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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  70 GIVTKLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECV 149
Cdd:cd23309   1 GIVTRLYSRQGYYLQMQPDGTIDGTKDENSSYTLFNLIPVGLRVVAIQGVKTGLYIAMNSEGYLYTSEHFTPECKFKESV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18677743 150 FENYYVLYASALYRQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVPK 199
Cdd:cd23309  81 FENYYVIYSSMLYRQQQSGRAWYLGLNKEGQIMKGNRVKKTKPAAHFLPK 130

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  70 GIVTKLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECV 149
Cdd:cd23309   1 GIVTRLYSRQGYYLQMQPDGTIDGTKDENSSYTLFNLIPVGLRVVAIQGVKTGLYIAMNSEGYLYTSEHFTPECKFKESV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18677743 150 FENYYVLYASALYRQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVPK 199
Cdd:cd23309  81 FENYYVIYSSMLYRQQQSGRAWYLGLNKEGQIMKGNRVKKTKPAAHFLPK 130

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743    72 VTKLFCRQ-GFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVF 150
Cdd:pfam00167   2 VRRLYCRTgGFHLQILPDGKVDGTGEDGSPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFTDECVFKERLL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18677743   151 ENYYVLYASALYrqrrSGRAWYLGLDKEGRVMKGNRVKKTKAAAHF 196
Cdd:pfam00167  82 ENNYNTYASAKY----SGRGWYVGLNKKGRPKRGSKTKPGQKAAHF 123

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  70 GIVTKLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECV 149
Cdd:cd23309   1 GIVTRLYSRQGYYLQMQPDGTIDGTKDENSSYTLFNLIPVGLRVVAIQGVKTGLYIAMNSEGYLYTSEHFTPECKFKESV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18677743 150 FENYYVLYASALYRQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVPK 199
Cdd:cd23309  81 FENYYVIYSSMLYRQQQSGRAWYLGLNKEGQIMKGNRVKKTKPAAHFLPK 130

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  66 PQLKGIVTKLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRF 145
Cdd:cd23328   1 PQLKGIVTRLFSQQGYFLQMHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKAGLYVAMNGEGYLYSSDVFTPECKF 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18677743 146 KECVFENYYVLYASALYRQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVPKLLEV 203
Cdd:cd23328  81 KESVFENYYVIYSSTLYRQQESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIEV 138

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743     69 KGIVTKLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKEC 148
Cdd:smart00442   1 TKRLRQLYCRNGQHLQILPDGTVDGTRDESSSFTILEIIAVAVGVVAIKGVASCRYLCMNKCGKLYGSKNFTEDCVFREE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 18677743    149 VFENYYVLYASALYRQRrsgraWYLGLDKEGRVMKGNRVKKTKAAAHFVPK 199
Cdd:smart00442  81 MEENGYNTYASAKYRKR-----WYVALNKKGRPRRGQKTKPLQKASHFLPR 126

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  74 KLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVFENY 153
Cdd:cd00058   4 RLYSRTGYFLQILPDGTVNGTKDENSPYAILELQSVGTGLVRIKGVKTGRYLAMDKNGKLYGTKKPTEDCVFKETLEENG 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 18677743 154 YVLYASALYRQRRSGraWYLGLDKEGRVMKGNRVKKTKAAAHFVPK 199
Cdd:cd00058  84 YNTYSSYKYYHTRKG--WYLAIKKNGKPKRGKKTKPGQKSTQFLPL 127

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  74 KLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVFENY 153
Cdd:cd23308   4 QLYCRTGFHLEILPNGTVQGTRQDHSRFGILEFISVAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTRECVFREQFEENW 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 18677743 154 YVLYASALYRQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVPK 199
Cdd:cd23308  84 YNTYSSNLYKHADTGRRYYVALNKDGTPREGCRTKRHQKFTHFLPR 129

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  67 QLKGIVTK--LFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECR 144
Cdd:cd23325   8 HLKGILRRrqLYCRTGFHLEIFPNGTIQGTRKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECV 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18677743 145 FKECVFENYYVLYASALYRQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVPKLLEVAvyREPSLH 212
Cdd:cd23325  88 FREQFEENWYNTYSSNLYKHVDTGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVDPD--KVPELY 153

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  74 KLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVFENY 153
Cdd:cd23306   7 RLFSRTKFFLRIDKNGKVNGTKSENNPYSILEIRSVDVGVVAIKGVKSNYYLAMNKKGKLYGKKDYNDDCRFKERIEENG 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 18677743 154 YVLYASAlyRQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVP 198
Cdd:cd23306  87 YNTYASA--KWTHNGREMFVALSQKGRPLRGKKTRRKNTAAHFLP 129

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  73 TKLFCRQ-GFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVFE 151
Cdd:cd23304   3 KKLYCSNgGYHLRILPDGTVDGTREESDPYIILQLKAESPGVVVIKGTETGQYLAMNEDGRLYGSQTVNDECLFLERLEE 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18677743 152 NYYVLYASalyrQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVP 198
Cdd:cd23304  83 NHYNTYRS----QKYAEKNWYVGLKKNGRCKLGPRTHYGQKAILFLP 125

