFR4. FGF18, also called zFGF5, plays an important role in the regulation of cell proliferation, cell differentiation, and cell migration. It is required for normal ossification and bone development. It stimulates hepatic and intestinal proliferation. FGF18 interacts FGFR3 and FGFR4. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466993  Cd Length: 127  Bit Score: 170.11  E-value: 2.87e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTSGKHVQVLaNKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKD-CVFT 148
Cdd:cd23307   1 RSVRLYSRCSKKFVRIT-GGRVDARGEKGSPYAKLTIESVGFSGKVRIRGAKSGRYLCFNKKGKLVAKKNGKKDKrCVFE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15147348 149 EIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQH-QREVHFMKR 195
Cdd:cd23307  80 EELTDGYYTRYRSVKNPSWYLGFNRNGRPLKGSKTRKKkQKCFHFLKR 127
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
 69-195 8.51e-40

Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The family play essential roles in patterning and differentiation during vertebrate embryogenesis, and have neurotrophic activities.


Pssm-ID: 214665  Cd Length: 126  Bit Score: 133.15  E-value: 8.51e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348     69 IRTYQLYSRTsGKHVQVLANKRINAMAEDGDPFakLIVETDTFG-SRVRVRGAETGLYICMNKKGKLIAKSNgKGKDCVF 147
Cdd:smart00442   2 KRLRQLYCRN-GQHLQILPDGTVDGTRDESSSF--TILEIIAVAvGVVAIKGVASCRYLCMNKCGKLYGSKN-FTEDCVF 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 15147348    148 TEIVLENNYTALQNAKYEG-WYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:smart00442  78 REEMEENGYNTYASAKYRKrWYVALNKKGRPRRGQKTKPLQKASHFLPR 126
beta-trefoil_FGF cd00058
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
 70-195 7.52e-38

FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) superfamily; The FGF superfamily includes FGF1-23 and similar proteins. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. They play essential roles in patterning and differentiation during vertebrate embryogenesis and have neurotrophic activities. FGFs have a high affinity for heparan sulfate proteoglycans and require heparan sulfate to activate one of four cell surface FGF receptors. Upon binding to FGF, the receptors dimerize, and their intracellular tyrosine kinase domains become active. The structure of FGFs is typical of the beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466989  Cd Length: 127  Bit Score: 128.47  E-value: 7.52e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTsGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGsRVRVRGAETGLYICMNKKGKLIAKSNgKGKDCVFTE 149
Cdd:cd00058   1 RLVRLYSRT-GYFLQILPDGTVNGTKDENSPYAILELQSVGTG-LVRIKGVKTGRYLAMDKNGKLYGTKK-PTEDCVFKE 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15147348 150 IVLENNYTALQNAKY----EGWYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:cd00058  78 TLEENGYNTYSSYKYyhtrKGWYLAIKKNGKPKRGKKTKPGQKSTQFLPL 127
beta-trefoil_FGF3-like cd23305
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 3 (FGF3)-like family; The ...
 70-198 1.33e-31

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 3 (FGF3)-like family; The FGF3-like family includes FGF3-6. FGF3, also called heparin-binding growth factor 3 (HBGF3), or proto-oncogene Int-2, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal ear development. FGF3 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. FGF4, also called heparin secretory-transforming protein 1 (HST-1), or HSTF-1, or heparin-binding growth factor 4 (HBGF4), or transforming protein KS3, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal limb and cardiac valve development during embryogenesis. It interacts with FGFR1, FGFR2, FGFR3, and FGFR4. FGF5, also called heparin-binding growth factor 5 (HBGF5), or Smag-82, plays an important role in the regulation of cell proliferation and cell differentiation. It is required for normal regulation of the hair growth cycle. It functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase. FGF5 interacts with FGFR1 and FGFR2. FGF6, also called heparin secretory-transforming protein 2 (HST-2), or HSTF-2, or heparin-binding growth factor 6 (HBGF6), plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration. FGF6 interacts with FGFR1, FGFR2, and FGFR4. Affinity between FGFs and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466991  Cd Length: 127  Bit Score: 112.39  E-value: 1.33e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTSGKHVQVLANKRINAMAEDGDpFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAKSNgKGKDCVFTE 149
Cdd:cd23305   1 RYRLLYCRVIGFHLQILPDGSVNGTHEDTE-YSWLEIFAVEVGV-VGIKGVKSGLYLCMNKKGKLYGSKE-FTDECKFKE 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15147348 150 IVLENNYTALQNAKYE----GWYMAFTRKGRPRKGSKTRQHQREVHFmkrLPR 198
Cdd:cd23305  78 RLEENHYNTYSSALYPrrkrGWYVALSKKGRPRRGSRVRRTQKSTHF---LPR 127
beta-trefoil_FGF1-like cd23304
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 1 (FGF1)-like family; The ...
 73-198 8.34e-26

