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 10190674  25 YPNASPLLGSSWG---GLIHLYTATARNSYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGN 101
Cdd:cd23333   1 FPNASPLLGPNWGnprRLIHLYTSTDRNSYHLQINPDGHVDGTPHQTIYSALLIKSEDAGRVVITGVKSNRYLCMDFRGN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10190674 102 IFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPGMNPPPYSQFLSRRNEIPLIHF 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 10190674  25 YPNASPLLGSSWG---GLIHLYTATARNSYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGN 101
Cdd:cd23333   1 FPNASPLLGPNWGnprRLIHLYTSTDRNSYHLQINPDGHVDGTPHQTIYSALLIKSEDAGRVVITGVKSNRYLCMDFRGN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10190674 102 IFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPGMNPPPYSQFLSRRNEIPLIHF 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 10190674    42 LYtatARNS-YHLQIHKNGHVDGAPHQT-IYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDpENCRFQHQT 119
Cdd:pfam00167   5 LY---CRTGgFHLQILPDGKVDGTGEDGsPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFT-DECVFKERL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 10190674   120 LENGYDVYHSPQYH---FLVSL---GRAKRAF 145
Cdd:pfam00167  81 LENNYNTYASAKYSgrgWYVGLnkkGRPKRGS 112

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 10190674  25 YPNASPLLGSSWG---GLIHLYTATARNSYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGN 101
Cdd:cd23333   1 FPNASPLLGPNWGnprRLIHLYTSTDRNSYHLQINPDGHVDGTPHQTIYSALLIKSEDAGRVVITGVKSNRYLCMDFRGN 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10190674 102 IFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPGMNPPPYSQFLSRRNEIPLIHF 169
Cdd:cd23333  81 IFGSHYFNKEDCLFQHETLENGYDVYHSPKYNILVSLGGAKQAFIPGMNLPPYSQFLSRRNEVPLIRF 148

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10190674  39 LIHLYTA--TARNSYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPENCRFQ 116
Cdd:cd23331   3 LRHLYTArpHGLSSCFLRIRADGVVDGSRGQSAHSLLEIKAVALGTVAIKGVASSRYLCMEADGKLYGSLSYSEEDCSFE 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 10190674 117 HQTLENGYDVYHSPQYHFLVSLGRAK-RAFLPGMNPPPYSQFL 158
Cdd:cd23331  83 EEILPDGYNVYRSKKHGLPVSLSSAKqRQQYKDKGFLPLSQFL 125

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 10190674  39 LIHLYTataRNSYHLQIHKNGHVDGAPHQ-TIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPEnCRFQH 117
Cdd:cd00058   2 LVRLYS---RTGYFLQILPDGTVNGTKDEnSPYAILELQSVGTGLVRIKGVKTGRYLAMDKNGKLYGTKKPTED-CVFKE 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 10190674 118 QTLENGYDVYHSPQY-----HFLVSL---GRAKRAF--LPGMNPppySQFLSR 160
Cdd:cd00058  78 TLEENGYNTYSSYKYyhtrkGWYLAIkknGKPKRGKktKPGQKS---TQFLPL 127

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 10190674  51 YHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPEnCRFQHQTLENGYDVYHSP 130
Cdd:cd23305  12 FHLQILPDGSVNGTHEDTEYSWLEIFAVEVGVVGIKGVKSGLYLCMNKKGKLYGSKEFTDE-CKFKERLEENHYNTYSSA 90

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 10190674 131 QYH-----FLVSL---GRAKRAFLPGmNPPPYSQFLSR 160
Cdd:cd23305  91 LYPrrkrgWYVALskkGRPRRGSRVR-RTQKSTHFLPR 127

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 10190674  42 LYTATarnSYHLQIHKNGHVDGA-PHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPEnCRFQHQTL 120
Cdd:cd23315   5 LYCAT---KYHLQIHPNGKIDGTlEKNSVFSILEITAVDVGVVAIKGLFSGRYLAMNKRGRLYASEVYNAE-CEFVERIH 80

                        90       100
                ....*....|....*....|...
gi 10190674 121 ENGYDVYHSPQYHFLVSLGRAKR 143
Cdd:cd23315  81 ELGYNTYASRLYRTVPSGAGTKR 103

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 10190674  48 RNSYHLQIHKNGHVDGA--PHQTiYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDpENCRFQHQTLENGYD 125
Cdd:cd23306  11 RTKFFLRIDKNGKVNGTksENNP-YSILEIRSVDVGVVAIKGVKSNYYLAMNKKGKLYGKKDYN-DDCRFKERIEENGYN 88

                        90       100
                ....*....|....*....|...
gi 10190674 126 VYHSPQY-----HFLVSLGRAKR 143
Cdd:cd23306  89 TYASAKWthngrEMFVALSQKGR 111

