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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109085696  56 ELAHLHGILRRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTS 135
Cdd:cd23327    1 DLAHLQGILRRRQLYCRTGFHLEILPDGSVQGTRKDHSRFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109085696 136 ECIFREQFEENWYNTYSSNTYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRPVDPERVPELYKDLL 208
Cdd:cd23327   81 ECIFREQFEENWYNTYSSNLYKHGDTGRRYFVALNKDGTPRDGTRSKRHQKFTHFLPRPVDPEKVPELYKDLL 153

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109085696  56 ELAHLHGILRRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTS 135
Cdd:cd23327    1 DLAHLQGILRRRQLYCRTGFHLEILPDGSVQGTRKDHSRFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109085696 136 ECIFREQFEENWYNTYSSNTYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRPVDPERVPELYKDLL 208
Cdd:cd23327   81 ECIFREQFEENWYNTYSSNLYKHGDTGRRYFVALNKDGTPRDGTRSKRHQKFTHFLPRPVDPEKVPELYKDLL 153

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 109085696    63 ILRRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQ 142
Cdd:smart00442   1 TKRLRQLYCRNGQHLQILPDGTVDGTRDESSSFTILEIIAVAVGVVAIKGVASCRYLCMNKCGKLYGSKNFTEDCVFREE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 109085696   143 FEENWYNTYSSNTYKHgdtgrRYFVALNKDGTPRDGARSKRHQKFTHFLPR 193
Cdd:smart00442  81 MEENGYNTYASAKYRK-----RWYVALNKKGRPRRGQKTKPLQKASHFLPR 126

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109085696  56 ELAHLHGILRRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTS 135
Cdd:cd23327    1 DLAHLQGILRRRQLYCRTGFHLEILPDGSVQGTRKDHSRFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109085696 136 ECIFREQFEENWYNTYSSNTYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRPVDPERVPELYKDLL 208
Cdd:cd23327   81 ECIFREQFEENWYNTYSSNLYKHGDTGRRYFVALNKDGTPRDGTRSKRHQKFTHFLPRPVDPEKVPELYKDLL 153

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 109085696  65 RRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQFE 144
Cdd:cd23308    1 RRRQLYCRTGFHLEILPNGTVQGTRQDHSRFGILEFISVAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTRECVFREQFE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 109085696 145 ENWYNTYSSNTYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRP 194
Cdd:cd23308   81 ENWYNTYSSNLYKHADTGRRYYVALNKDGTPREGCRTKRHQKFTHFLPRP 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 109085696   65 RRRQLYCRT-GFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQF 143
Cdd:pfam00167   1 RVRRLYCRTgGFHLQILPDGKVDGTGEDGSPYSILEIESVSVGVVRIKGVESGLYLAMNKKGRLYGSKNFTDECVFKERL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 109085696  144 EENWYNTYSSNTYKhgdtGRRYFVALNKDGTPRDGARSKRHQKFTHFL 191
Cdd:pfam00167  81 LENNYNTYASAKYS----GRGWYVGLNKKGRPKRGSKTKPGQKAAHFL 124

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 109085696  65 RRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQFE 144
Cdd:cd00058    1 RLVRLYSRTGYFLQILPDGTVNGTKDENSPYAILELQSVGTGLVRIKGVKTGRYLAMDKNGKLYGTKKPTEDCVFKETLE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 109085696 145 ENWYNTYSSntYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPR 193
Cdd:cd00058   81 ENGYNTYSS--YKYYHTRKGWYLAIKKNGKPKRGKKTKPGQKSTQFLPL 127

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 109085696  62 GILRRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFRE 141
Cdd:cd23306    1 GDVRWRRLFSRTKFFLRIDKNGKVNGTKSENNPYSILEIRSVDVGVVAIKGVKSNYYLAMNKKGKLYGKKDYNDDCRFKE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 109085696 142 QFEENWYNTYSSNTYKHgdTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRP 194
Cdd:cd23306   81 RIEENGYNTYASAKWTH--NGREMFVALSQKGRPLRGKKTRRKNTAAHFLPMV 131

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 109085696  62 GILRRrqLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFRE 141
Cdd:cd23309    1 GIVTR--LYSRQGYYLQMQPDGTIDGTKDENSSYTLFNLIPVGLRVVAIQGVKTGLYIAMNSEGYLYTSEHFTPECKFKE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109085696 142 QFEENWYNTYSSNTYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPR 193
Cdd:cd23309   79 SVFENYYVIYSSMLYRQQQSGRAWYLGLNKEGQIMKGNRVKKTKPAAHFLPK 130

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 109085696  65 RRRQLYCRTG--FHLQILPDGSVQGTrQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQ 142
Cdd:cd23317    1 RTGRLYCRVGigFHLQIHPDGRVNGS-HEANLLSVLEIFAVSQGIVGIRGVFSNRFLAMSKKGKLHASAKFTDDCKFRER 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 109085696 143 FEENWYNTYSSNTYKHGDTGRRYFVALNKDGTPRDGA--RSKRHQKFTHFLPR 193
Cdd:cd23317   80 FQENSYNTYASATHRNHRTGREWYVALNKRGKAKRGCspRVKPQHISTHFLPR 132

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 109085696  62 GILRRRQLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFRE 141
Cdd:cd23319    6 GDVRVRRLFCRTQWYLRIDKRGKVKGTQEMNNSYNILEIRTVAVGIVAIKGVESEYFLAMNKEGKLYGKKVCNEDCNFKE 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109085696 142 QFEENWYNTYSSNtyKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLP 192
Cdd:cd23319   86 LIEENHYNTYASA--KWTHKGKEMFVALNQKGKPMKGKKTKKEHKTSHFLP 134