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 1 (FGF1)-like family; The FGF1-like family includes FGF1 and FGF2. FGF1, also called acidic fibroblast growth factor (aFGF), or endothelial cell growth factor (ECGF), or heparin-binding growth factor 1 (HBGF-1), plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation, and cell migration. It functions as a potent mitogen in vitro. FGF1 acts as a ligand for fibroblast growth factor receptor 1 (FGFR1) and integrin. It interacts with FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF1 also interacts with fibroblast growth factor-binding protein 1 (FGFBP1), FGF1, and FGF2. FGF2, also called basic fibroblast growth factor (bFGF), or heparin-binding growth factor 2 (HBGF2), acts as a ligand for FGFR1, FGFR2, FGFR3, and FGFR4. It also acts as an integrin ligand which is required for FGF2 signaling. FGF2 plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration. Both FGF1 and FGF2 contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466990  Cd Length: 127  Bit Score: 97.51  E-value: 8.34e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  73 QLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTEIVL 152
Cdd:cd23304   4 KLYCSNGGYHLRILPDGTVDGTREESDPYIILQLKAESPGV-VVIKGTETGQYLAMNEDGRLYG-SQTVNDECLFLERLE 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15147348 153 ENNYTALQNAKY--EGWYMAFTRKGRPRKGSKTRQHQREVHFmkrLPR 198
Cdd:cd23304  82 ENHYNTYRSQKYaeKNWYVGLKKNGRCKLGPRTHYGQKAILF---LPR 126
beta-trefoil_FGF9-like cd23308
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 9 (FGF9)-like family; The ...
 70-195 1.22e-21

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 9 (FGF9)-like family; The FGF9-like family includes FGF9, FGF16, and FGF20. FGF9, also called glia-activating factor (GAF), or heparin-binding growth factor 9 (HBGF-9), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It acts as a heparin-binding glia-activating factor that may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors. FGF9 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. FGF16 plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. It is required for normal cardiomyocyte proliferation and heart development. FGF16 interacts with FGFR1 and FGFR2. FGF20 acts as a neurotrophic factor that regulates central nervous development and function. It interacts with FGFR2 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466994  Cd Length: 130  Bit Score: 86.70  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTsGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTE 149
Cdd:cd23308   1 RRRQLYCRT-GFHLEILPNGTVQGTRQDHSRFGILEFISVAVGL-VSIRGVDSGLYLGMNEKGELYG-SEKLTRECVFRE 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15147348 150 IVLENNY-TALQNAKYEG-----WYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:cd23308  78 QFEENWYnTYSSNLYKHAdtgrrYYVALNKDGTPREGCRTKRHQKFTHFLPR 129
beta-trefoil_FGF20 cd23327
FGF domain, beta-trefoil fold, found in fibroblast growth factor 20 (FGF20) and similar ...
 68-195 5.14e-18

FGF domain, beta-trefoil fold, found in fibroblast growth factor 20 (FGF20) and similar proteins; FGF20 acts as a neurotrophic factor that regulates central nervous development and function. It interacts with fibroblast growth factor receptors, FGFR2 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF20 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467013  Cd Length: 153  Bit Score: 77.69  E-value: 5.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  68 LIRTYQLYSRTsGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGsRVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVF 147
Cdd:cd23327   8 ILRRRQLYCRT-GFHLEILPDGSVQGTRKDHSRFGILEFISVAVG-LVSIRGVDSGLYLGMNDKGELYG-SEKLTAECIF 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15147348 148 TEIVLENNYTALQNAKYEG------WYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:cd23327  85 REQFEENWYNTYSSNLYKHgdtgrrYFVALNKDGTPRDGTRSKRHQKFTHFLPR 138
beta-trefoil_FGF6 cd23318
FGF domain, beta-trefoil fold, found in fibroblast growth factor 6 (FGF6) and similar proteins; ...
 70-196 3.38e-17

FGF domain, beta-trefoil fold, found in fibroblast growth factor 6 (FGF6) and similar proteins; FGF6, also called heparin secretory-transforming protein 2 (HST-2), or HSTF-2, or heparin-binding growth factor 6 (HBGF6), plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis, and myogenesis, and is required for normal muscle regeneration. FGF6 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF6 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467004  Cd Length: 125  Bit Score: 74.85  E-value: 3.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTS-GKHVQVLANKRINAMAEDgDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAKSNGKgKDCVFT 148
Cdd:cd23318   1 RLRRLYCNVGiGFHLQILPDGRINGVHNE-NQYSLLEISTVERGV-VSLYGVKSGLFVAMNSKGRLYGTPNFQ-DECKFK 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15147348 149 EIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRL 196
Cdd:cd23318  78 ETLLPNNYNAYESSLYKGAYIALSKHGRVKRGNKVSPAMTVTHFLPRI 125
beta-trefoil_FGF7-like cd23306
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 7 (FGF7)-like family; The ...
 69-196 1.16e-16

