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 1965385973  122 PIRLRHLYTAGPhglssCFLRIRADGSVDCARGQ-SAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSeED 200
Cdd:smart00442   1 TKRLRQLYCRNG-----QHLQILPDGTVDGTRDEsSSFTILEIIAVAVGVVAIKGVASCRYLCMNKCGKLYGSKNFT-ED 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1965385973  201 CAFEEEIRPDGYNVYRSEKHR--LPVSLSSARQRQLY-KGRGFLPLSHFLPM 249
Cdd:smart00442  75 CVFREEMEENGYNTYASAKYRkrWYVALNKKGRPRRGqKTKPLQKASHFLPR 126

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965385973 124 RLRHLYTAGPHglSSCFLRIRADGSVDCARGQSAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSEEDCAF 203
Cdd:cd23310     1 RQRHLYTETPR--SSCFLEIRPDGTVDGAPHQTAYSLLELKSVKPGETVIKGVASSLYLCVDSDGKLKGQHHYDEEDCSF 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1965385973 204 EEEIRPDGYNVYRSEKHRLPVSLSSARQRQlykgRGFLPLSHFLPML 250
Cdd:cd23310    79 QELLLEDGYTVFLSPHHGLPVSLLSKKQPF----RHPLPLSRFLPLR 121

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965385973 123 IRLRHLYTAGPHglSSCFLRIRADGSVDCARGQSAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSEEDCA 202
Cdd:cd23332     2 VRLRHLYTADEQ--TQLHLEIREDGTVGGAADQSPYSLLELKAVKPGVVQILGKKTLRFLCMDPDGRLYGSLHYSPEACS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1965385973 203 FEEEIRPDGYNVYRSEKHRLPVSLSSARQRQLyKGRGFLPLSHFLPM 249
Cdd:cd23332    80 FREVVLEDGYNLYQSEAHGLPLTLSPNRAPHR-DGGAPPPLAHFLPL 125

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965385973 124 RLRHLY--TAGPHglsscfLRIRADGSVDCARGQSAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSEEdC 201
Cdd:cd23305     1 RYRLLYcrVIGFH------LQILPDGSVNGTHEDTEYSWLEIFAVEVGVVGIKGVKSGLYLCMNKKGKLYGSKEFTDE-C 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1965385973 202 AFEEEIRPDGYNVYRSEKHRLP-----VSLS---------SARQRQLYkgrgflplSHFLP 248
Cdd:cd23305    74 KFKERLEENHYNTYSSALYPRRkrgwyVALSkkgrprrgsRVRRTQKS--------THFLP 126

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 1965385973 124 RLRHLY--TAGPHglsscfLRIRADGSVDCARG-QSAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSEEd 200
Cdd:pfam00167   1 RVRRLYcrTGGFH------LQILPDGKVDGTGEdGSPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFTDE- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1965385973 201 CAFEEEIRPDGYNVYRSEKHRLP---VSLSsaRQRQLYKGRGFLPL---SHFL 247
Cdd:pfam00167  74 CVFKERLLENNYNTYASAKYSGRgwyVGLN--KKGRPKRGSKTKPGqkaAHFL 124

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 1965385973 123 IRLRHLYTAgphglSSCFLRIRADGSVDCARGQ-SAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSeEDC 201
Cdd:cd23306     3 VRWRRLFSR-----TKFFLRIDKNGKVNGTKSEnNPYSILEIRSVDVGVVAIKGVKSNYYLAMNKKGKLYGKKDYN-DDC 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1965385973 202 AFEEEIRPDGYNVYRSEKHR-----LPVSLSS-ARQRQLYKGRGFLPLSHFLPML 250
Cdd:cd23306    77 RFKERIEENGYNTYASAKWThngreMFVALSQkGRPLRGKKTRRKNTAAHFLPMV 131

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 1965385973 140 FLRIRADGSVDCARGQS-AHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGllrySE---EDCAFEEEIRPDGYNVY 215
Cdd:cd23304    13 HLRILPDGTVDGTREESdPYIILQLKAESPGVVVIKGTETGQYLAMNEDGRLYG----SQtvnDECLFLERLEENHYNTY 88

                  ....*
gi 1965385973 216 RSEKH 220
Cdd:cd23304    89 RSQKY 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965385973 140 FLRIRADGSVDCARGQS-AHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSEEdCAFEEEIRPDGYNVYRSE 218
Cdd:cd23313    13 FLRILPDGTVDGTRDRSdQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPNEE-CLFLERLEENHYNTYISK 91