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  74 KLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVFENY 153
Cdd:cd23315   4 KLYCATKYHLQIHPNGKIDGTLEKNSVFSILEITAVDVGVVAIKGLFSGRYLAMNKRGRLYASEVYNAECEFVERIHELG 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18677743 154 YVLYASALY----------RQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVPKL 200
Cdd:cd23315  84 YNTYASRLYrtvpsgagtkRKASAERLWYVSINGKGRPRRGFKTRRTQKSSLFLPRV 140

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  72 VTKLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVFE 151
Cdd:cd23319  10 VRRLFCRTQWYLRIDKRGKVKGTQEMNNSYNILEIRTVAVGIVAIKGVESEYFLAMNKEGKLYGKKVCNEDCNFKELIEE 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18677743 152 NYYVLYASAlyRQRRSGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVP 198
Cdd:cd23319  90 NHYNTYASA--KWTHKGKEMFVALNQKGKPMKGKKTKKEHKTSHFLP 134

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  74 KLFCRQGFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVFENY 153
Cdd:cd23321  10 RLYSATKFFLRIDKGGRVEGTRWKNCPDSILEIRSVSVGVVAIKSVSTGFYLAMNKKGKLYGSKLYSPNCKFKERIEENG 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18677743 154 YVLYASALYRQRrsGRAWYLGLDKEGRVMKGNRVKKTKAAAHFVPKL 200
Cdd:cd23321  90 YNTYASLRWRHR--GRPMFLSLNSRGRPRRGGKTRRKHLSTHFLPML 134

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  80 GFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAECRFKECVFENYYVLYAS 159
Cdd:cd23311  12 NRYLQVNADGTVNGTTDSNSNDTVWQRIAVNNGKILIRSVATCMYLCINECGYVYSSKVPNKDCLFNESYEENNYNYYYK 91

                        90       100
                ....*....|....*....|.
gi 18677743 160 ALYRqRRSgrawYLGLDKEGR 180
Cdd:cd23311  92 KFNR-RRA----YLALNKEGK 107

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  82 YLQANPdGSIQGTPEDTSSFTHFNLIPVGLR-VVTIQSAKLGHYMAMNAEGLLYSSPHFTA--ECRFKECVFENYYVLYA 158
Cdd:cd23307  13 FVRITG-GRVDARGEKGSPYAKLTIESVGFSgKVRIRGAKSGRYLCFNKKGKLVAKKNGKKdkRCVFEEELTDGYYTRYR 91

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 18677743 159 SALYRQrrsgraWYLGLDKEGRVMKGNRV-KKTKAAAHF 196
Cdd:cd23307  92 SVKNPS------WYLGFNRNGRPLKGSKTrKKKQKCFHF 124

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  78 RQGFYLQANPDGSIQGTPEDTsSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAE-CRFKECVFENYYVL 156
Cdd:cd23333  27 RNSYHLQINPDGHVDGTPHQT-IYSALLIKSEDAGRVVITGVKSNRYLCMDFRGNIFGSHYFNKEdCLFQHETLENGYDV 105

                ....*.
gi 18677743 157 YASALY 162
Cdd:cd23333 106 YHSPKY 111

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18677743  82 YLQANPDGSIQGTPeDTSSFTHFNLIPVGLRVVTIQSAKLGHYMAMNAEGLLYSSPHFTAE-CRFKECVFENYYVLYAS 159
Cdd:cd23332  17 HLEIREDGTVGGAA-DQSPYSLLELKAVKPGVVQILGKKTLRFLCMDPDGRLYGSLHYSPEaCSFREVVLEDGYNLYQS 94

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743 114 VTIQSAKLGHYMAMNAEG-LLYSSPHFTAECRFKECVFENYYVLYASALYRqrrsgrAWYLGLDKEGRVMKGNRVKKTKA 192
Cdd:cd23322  66 VRIKGAETGYYICMNKKGkLIGKSNGKGKDCVFTEIVLENNYTALQNAKYE------GWYMAFTRKGRPRKGSKTRQHQR 139

                ....*...
gi 18677743 193 AAHFVPKL 200
Cdd:cd23322 140 EVHFMKRL 147

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  69 KGIVTKLFCRQ-GFYLQANPDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQS-AKLGHYMAM-------NAEGllyssphf 139
Cdd:cd23312   2 DGNVVQLYSKLtGQALRVKPDGSVDATGDKKDKFAYFRVHKVKGNIRIFQSvANPGYFLAIddgkvdgNGKG-------- 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18677743 140 TAECRFKECVFENYYVLYASALYRQRrsgrawYLGLDKEGRVMKGNRVKKtKAAAHFVPKL 200
Cdd:cd23312  74 GEDCEFRVRVQPDRSVTLESVKNPGQ------FVGFNPDGKPRDPRGTGD-GPNAQFYVYV 127

fascin-like domain, beta-trefoil fold, found in the hisactophilin subfamily; Hisactophilin is a histidine-rich actin-binding protein from Dictyostelium discoideum. It exists in two isoforms, hisactophilin-1 (HatA, also called HS I) and hisactophilin-2 (HatB, also called HS II), which are both myristoylated and distributed between plasma membrane and cytoplasm. Hisactophilin may act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments. Hisactophilin contains a fascin-like domain with 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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18677743  80 GFYLQANpDGSIQGTPEDTSSFTHFNLIPVGLRVVTIQSAKlGHYMAMNAEGLLYSSPHF 139
Cdd:cd23341  10 GHFLSAE-DGVVKTEHGHHDHHTHFHIENHGDDKVAIKTHH-GKYVAIDDNKQVYLSHHH 67