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 7 (FGF7)-like family; The FGF7-like family includes FGF7, FGF10 and FGF22. FGF7, also called heparin-binding growth factor 7 (HBGF7), or keratinocyte growth factor (KGF), and FGF10 play important roles in the regulation of embryonic development, cell proliferation, and cell differentiation. They are required for normal branching morphogenesis. FGF7 is a growth factor active on keratinocytes. It may act as major paracrine effector of normal epithelial cell proliferation. FGF10 may play a role in wound healing. FGF22 plays a role in the fasting response, glucose homeostasis, lipolysis, and lipogenesis. It can stimulate cell proliferation (in vitro). It may be involved in hair development. FGF7 interacts with fibroblast growth factor receptor FGFR2 and fibroblast growth factor-binding protein 1 (FGFBP1). FGF10 and FGF22 interact with FGFR1, FGFR2 and FGFBP1. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466992  Cd Length: 131  Bit Score: 73.61  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  69 IRTYQLYSRTSgKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAKSNgKGKDCVFT 148
Cdd:cd23306   3 VRWRRLFSRTK-FFLRIDKNGKVNGTKSENNPYSILEIRSVDVGV-VAIKGVKSNYYLAMNKKGKLYGKKD-YNDDCRFK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15147348 149 EIVLENNYTALQNAKYEG----WYMAFTRKGRPRKGSKTRQHQREVHFMKRL 196
Cdd:cd23306  80 ERIEENGYNTYASAKWTHngreMFVALSQKGRPLRGKKTRRKNTAAHFLPMV 131
beta-trefoil_FGF9 cd23325
FGF domain, beta-trefoil fold, found in fibroblast growth factor 9 (FGF9) and similar proteins; ...
 68-195 1.74e-16

FGF domain, beta-trefoil fold, found in fibroblast growth factor 9 (FGF9) and similar proteins; FGF9, also called glia-activating factor (GAF), or heparin-binding growth factor 9 (HBGF-9), plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation, and cell migration. It acts as a heparin-binding glia-activating factor that may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors. FGF9 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF9 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467011  Cd Length: 160  Bit Score: 73.97  E-value: 1.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  68 LIRTYQLYSRTsGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGsRVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVF 147
Cdd:cd23325  12 ILRRRQLYCRT-GFHLEIFPNGTIQGTRKDHSRFGILEFISIAVG-LVSIRGVDSGLYLGMNEKGELYG-SEKLTQECVF 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15147348 148 TEIVLENNYTALQNAKYEG------WYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:cd23325  89 REQFEENWYNTYSSNLYKHvdtgrrYYVALNKDGTPREGTRTKRHQKFTHFLPR 142
beta-trefoil_FGF4 cd23316
FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; ...
 70-196 2.80e-15

FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; FGF4, also called heparin secretory-transforming protein 1 (HST-1), or HSTF-1, or heparin-binding growth factor 4 (HBGF4), or transforming protein KS3, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal limb and cardiac valve development during embryogenesis. It interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF4 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467002  Cd Length: 125  Bit Score: 69.91  E-value: 2.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTS-GKHVQVLANKRINAM-AEDGDPFAKLI-VETDTfgsrVRVRGAETGLYICMNKKGKLIAkSNGKGKDCV 146
Cdd:cd23316   1 RLRRLYCNVGiGFHIQVLPDGRINGVhNENRYSLLEISpVERGV----VSIFGVKSGLFVAMNSKGKLYG-SPFFNDECK 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15147348 147 FTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRL 196
Cdd:cd23316  76 FKEILLPNNYNAYESRKYPGMYIALSKNGKTKKGNRVSPTMTVTHFLPRI 125
beta-trefoil_FGF16 cd23326
FGF domain, beta-trefoil fold, found in fibroblast growth factor 16 (FGF16) and similar ...
 68-195 3.26e-15

