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 12083589  25 YPDTSPLLGSNWGS---LTHLYTATARTSYHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGN 101
Cdd:cd23333   1 FPNASPLLGPNWGNprrLIHLYTSTDRNSYHLQINPDGHVDGTPHQTIYSALLIKSEDAGRVVITGVKSNRYLCMDFRGN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12083589 102 IFGSLHFSPENCKFRQWTLENGYDVYLSQKHHYLVSLGRAKRIFQPGTNPPPFSQFLARRNEVPLLHF 169
Cdd:cd23333  81 IFGSHYFNKEDCLFQHETLENGYDVYHSPKYNILVSLGGAKQAFIPGMNLPPYSQFLSRRNEVPLIRF 148

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 12083589  25 YPDTSPLLGSNWGS---LTHLYTATARTSYHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGN 101
Cdd:cd23333   1 FPNASPLLGPNWGNprrLIHLYTSTDRNSYHLQINPDGHVDGTPHQTIYSALLIKSEDAGRVVITGVKSNRYLCMDFRGN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12083589 102 IFGSLHFSPENCKFRQWTLENGYDVYLSQKHHYLVSLGRAKRIFQPGTNPPPFSQFLARRNEVPLLHF 169
Cdd:cd23333  81 IFGSHYFNKEDCLFQHETLENGYDVYHSPKYNILVSLGGAKQAFIPGMNLPPYSQFLSRRNEVPLIRF 148

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 12083589    42 LYTATarTSYHLQIHRDGHVDGTPHQT-IYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSpENCKFRQWTL 120
Cdd:pfam00167   5 LYCRT--GGFHLQILPDGKVDGTGEDGsPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFT-DECVFKERLL 81

                          90       100
                  ....*....|....*....|....*....
gi 12083589   121 ENGYDVYLSQKHH---YLVSL---GRAKR 143
Cdd:pfam00167  82 ENNYNTYASAKYSgrgWYVGLnkkGRPKR 110

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 12083589  25 YPDTSPLLGSNWGS---LTHLYTATARTSYHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGN 101
Cdd:cd23333   1 FPNASPLLGPNWGNprrLIHLYTSTDRNSYHLQINPDGHVDGTPHQTIYSALLIKSEDAGRVVITGVKSNRYLCMDFRGN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12083589 102 IFGSLHFSPENCKFRQWTLENGYDVYLSQKHHYLVSLGRAKRIFQPGTNPPPFSQFLARRNEVPLLHF 169
Cdd:cd23333  81 IFGSHYFNKEDCLFQHETLENGYDVYHSPKYNILVSLGGAKQAFIPGMNLPPYSQFLSRRNEVPLIRF 148

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 12083589  39 LTHLYTATARTSYHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPENCKFRQW 118
Cdd:cd23332   4 LRHLYTADEQTQLHLEIREDGTVGGAADQSPYSLLELKAVKPGVVQILGKKTLRFLCMDPDGRLYGSLHYSPEACSFREV 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 12083589 119 TLENGYDVYLSQKHHYLVSLGRAKRIFQPGTNPPPFSQFL 158
Cdd:cd23332  84 VLEDGYNLYQSEAHGLPLTLSPNRAPHRDGGAPPPLAHFL 123

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 12083589  48 RTSYHLQIHRDGHVDGTPHQ-TIYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPEnCKFRQWTLENGYDV 126
Cdd:cd00058   8 RTGYFLQILPDGTVNGTKDEnSPYAILELQSVGTGLVRIKGVKTGRYLAMDKNGKLYGTKKPTED-CVFKETLEENGYNT 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 12083589 127 YLSQKH-----HYLVSLGRAKRIfQPGTNPPPF---SQFLAR 160
Cdd:cd00058  87 YSSYKYyhtrkGWYLAIKKNGKP-KRGKKTKPGqksTQFLPL 127

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 12083589    42 LYTATarTSYHLQIHRDGHVDGTPHQT-IYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSpENCKFRQWTL 120
Cdd:pfam00167   5 LYCRT--GGFHLQILPDGKVDGTGEDGsPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFT-DECVFKERLL 81

                          90       100
                  ....*....|....*....|....*....
gi 12083589   121 ENGYDVYLSQKHH---YLVSL---GRAKR 143
Cdd:pfam00167  82 ENNYNTYASAKYSgrgWYVGLnkkGRPKR 110

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 12083589  51 YHLQIHRDGHVDGTPHQT-IYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPEnCKFRQWTLENGYDVYLS 129
Cdd:cd23304  12 YHLRILPDGTVDGTREESdPYIILQLKAESPGVVVIKGTETGQYLAMNEDGRLYGSQTVNDE-CLFLERLEENHYNTYRS 90

                        90       100
                ....*....|....*....|
gi 12083589 130 QKH---HYLVSL---GRAKR 143
Cdd:cd23304  91 QKYaekNWYVGLkknGRCKL 110

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 12083589  51 YHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPEnCKFRQWTLENGYDVYLSQ 130
Cdd:cd23317  13 FHLQIHPDGRVNGSHEANLLSVLEIFAVSQGIVGIRGVFSNRFLAMSKKGKLHASAKFTDD-CKFRERFQENSYNTYASA 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 12083589 131 KH-------HYLVSL---GRAKRIFQPGTNPPPFS-QFLAR 160
Cdd:cd23317  92 THrnhrtgrEWYVALnkrGKAKRGCSPRVKPQHIStHFLPR 132