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 109085696  59 HLHGILRRrqLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECI 138
Cdd:cd23328    2 QLKGIVTR--LFSQQGYFLQMHPDGTIDGTKDENSDYTLFNLIPVGLRVVAIQGVKAGLYVAMNGEGYLYSSDVFTPECK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 109085696 139 FREQFEENWYNTYSSNTYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRPVD 196
Cdd:cd23328   80 FKESVFENYYVIYSSTLYRQQESGRAWFLGLNKEGQIMKGNRVKKTKPSSHFVPKPIE 137

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 109085696  59 HLHGILRRrqLYCRTGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECI 138
Cdd:cd23330    3 QLKGIVTR--LYCRQGYYLQMHPDGSLDGTKDDSSNSTLFNLIPVGLRVVAIQGVKTGLYIAMNGEGYLYTSELFTPECK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 109085696 139 FREQFEENWYNTYSSNTYKHGDTGRRYFVALNKDGTPRDGARSKRHQKFTHFLPRPVD 196
Cdd:cd23330   81 FKESVFENYYVIYSSMLYRQQESGRAWFLGLNKEGQAMKGNRVKKTKPAAHFLPKPLE 138

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 109085696  65 RRRQLYCRTG--FHLQILPDGSVQGTRQDHSlFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQ 142
Cdd:cd23316    1 RLRRLYCNVGigFHIQVLPDGRINGVHNENR-YSLLEISPVERGVVSIFGVKSGLFVAMNSKGKLYGSPFFNDECKFKEI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 109085696 143 FEENWYNTYSSNTYKHgdtgrrYFVALNKDGTPRDGARSKRHQKFTHFLPR 193
Cdd:cd23316   80 LLPNNYNAYESRKYPG------MYIALSKNGKTKKGNRVSPTMTVTHFLPR 124

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 109085696  67 RQLYCRTG-FHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSECIFREQFEE 145
Cdd:cd23314    3 KRLYCKNGgFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKSVTDECFFFERLES 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 109085696 146 NWYNTYSSNTYKHgdtgrrYFVALNKDGTPRDGARSKRHQKFTHFLP 192
Cdd:cd23314   83 NNYNTYRSRKYTS------WYVALKRTGQYKLGSKTGPGQKAILFLP 123

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 109085696  65 RRRQLY-----CRTGFHLQILPDGSVQGTRQdHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSE-CI 138
Cdd:cd23331    2 RLRHLYtarphGLSSCFLRIRADGVVDGSRG-QSAHSLLEIKAVALGTVAIKGVASSRYLCMEADGKLYGSLSYSEEdCS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 109085696 139 FREQFEENWYNTYSSNtyKHGdtgrrYFVALNKdGTPRDGARSKRHQKFTHFLP 192
Cdd:cd23331   81 FEEEILPDGYNVYRSK--KHG-----LPVSLSS-AKQRQQYKDKGFLPLSQFLP 126

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 109085696  65 RRRQLYCR-TGFHLQILPdGSVQGTRQDHSLFGILEFISVA-VGLVSIRGVDSGLYLGMNDKGELYGSEKLTS--ECIFR 140
Cdd:cd23307    1 RSVRLYSRcSKKFVRITG-GRVDARGEKGSPYAKLTIESVGfSGKVRIRGAKSGRYLCFNKKGKLVAKKNGKKdkRCVFE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 109085696 141 EQFEENWYNTYSSNTYKhgdtgrRYFVALNKDGTPRDGARSKRH-QKFTHFLPR 193
Cdd:cd23307   80 EELTDGYYTRYRSVKNP------SWYLGFNRNGRPLKGSKTRKKkQKCFHFLKR 127

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 109085696  64 LRRRQLYC---RTGFHLQILPDGSVQGTRqDHSLFGILEFISVAVGLVSIRGVDSGLYLGMNDKGELYGSEKLTSE-CIF 139
Cdd:cd23332    2 VRLRHLYTadeQTQLHLEIREDGTVGGAA-DQSPYSLLELKAVKPGVVQILGKKTLRFLCMDPDGRLYGSLHYSPEaCSF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 109085696 140 REQFEENWYNTYSSNtyKHGDTgrryfVALNKDGTPRDGARSKRhqKFTHFLPRP 194
Cdd:cd23332   81 REVVLEDGYNLYQSE--AHGLP-----LTLSPNRAPHRDGGAPP--PLAHFLPLV 126

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109085696  65 RRRQLYCRT-GFHLQILPDG-SVQGTRQDHSLFGILEFISVAvGLVSIRGVDSGLYLGMNDKGELYGSEKLTS-ECIFRE 141
Cdd:cd23324    1 RLYQLYSRTsGKHIQVLGRRiSARGEDGDKYAQLLVETDTFG-SQVRIKGKETDFYLCMNRKGKLVGKPDGTSkECVFIE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 109085696 142 QFEENWYNTYSSNTYkhgdTGrrYFVALNKDGTPRDGARSKRHQKFTHFLPR 193
Cdd:cd23324   80 KVLENNYTALMSAKY----SG--WYVGFTKKGRPRKGPKTRENQQDVHFMKR 125

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 109085696  68 QLYCR-TGFHLQILPDGSVQGTRQDHSLFGILEFISVAVGLVSIRGV-DSGLYLGMNDkGELYGSEKLTSECIFREQFEE 145
Cdd:cd23312    7 QLYSKlTGQALRVKPDGSVDATGDKKDKFAYFRVHKVKGNIRIFQSVaNPGYFLAIDD-GKVDGNGKGGEDCEFRVRVQP 85

                         90       100       110
                 ....*....|....*....|....*....|....
gi 109085696 146 NWYNTYSSNTYkhgdtgRRYFVALNKDGTPRDGA 179
Cdd:cd23312   86 DRSVTLESVKN------PGQFVGFNPDGKPRDPR 113