FGF domain, beta-trefoil fold, found in fibroblast growth factor 16 (FGF16) and similar proteins; FGF16 plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal cardiomyocyte proliferation and heart development. FGF16 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. FGF16 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467012  Cd Length: 150  Bit Score: 70.39  E-value: 3.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  68 LIRTYQLYSRTsGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGsRVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVF 147
Cdd:cd23326   5 ILRRRQLYCRT-GFHLEIFPNGTVHGTRQDHSRFGILEFISLAVG-LVSIRGVDSGLYLGMNERGELYG-SKKLTRECVF 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15147348 148 TEIVLENNYTALQNAKYEG------WYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:cd23326  82 REQFEENWYNTYASTLYKHadsgrqYYVALNKDGSPREGYRTKRHQKFTHFLPR 135
beta-trefoil_FGF2 cd23314
FGF domain, beta-trefoil fold, found in fibroblast growth factor 2 (FGF2) and similar proteins; ...
 73-193 1.73e-14

FGF domain, beta-trefoil fold, found in fibroblast growth factor 2 (FGF2) and similar proteins; FGF2, also called basic fibroblast growth factor (bFGF), or heparin-binding growth factor 2 (HBGF2), acts as a ligand for fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. It also acts as an integrin ligand which is required for FGF2 signaling. FGF2 plays an important role in the regulation of cell survival, cell division, cell differentiation, and cell migration. It functions as a potent mitogen in vitro. It can induce angiogenesis. FGF2 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467000  Cd Length: 125  Bit Score: 67.56  E-value: 1.73e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  73 QLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTEIVL 152
Cdd:cd23314   4 RLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGV-VSIKGVCANRYLAMKEDGRLLA-SKSVTDECFFFERLE 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15147348 153 ENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFM 193
Cdd:cd23314  82 SNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFL 122
beta-trefoil_FGF7 cd23319
FGF domain, beta-trefoil fold, found in fibroblast growth factor 7 (FGF7) and similar proteins; ...
 69-193 2.23e-14

FGF domain, beta-trefoil fold, found in fibroblast growth factor 7 (FGF7) and similar proteins; FGF7, also called heparin-binding growth factor 7 (HBGF7), or keratinocyte growth factor (KGF), plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal branching morphogenesis. It is a growth factor active on keratinocytes. It may act as major paracrine effector of normal epithelial cell proliferation. FGF7 interacts with fibroblast growth factor receptor FGFR2 and fibroblast growth factor-binding protein 1 (FGFBP1). Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF7 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467005  Cd Length: 136  Bit Score: 67.58  E-value: 2.23e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  69 IRTYQLYSRTSGkHVQVLANKRINAMAEDGDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAKSNGKgKDCVFT 148
Cdd:cd23319   8 VRVRRLFCRTQW-YLRIDKRGKVKGTQEMNNSYNILEIRTVAVGI-VAIKGVESEYFLAMNKEGKLYGKKVCN-EDCNFK 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15147348 149 EIVLENNYTALQNAKY--EGWYM--AFTRKGRPRKGSKTRQHQREVHFM 193
Cdd:cd23319  85 ELIEENHYNTYASAKWthKGKEMfvALNQKGKPMKGKKTKKEHKTSHFL 133
beta-trefoil_FGF1 cd23313
FGF domain, beta-trefoil fold, found in fibroblast growth factor 1 (FGF1) and similar proteins; ...
 74-193 3.49e-13

FGF domain, beta-trefoil fold, found in fibroblast growth factor 1 (FGF1) and similar proteins; FGF1, also called acidic fibroblast growth factor (aFGF), or endothelial cell growth factor (ECGF), or heparin-binding growth factor 1 (HBGF1), plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation, and cell migration. It functions as potent mitogen in vitro. FGF-1 acts as a ligand for fibroblast growth factor receptor 1 (FGFR1) and integrins. It interacts with FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. It also interacts with fibroblast growth factor-binding protein 1 (FGFBP1), FGF1, and FGF2. It can induce angiogenesis. FGF1 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466999  Cd Length: 128  Bit Score: 64.08  E-value: 3.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  74 LYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTEIVLE 153
Cdd:cd23313   5 LYCSNGGHFLRILPDGTVDGTRDRSDQHIQLQLSAESVGE-VYIKSTETGQYLAMDTDGLLYG-SQTPNEECLFLERLEE 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15147348 154 NNYTALQNAKY--EGWYMAFTRKGRPRKGSKTRQHQREVHFM 193
Cdd:cd23313  83 NHYNTYISKKHaeKNWFVGLKKNGSCKRGPRTHYGQKAILFL 124
beta-trefoil_FGF13 cd23329
FGF domain, beta-trefoil fold, found in fibroblast growth factor 13 (FGF13) and similar ...
 73-195 5.44e-12