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 12083589  51 YHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPEnCKFRQWTLENGYDVYLSQ 130
Cdd:cd23316  13 FHIQVLPDGRINGVHNENRYSLLEISPVERGVVSIFGVKSGLFVAMNSKGKLYGSPFFNDE-CKFKEILLPNNYNAYESR 91

                        90
                ....*....|....
gi 12083589 131 KHHYL-VSLGRAKR 143
Cdd:cd23316  92 KYPGMyIALSKNGK 105

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 12083589  42 LYTATartSYHLQIHRDGHVDGTPHQTIYSALM-ITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPeNCKFRQWTL 120
Cdd:cd23321  11 LYSAT---KFFLRIDKGGRVEGTRWKNCPDSILeIRSVSVGVVAIKSVSTGFYLAMNKKGKLYGSKLYSP-NCKFKERIE 86

                        90
                ....*....|.
gi 12083589 121 ENGYDVYLSQK 131
Cdd:cd23321  87 ENGYNTYASLR 97

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 12083589  48 RTSYHLQIHRDGHVDGT--PHqTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSpENCKFRQWTLENGYD 125
Cdd:cd23308   8 RTGFHLEILPNGTVQGTrqDH-SRFGILEFISVAVGLVSIRGVDSGLYLGMNEKGELYGSEKLT-RECVFREQFEENWYN 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 12083589 126 VYLS--QKHH-----YLVSLGRAKRIFQpGTNPPP---FSQFLAR 160
Cdd:cd23308  86 TYSSnlYKHAdtgrrYYVALNKDGTPRE-GCRTKRhqkFTHFLPR 129

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12083589  51 YHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPEnCKFRQWTLENGYDVYLSQ 130
Cdd:cd23318  13 FHLQILPDGRINGVHNENQYSLLEISTVERGVVSLYGVKSGLFVAMNSKGRLYGTPNFQDE-CKFKETLLPNNYNAYESS 91

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 12083589 131 KHH----YLVSLGRAKRifqpGTNPPP---FSQFLAR 160
Cdd:cd23318  92 LYKgayiALSKHGRVKR----GNKVSPamtVTHFLPR 124

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 12083589  51 YHLQIHRDGHVDGTP-HQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPEnCKFRQWTLENGYDVYLS 129
Cdd:cd23311  13 RYLQVNADGTVNGTTdSNSNDTVWQRIAVNNGKILIRSVATCMYLCINECGYVYSSKVPNKD-CLFNESYEENNYNYYYK 91

                        90       100
                ....*....|....*....|....*..
gi 12083589 130 Q--KHHYLVSL---GRAKRIFQPGTNP 151
Cdd:cd23311  92 KfnRRRAYLALnkeGKTRRVVLPKSEP 118

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12083589  51 YHLQIHRDGHVDGTPHQT-IYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGsLHFSPENCKFRQWTLENGYDVYLS 129
Cdd:cd23314  12 FFLRIHPDGRVDGVREKSdPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLA-SKSVTDECFFFERLESNNYNTYRS 90

                        90       100
                ....*....|....*....|....*
gi 12083589 130 QKH-HYLVSLGRAKRiFQPGTNPPP 153
Cdd:cd23314  91 RKYtSWYVALKRTGQ-YKLGSKTGP 114

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12083589  37 GSLTHLYtatARTSYHLQIHRDGHVDGTPHQTIYSALM-ITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPEnCKF 115
Cdd:cd23330   6 GIVTRLY---CRQGYYLQMHPDGSLDGTKDDSSNSTLFnLIPVGLRVVAIQGVKTGLYIAMNGEGYLYTSELFTPE-CKF 81

                        90       100
                ....*....|....*....|....*.
gi 12083589 116 RQWTLENGYDVYLSQKHHYLVSlGRA 141
Cdd:cd23330  82 KESVFENYYVIYSSMLYRQQES-GRA 106

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 12083589  52 HLQIHRdGHVDGT-----PHQTIYsalMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFS-PENCKFRQWTLENGYD 125
Cdd:cd23307  13 FVRITG-GRVDARgekgsPYAKLT---IESVGFSGKVRIRGAKSGRYLCFNKKGKLVAKKNGKkDKRCVFEEELTDGYYT 88

                ....*..
gi 12083589 126 VYLSQKH 132
Cdd:cd23307  89 RYRSVKN 95

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 12083589  48 RTSYHLQIHRDGHVDGT-PHQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPEnCKFRQWTLENGYDV 126
Cdd:cd23325  21 RTGFHLEIFPNGTIQGTrKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQE-CVFREQFEENWYNT 99

                        90
                ....*....|....
gi 12083589 127 YLSQKHHYlVSLGR 140
Cdd:cd23325 100 YSSNLYKH-VDTGR 112

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 12083589  39 LTHLYTATARTS-YHLQIHRDGHV-----DGTPHqtiySALMITSEDAGSVV-ITGAMTRRFLCMDLHGNIFGSLHFSPE 111
Cdd:cd23322  19 LIRTYQLYSRTSgKHVQVLANKKInamaeDGDPH----AKLIVETDTFGSRVrIKGAETGYYICMNKKGKLIGKSNGKGK 94

                        90       100
                ....*....|....*....|.
gi 12083589 112 NCKFRQWTLENGYDVYLSQKH 132
Cdd:cd23322  95 DCVFTEIVLENNYTALQNAKY 115