                  ..
gi 1965385973 219 KH 220
Cdd:cd23313    92 KH 93

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965385973 123 IRLRHLYTagphgLSSCFLRIRADGSVD-CARGQSAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSeEDC 201
Cdd:cd23320     6 VRWRKLFS-----FTKYFLKIDKNGKVSgTKKENCPYSILEITSVEVGVVAVKAINSNYYLAMNKKGKIYGSKEFN-IDC 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1965385973 202 AFEEEIRPDGYNVYRSEK-----HRLPVSLSS-ARQRQLYKGRGFLPLSHFLPML 250
Cdd:cd23320    80 KLKERIEENGYNTYASLNwkhngRQMFVALNGkGAPKRGQKTRRKNTSAHFLPMV 134

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965385973 124 RLRHLYTAGPHGLSscfLRIRADGSVDCARGQSAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSEEdCAF 203
Cdd:cd23316     1 RLRRLYCNVGIGFH---IQVLPDGRINGVHNENRYSLLEISPVERGVVSIFGVKSGLFVAMNSKGKLYGSPFFNDE-CKF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1965385973 204 EEEIRPDGYNVYRSEKHR-LPVSLSSARQRQlyKGRGFLP---LSHFLPML 250
Cdd:cd23316    77 KEILLPNNYNAYESRKYPgMYIALSKNGKTK--KGNRVSPtmtVTHFLPRI 125

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965385973 141 LRIRADGSVDCARGQSAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSeEDCAFEEEIRPDGYNVYRSEKH 220
Cdd:cd23317    15 LQIHPDGRVNGSHEANLLSVLEIFAVSQGIVGIRGVFSNRFLAMSKKGKLHASAKFT-DDCKFRERFQENSYNTYASATH 93

                  .
gi 1965385973 221 R 221
Cdd:cd23317    94 R 94

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 1965385973 137 SSC---FLRIRaDGSVDcARG--QSAHSLLEIRAVALRT-VAIKGVHSVRYLCMGADGRMQGLLRYSEED-CAFEEEIRP 209
Cdd:cd23307     7 SRCskkFVRIT-GGRVD-ARGekGSPYAKLTIESVGFSGkVRIRGAKSGRYLCFNKKGKLVAKKNGKKDKrCVFEEELTD 84

                          90
                  ....*....|..
gi 1965385973 210 DGYNVYRSEKHR 221
Cdd:cd23307    85 GYYTRYRSVKNP 96

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965385973 141 LRIRADGSVDCARGQ-SAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSEEdCAFEEEIRPDGYNVYRSEK 219
Cdd:cd23329    17 LQLQADGTIDGTKEEdSSYTLFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSEHFTPE-CKFKESVFENYYVTYSSMI 95

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1965385973 220 HRLPVS-----LSSARQRQLYKG---RGFLPLSHFLP 248
Cdd:cd23329    96 YRQQQSgrgwyLGLNKEGEIMKGnhvKKNKPAAHFLP 132

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 1965385973 123 IRLRHLYT-AGPHglsscfLRIRADGSVDCAR-GQSAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSEEd 200
Cdd:cd23325    13 LRRRQLYCrTGFH------LEIFPNGTIQGTRkDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQE- 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1965385973 201 CAFEEEIRPDGYNVYRSE--KH-----RLPVSLSS-ARQRQLYKGRGFLPLSHFLPMlPVTPAETGDL 260
Cdd:cd23325    86 CVFREQFEENWYNTYSSNlyKHvdtgrRYYVALNKdGTPREGTRTKRHQKFTHFLPR-PVDPDKVPEL 152

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965385973 123 IRLRHLYT-AGPHglsscfLRIRADGSVDCAR-GQSAHSLLEIRAVALRTVAIKGVHSVRYLCMGADGRMQGLLRYSEEd 200
Cdd:cd23326     6 LRRRQLYCrTGFH------LEIFPNGTVHGTRqDHSRFGILEFISLAVGLVSIRGVDSGLYLGMNERGELYGSKKLTRE- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1965385973 201 CAFEEEIRPDGYNVYRSE--KH-----RLPVSLSS-ARQRQLYKGRGFLPLSHFLPMlPVTP 254
Cdd:cd23326    79 CVFREQFEENWYNTYASTlyKHadsgrQYYVALNKdGSPREGYRTKRHQKFTHFLPR-PVDP 139

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1965385973 171 VAIKGVHSVRYLCMGADGRMQGLLRYSEEDCAFEEEIRPDGYNVYRSEKHR----------LPVSLSSARQRQ 233
Cdd:cd23323    45 VRIKGAESGKYICMNKRGKLVGKPNGKSKDCIFTEIVLENNYTAFQNARHEgwfmaftrkgRPRKASKTRQNQ 117