FGF domain, beta-trefoil fold, found in fibroblast growth factor 13 (FGF13) and similar proteins; FGF13, also called fibroblast growth factor homologous factor 2 (FHF2), is a microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules. Through its action on microtubules, it may participate in the refinement of axons by negatively regulating axonal and leading processes branching. FGF13 plays a crucial role in neuron polarization and migration in the cerebral cortex and the hippocampus. It may regulate voltage-gated sodium channels transport and function. It may also play a role in MAPK signaling. It is required for the development of axonal initial segment-targeting inhibitory GABAergic synapses made by chandelier neurons. FGF13 interacts with SCN1A, SCN5A, and SCN8A. It may also interact with SCN2A and SCN11A. FGF-13 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467015  Cd Length: 148  Bit Score: 61.59  E-value: 5.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  73 QLYSRtSGKHVQVLANKRINAMAEDGDPFAklIVETDTFGSRV-RVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTEIV 151
Cdd:cd23329   8 KLYSR-QGYHLQLQADGTIDGTKEEDSSYT--LFNLIPVGLRVvAIQGVQTKLYLAMNSEGYLYT-SEHFTPECKFKESV 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15147348 152 LENNYTALQNAKYE------GWYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:cd23329  84 FENYYVTYSSMIYRqqqsgrGWYLGLNKEGEIMKGNHVKKNKPAAHFLPK 133
beta-trefoil_FGF3 cd23315
FGF domain, beta-trefoil fold, found in fibroblast growth factor 3 (FGF3) and similar proteins; ...
 70-196 1.98e-11

FGF domain, beta-trefoil fold, found in fibroblast growth factor 3 (FGF3) and similar proteins; FGF3, also called heparin-binding growth factor 3 (HBGF3), or proto-oncogene Int-2, plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal ear development. FGF3 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. Affinity between FGFs and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF3 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467001  Cd Length: 140  Bit Score: 59.98  E-value: 1.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTSgKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTE 149
Cdd:cd23315   1 RRRKLYCATK-YHLQIHPNGKIDGTLEKNSVFSILEITAVDVGV-VAIKGLFSGRYLAMNKRGRLYA-SEVYNAECEFVE 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15147348 150 IVLENNYTALQNAKYEG----------------WYMAFTRKGRPRKGSKTRQHQREVHFMKRL 196
Cdd:cd23315  78 RIHELGYNTYASRLYRTvpsgagtkrkasaerlWYVSINGKGRPRRGFKTRRTQKSSLFLPRV 140
beta-trefoil_FGF11-like cd23309
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 11 (FGF11)-like family; ...
 73-195 3.71e-11

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 11 (FGF11)-like family; The FGF11-like family includes FGF11-14. FGF11, also called fibroblast growth factor homologous factor 3 (FHF3), may be involved in nervous system development and function. It plays roles in angiogenesis, tumorigenesis, adipogenesis, or liver regeneration. FGF12, also called fibroblast growth factor homologous factor 1 (FHF1), or myocyte-activating factor, is involved in nervous system development and function. It plays a role in the positive regulation of voltage-gated sodium channel activity. It promotes neuronal excitability by elevating the voltage dependence of neuronal sodium channel SCN8A fast inactivation. FGF12 interacts with the C-terminal region of SCN9A. FGF13, also called Fibroblast growth factor homologous factor 2 (FHF2), is a microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules. Through its action on microtubules, it may participate in the refinement of axons by negatively regulating axonal and leading processes branching. FGF13 plays a crucial role in neuron polarization and migration in the cerebral cortex and the hippocampus. It may regulate voltage-gated sodium channels transport and function. It may also play a role in MAPK signaling. It is required for the development of axonal initial segment-targeting inhibitory GABAergic synapses made by chandelier neurons. FGF13 interacts with SCN1A, SCN5A, and SCN8A. It may also interact with SCN2A and SCN11A. FGF14, also called fibroblast growth factor homologous factor 4 (FH-4), may be involved in nervous system development and function. It interacts with SCN8A. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466995  Cd Length: 130  Bit Score: 58.97  E-value: 3.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  73 QLYSRtSGKHVQVLANKRINAMAEDGDPFA--KLIvetdTFGSR-VRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTE 149
Cdd:cd23309   5 RLYSR-QGYYLQMQPDGTIDGTKDENSSYTlfNLI----PVGLRvVAIQGVKTGLYIAMNSEGYLYT-SEHFTPECKFKE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15147348 150 IVLENNYTALQNAKYE------GWYMAFTRKGRPRKGSKTRQHQREVHFMKR 195
Cdd:cd23309  79 SVFENYYVIYSSMLYRqqqsgrAWYLGLNKEGQIMKGNRVKKTKPAAHFLPK 130
beta-trefoil_FGF22 cd23321
FGF domain, beta-trefoil fold, found in fibroblast growth factor 22 (FGF22) and similar ...
 115-196 9.66e-10