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 10190674  51 YHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPEnCRFQHQTLENGYDVYHSP 130
Cdd:cd23317  13 FHLQIHPDGRVNGSHEANLLSVLEIFAVSQGIVGIRGVFSNRFLAMSKKGKLHASAKFTDD-CKFRERFQENSYNTYASA 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 10190674 131 QY-------HFLVSL---GRAKRAFLPGMNPPPYS-QFLSR 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 10190674  51 YHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPEnCRFQHQTLENGYDVYHSP 130
Cdd:cd23316  13 FHIQVLPDGRINGVHNENRYSLLEISPVERGVVSIFGVKSGLFVAMNSKGKLYGSPFFNDE-CKFKEILLPNNYNAYESR 91

                        90
                ....*....|....
gi 10190674 131 QY-HFLVSLGRAKR 143
Cdd:cd23316  92 KYpGMYIALSKNGK 105

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 10190674  48 RNSYHLQIHKNGHVDGA--PHqTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDpENCRFQHQTLENGYD 125
Cdd:cd23308   8 RTGFHLEILPNGTVQGTrqDH-SRFGILEFISVAVGLVSIRGVDSGLYLGMNEKGELYGSEKLT-RECVFREQFEENWYN 85

                        90       100
                ....*....|....*....|....*.
gi 10190674 126 VYHSPQYH-------FLVSLGRAKRA 144
Cdd:cd23308  86 TYSSNLYKhadtgrrYYVALNKDGTP 111

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 10190674  51 YHLQIHKNGHVDGAPHQT-IYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPEnCRFQHQTLENGYDVYHS 129
Cdd:cd23314  12 FFLRIHPDGRVDGVREKSdPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKSVTDE-CFFFERLESNNYNTYRS 90

                ...
gi 10190674 130 PQY 132
Cdd:cd23314  91 RKY 93

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 10190674  37 GGLIHLYTATARNSYHLQIHKNGHVDG-APHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDpENCRF 115
Cdd:cd23319   5 GGDVRVRRLFCRTQWYLRIDKRGKVKGtQEMNNSYNILEIRTVAVGIVAIKGVESEYFLAMNKEGKLYGKKVCN-EDCNF 83

                        90
                ....*....|....*..
gi 10190674 116 QHQTLENGYDVYHSPQY 132
Cdd:cd23319  84 KELIEENHYNTYASAKW 100

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 10190674  51 YHLQIHKNGHVDGAPHQT-IYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDpENCRFQHQTLENGYDVYHS 129
Cdd:cd23313  12 HFLRILPDGTVDGTRDRSdQHIQLQLSAESVGEVYIKSTETGQYLAMDTDGLLYGSQTPN-EECLFLERLEENHYNTYIS 90

                        90       100
                ....*....|....*....|
gi 10190674 130 PQY---HFLVSL---GRAKR 143
Cdd:cd23313  91 KKHaekNWFVGLkknGSCKR 110

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 10190674  48 RNSYHLQIHKNGHVDGAPHQTIYSALM-IRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPEnCRFQHQTLENGYDV 126
Cdd:cd23330  14 RQGYYLQMHPDGSLDGTKDDSSNSTLFnLIPVGLRVVAIQGVKTGLYIAMNGEGYLYTSELFTPE-CKFKESVFENYYVI 92

                        90       100
                ....*....|....*....|....
gi 10190674 127 YHSpqyhFLVSLGRAKRAFLPGMN 150
Cdd:cd23330  93 YSS----MLYRQQESGRAWFLGLN 112

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 10190674  38 GLIHLYTATARNSYHLQIHKNGHVDGA-PHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPEnCRFQ 116
Cdd:cd23325  11 GILRRRQLYCRTGFHLEIFPNGTIQGTrKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQE-CVFR 89

                        90       100
                ....*....|....*....|....
gi 10190674 117 HQTLENGYDVYHSPQYHFlVSLGR 140
Cdd:cd23325  90 EQFEENWYNTYSSNLYKH-VDTGR 112

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 10190674  52 HLQIHkNGHVDG-APHQTIYSALMIRSE-DAGFVVITGVMSRRYLCMDFRGNIFG-SHYFDPENCRFQHQTLENGYDVYH 128
Cdd:cd23307  13 FVRIT-GGRVDArGEKGSPYAKLTIESVgFSGKVRIRGAKSGRYLCFNKKGKLVAkKNGKKDKRCVFEEELTDGYYTRYR 91

                ....
gi 10190674 129 SPQY 132
Cdd:cd23307  92 SVKN 95

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 10190674  39 LIHLYTATARNS-YHLQIHKNGHV-----DGAPHqtiySALMIRSEDAGFVV-ITGVMSRRYLCMDFRGNIFGSHYFDPE 111
Cdd:cd23322  19 LIRTYQLYSRTSgKHVQVLANKKInamaeDGDPH----AKLIVETDTFGSRVrIKGAETGYYICMNKKGKLIGKSNGKGK 94

                        90       100
                ....*....|....*....|.
gi 10190674 112 NCRFQHQTLENGYDVYHSPQY 132
Cdd:cd23322  95 DCVFTEIVLENNYTALQNAKY 115