FGF domain, beta-trefoil fold, found in fibroblast growth factor 22 (FGF22) and similar proteins; FGF22 plays a role in the fasting response, glucose homeostasis, lipolysis, and lipogenesis. It can stimulate cell proliferation (in vitro). It may be involved in hair development. FGF22 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2, as well as fibroblast growth factor-binding protein 1 (FGFBP1). FGF22 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467007  Cd Length: 134  Bit Score: 55.19  E-value: 9.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348 115 VRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTEIVLENNYT--ALQNAKYEGWYM--AFTRKGRPRKGSKTRQHQREV 190
Cdd:cd23321  50 VAIKSVSTGFYLAMNKKGKLYG-SKLYSPNCKFKERIEENGYNtyASLRWRHRGRPMflSLNSRGRPRRGGKTRRKHLST 128


                ....*.
gi 15147348 191 HFMKRL 196
Cdd:cd23321 129 HFLPML 134
beta-trefoil_FGF5 cd23317
FGF domain, beta-trefoil fold, found in fibroblast growth factor 5 (FGF5) and similar proteins; ...
 70-196 9.91e-10

FGF domain, beta-trefoil fold, found in fibroblast growth factor 5 (FGF5) and similar proteins; FGF5, also called heparin-binding growth factor 5 (HBGF5), or Smag-82, plays an important role in the regulation of cell proliferation and cell differentiation. It is required for normal regulation of the hair growth cycle. It functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase. FGF5 interacts with fibroblast growth factor receptors, FGFR1 and FGFR2. Affinity between FGFs and their receptors is increased by heparan sulfate glycosaminoglycans that function as coreceptors. FGF-5 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467003  Cd Length: 133  Bit Score: 54.90  E-value: 9.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  70 RTYQLYSRTS-GKHVQVLANKRINAmAEDGDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFT 148
Cdd:cd23317   1 RTGRLYCRVGiGFHLQIHPDGRVNG-SHEANLLSVLEIFAVSQGI-VGIRGVFSNRFLAMSKKGKLHA-SAKFTDDCKFR 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15147348 149 EIVLENNYTALQNAKYEG------WYMAFTRKGRPRKGSKTRQHQREV--HFMKRL 196
Cdd:cd23317  78 ERFQENSYNTYASATHRNhrtgreWYVALNKRGKAKRGCSPRVKPQHIstHFLPRF 133
beta-trefoil_FGF10 cd23320
FGF domain, beta-trefoil fold, found in fibroblast growth factor 10 (FGF10) and similar ...
 69-193 5.50e-09

FGF domain, beta-trefoil fold, found in fibroblast growth factor 10 (FGF10) and similar proteins; FGF10 plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. It is required for normal branching morphogenesis. It may play a role in wound healing. FGF10 interacts with fibroblast growth factor receptors FGFR1 and FGFR2, as well as fibroblast growth factor-binding protein 1 (FGFBP1). FGF10 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467006  Cd Length: 134  Bit Score: 53.01  E-value: 5.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  69 IRTYQLYSRTSgKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFT 148
Cdd:cd23320   6 VRWRKLFSFTK-YFLKIDKNGKVSGTKKENCPYSILEITSVEVGV-VAVKAINSNYYLAMNKKGKIYG-SKEFNIDCKLK 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15147348 149 EIVLENNYT--ALQNAKYEG--WYMAFTRKGRPRKGSKTRQHQREVHFM 193
Cdd:cd23320  83 ERIEENGYNtyASLNWKHNGrqMFVALNGKGAPKRGQKTRRKNTSAHFL 131
beta-trefoil_FGF_RP1 cd23312
FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ...
 73-183 2.27e-08

FGF domain, beta-trefoil fold, found in oxygen-regulated protein 1 (ORP1) and similar proteins; ORP1, also called retinitis pigmentosa 1 protein, or retinitis pigmentosa RP1 protein, is a microtubule-associated protein that regulates the stability and length of the microtubule-based axoneme of photoreceptors. It is required for the differentiation of photoreceptor cells. It plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Members in this family may contain one or two fibroblast growth factor (FGF) domain(s) in the middle region. The FGF domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466998  Cd Length: 128  Bit Score: 51.04  E-value: 2.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  73 QLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVetdtfgsrVRVRG--------AETGLYICMnKKGKLIAKSNGkGKD 144
Cdd:cd23312   7 QLYSKLTGQALRVKPDGSVDATGDKKDKFAYFRV--------HKVKGnirifqsvANPGYFLAI-DDGKVDGNGKG-GED 76

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15147348 145 CVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKT 183
Cdd:cd23312  77 CEFRVRVQPDRSVTLESVKNPGQFVGFNPDGKPRDPRGT 115
beta-trefoil_FGF_Bnl-like cd23311
FGF domain, beta-trefoil fold, found in Drosophila melanogaster protein branchless (Bnl) and ...
 65-193 9.58e-08

FGF domain, beta-trefoil fold, found in Drosophila melanogaster protein branchless (Bnl) and similar proteins; Protein Bnl is a homolog of mammalian fibroblast growth factors. It is a dosage-sensitive regulator of terminal branching. It functions as a chemoattractant that can guide terminal branches to new tissues and even to individual cells within a tissue. Bnl contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466997  Cd Length: 129  Bit Score: 49.53  E-value: 9.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  65 SRRLIrtyQLYSRtsGKHVQVLANKRINAMAEDGDP---FAKLIVETDTfgsrVRVRGAETGLYICMNKKGKL--IAKSN 139
Cdd:cd23311   2 TSRLI---QLFIN--NRYLQVNADGTVNGTTDSNSNdtvWQRIAVNNGK----ILIRSVATCMYLCINECGYVysSKVPN 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15147348 140 gkgKDCVFTEIVLENNYT----ALQNAKYegwYMAFTRKGRPRK-----GSKTRQHQREVHFM 193
Cdd:cd23311  73 ---KDCLFNESYEENNYNyyykKFNRRRA---YLALNKEGKTRRvvlpkSEPLGKLSRYTIVL 129
beta-trefoil_FGF12 cd23328
FGF domain, beta-trefoil fold, found in fibroblast growth factor 12 (FGF12) and similar ...
 115-195 1.45e-07

FGF domain, beta-trefoil fold, found in fibroblast growth factor 12 (FGF12) and similar proteins; FGF12, also called fibroblast growth factor homologous factor 1 (FHF1), or myocyte-activating factor, is involved in nervous system development and function. It plays a role in the positive regulation of voltage-gated sodium channel activity. It promotes neuronal excitability by elevating the voltage dependence of neuronal sodium channel SCN8A fast inactivation. FGF12 interacts with the C-terminal region of SCN9A. FGF12 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467014  Cd Length: 139  Bit Score: 49.25  E-value: 1.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348 115 VRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTEIVLENNYTALQNAKYE------GWYMAFTRKGRPRKGSKTRQHQR 188
Cdd:cd23328  49 VAIQGVKAGLYVAMNGEGYLYS-SDVFTPECKFKESVFENYYVIYSSTLYRqqesgrAWFLGLNKEGQIMKGNRVKKTKP 127


                ....*..
gi 15147348 189 EVHFMKR 195
Cdd:cd23328 128 SSHFVPK 134
beta-trefoil_FGF14 cd23330
FGF domain, beta-trefoil fold, found in fibroblast growth factor 14 (FGF14) and similar ...
 115-195 3.93e-07

FGF domain, beta-trefoil fold, found in fibroblast growth factor 14 (FGF14) and similar proteins; FGF14, also called fibroblast growth factor homologous factor 4 (FH-4), may be involved in nervous system development and function. It interacts with SCN8A. FGF14 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467016  Cd Length: 145  Bit Score: 48.12  E-value: 3.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348 115 VRVRGAETGLYICMNKKGKLIAkSNGKGKDCVFTEIVLENNYTALQNAKYE------GWYMAFTRKGRPRKGSKTRQHQR 188
Cdd:cd23330  50 VAIQGVKTGLYIAMNGEGYLYT-SELFTPECKFKESVFENYYVIYSSMLYRqqesgrAWFLGLNKEGQAMKGNRVKKTKP 128


                ....*..
gi 15147348 189 EVHFMKR 195
Cdd:cd23330 129 AAHFLPK 135
beta-trefoil_FGF23 cd23333
FGF domain, beta-trefoil fold, found in fibroblast growth factor 23 (FGF23) and similar ...
 66-164 8.46e-06

FGF domain, beta-trefoil fold, found in fibroblast growth factor 23 (FGF23) and similar proteins; FGF23, also called phosphatonin, or tumor-derived hypophosphatemia-inducing factor (HYPF), is a regulator of phosphate homeostasis. It inhibits renal tubular phosphate transport by reducing SLC34A1 levels. It upregulates EGR1 expression in the presence of alpha-Klotho (KL). It acts directly on the parathyroid to decrease PTH secretion. FGF23 acts as a regulator of vitamin-D metabolism. It negatively regulates osteoblast differentiation and matrix mineralization. FGF23 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by KL and heparan sulfate glycosaminoglycans that function as coreceptors. FGF23 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467019  Cd Length: 148  Bit Score: 44.36  E-value: 8.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  66 RRLIRTYQlYSRTSGKHVQVLANKRINAMAEDGdPFAKLIVETDTFGsRVRVRGAETGLYICMNKKGKLIAKSNGKGKDC 145
Cdd:cd23333  16 RRLIHLYT-STDRNSYHLQINPDGHVDGTPHQT-IYSALLIKSEDAG-RVVITGVKSNRYLCMDFRGNIFGSHYFNKEDC 92

                        90
                ....*....|....*....
gi 15147348 146 VFTEIVLENNYTALQNAKY 164
Cdd:cd23333  93 LFQHETLENGYDVYHSPKY 111
beta-trefoil_FGF19-like cd23310
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 19 (FGF19)-like family; ...
 115-164 1.81e-04

FGF domain, beta-trefoil fold, found in the fibroblast growth factor 19 (FGF19)-like family; The FGF19-like family includes FGF19, FGF21, and FGF23. FGF19 is involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. It stimulates glucose uptake in adipocytes. Its activity requires the presence of beta-Klotho (KLB) and FGFR4. FGF-19 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. FGF21 stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Its activity requires the presence of KLB. It interacts (via C-terminus) with KLB and fibroblast growth factor receptor FGFR4. FGF23, also called phosphatonin, or tumor-derived hypophosphatemia-inducing factor (HYPF), is a regulator of phosphate homeostasis. It inhibits renal tubular phosphate transport by reducing SLC34A1 levels. It upregulates EGR1 expression in the presence of alpha-Klotho (KL). It acts directly on the parathyroid to decrease PTH secretion. FGF23 acts as a regulator of vitamin-D metabolism. It negatively regulates osteoblast differentiation and matrix mineralization. FGF23 interacts with FGFR1, FGFR2, FGFR3, and FGFR4. Members in this family contain a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 466996  Cd Length: 121  Bit Score: 40.09  E-value: 1.81e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15147348 115 VRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKY 164
Cdd:cd23310  46 TVIKGVASSLYLCVDSDGKLKGQHHYDEEDCSFQELLLEDGYTVFLSPHH 95
beta-trefoil_FGF19 cd23331
FGF domain, beta-trefoil fold, found in fibroblast growth factor 19 (FGF19) and similar ...
 69-193 3.55e-03

FGF domain, beta-trefoil fold, found in fibroblast growth factor 19 (FGF19) and similar proteins; FGF19 is involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. It stimulates glucose uptake in adipocytes. Its activity requires the presence of beta-Klotho (KLB) and FGFR4. FGF-19 interacts with fibroblast growth factor receptors, FGFR1, FGFR2, FGFR3, and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by alpha-Klotho (KL), KLB and heparan sulfate glycosaminoglycans that function as coreceptors. FGF19 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467017  Cd Length: 128  Bit Score: 36.26  E-value: 3.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  69 IRTYQLYsrTSGKHVQVLANKRINAMAE-DGDPFAKL--IVETDTFGSR-VRVRGAETGLYICMNKKGKLIAKSNGKGKD 144
Cdd:cd23331   1 IRLRHLY--TARPHGLSSCFLRIRADGVvDGSRGQSAhsLLEIKAVALGtVAIKGVASSRYLCMEADGKLYGSLSYSEED 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15147348 145 CVFTEIVLENNYTALQNAKYeGWYMAFtRKGRPRKGSKTRQHQREVHFM 193
Cdd:cd23331  79 CSFEEEILPDGYNVYRSKKH-GLPVSL-SSAKQRQQYKDKGFLPLSQFL 125
beta-trefoil_FGF21 cd23332
FGF domain, beta-trefoil fold, found in fibroblast growth factor 21 (FGF21) and similar ...
 68-164 3.64e-03

FGF domain, beta-trefoil fold, found in fibroblast growth factor 21 (FGF21) and similar proteins; FGF21 stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Its activity requires the presence of beta-Klotho (KLB). It interacts (via C-terminus) with KLB and fibroblast growth factor receptor FGFR4. FGF21 contains a FGF domain with beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry.


Pssm-ID: 467018  Cd Length: 126  Bit Score: 36.31  E-value: 3.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15147348  68 LIRTYQLY--SRTSGKHVQVLANKRINAMAEDgDPFAKLIVETDTFGSrVRVRGAETGLYICMNKKGKLIAKSNGKGKDC 145
Cdd:cd23332   1 QVRLRHLYtaDEQTQLHLEIREDGTVGGAADQ-SPYSLLELKAVKPGV-VQILGKKTLRFLCMDPDGRLYGSLHYSPEAC 78

                        90
                ....*....|....*....
gi 15147348 146 VFTEIVLENNYTALQNAKY 164
Cdd:cd23332  79 SFREVVLEDGYNLYQSEAH 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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