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Conserved domains on  [gi|15055549|ref|NP_149134|]
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fibroblast growth factor 5 isoform 2 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
beta-trefoil_FGF super family cl00060
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
87-119 2.50e-17

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.


The actual alignment was detected with superfamily member cd23317:

Pssm-ID: 469595  Cd Length: 133  Bit Score: 72.23  E-value: 2.50e-17
                        10        20        30
                ....*....|....*....|....*....|...
gi 15055549  87 RTGSLYCRVGIGFHLQIYPDGKVNGSHEANMLS 119
Cdd:cd23317   1 RTGRLYCRVGIGFHLQIHPDGRVNGSHEANLLS 33
 
Name Accession Description Interval E-value
beta-trefoil_FGF5 cd23317
FGF domain, beta-trefoil fold, found in fibroblast growth factor 5 (FGF5) and similar proteins; ...
87-119 2.50e-17

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.


Pssm-ID: 467003  Cd Length: 133  Bit Score: 72.23  E-value: 2.50e-17
                        10        20        30
                ....*....|....*....|....*....|...
gi 15055549  87 RTGSLYCRVGIGFHLQIYPDGKVNGSHEANMLS 119
Cdd:cd23317   1 RTGRLYCRVGIGFHLQIHPDGRVNGSHEANLLS 33
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
87-116 3.00e-08

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.


Pssm-ID: 425498  Cd Length: 124  Bit Score: 48.31  E-value: 3.00e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 15055549    87 RTGSLYCRVGiGFHLQIYPDGKVNGSHEAN 116
Cdd:pfam00167   1 RVRRLYCRTG-GFHLQILPDGKVDGTGEDG 29
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
85-116 4.02e-07

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.


Pssm-ID: 214665  Cd Length: 126  Bit Score: 45.33  E-value: 4.02e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 15055549     85 GRRTGSLYCRVGigFHLQIYPDGKVNGSHEAN 116
Cdd:smart00442   1 TKRLRQLYCRNG--QHLQILPDGTVDGTRDES 30
 
Name Accession Description Interval E-value
beta-trefoil_FGF5 cd23317
FGF domain, beta-trefoil fold, found in fibroblast growth factor 5 (FGF5) and similar proteins; ...
87-119 2.50e-17

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.


Pssm-ID: 467003  Cd Length: 133  Bit Score: 72.23  E-value: 2.50e-17
                        10        20        30
                ....*....|....*....|....*....|...
gi 15055549  87 RTGSLYCRVGIGFHLQIYPDGKVNGSHEANMLS 119
Cdd:cd23317   1 RTGRLYCRVGIGFHLQIHPDGRVNGSHEANLLS 33
beta-trefoil_FGF3-like cd23305
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 3 (FGF3)-like family; The ...
87-119 8.59e-12

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.


Pssm-ID: 466991  Cd Length: 127  Bit Score: 57.70  E-value: 8.59e-12
                        10        20        30
                ....*....|....*....|....*....|...
gi 15055549  87 RTGSLYCRVgIGFHLQIYPDGKVNGSHEANMLS 119
Cdd:cd23305   1 RYRLLYCRV-IGFHLQILPDGSVNGTHEDTEYS 32
beta-trefoil_FGF6 cd23318
FGF domain, beta-trefoil fold, found in fibroblast growth factor 6 (FGF6) and similar proteins; ...
87-119 2.91e-10

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.


Pssm-ID: 467004  Cd Length: 125  Bit Score: 53.66  E-value: 2.91e-10
                        10        20        30
                ....*....|....*....|....*....|...
gi 15055549  87 RTGSLYCRVGIGFHLQIYPDGKVNGSHEANMLS 119
Cdd:cd23318   1 RLRRLYCNVGIGFHLQILPDGRINGVHNENQYS 33
beta-trefoil_FGF4 cd23316
FGF domain, beta-trefoil fold, found in fibroblast growth factor 4 (FGF4) and similar proteins; ...
87-119 1.49e-08

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.


Pssm-ID: 467002  Cd Length: 125  Bit Score: 49.11  E-value: 1.49e-08
                        10        20        30
                ....*....|....*....|....*....|...
gi 15055549  87 RTGSLYCRVGIGFHLQIYPDGKVNGSHEANMLS 119
Cdd:cd23316   1 RLRRLYCNVGIGFHIQVLPDGRINGVHNENRYS 33
FGF pfam00167
Fibroblast growth factor; Fibroblast growth factors are a family of proteins involved in ...
87-116 3.00e-08

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.


Pssm-ID: 425498  Cd Length: 124  Bit Score: 48.31  E-value: 3.00e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 15055549    87 RTGSLYCRVGiGFHLQIYPDGKVNGSHEAN 116
Cdd:pfam00167   1 RVRRLYCRTG-GFHLQILPDGKVDGTGEDG 29
FGF smart00442
Acidic and basic fibroblast growth factor family; Mitogens that stimulate growth or ...
85-116 4.02e-07

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.


Pssm-ID: 214665  Cd Length: 126  Bit Score: 45.33  E-value: 4.02e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 15055549     85 GRRTGSLYCRVGigFHLQIYPDGKVNGSHEAN 116
Cdd:smart00442   1 TKRLRQLYCRNG--QHLQILPDGTVDGTRDES 30
beta-trefoil_FGF cd00058
FGF domain, beta-trefoil fold, found in acidic and basic fibroblast growth factor (FGF) ...
87-116 1.02e-05

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.


Pssm-ID: 466989  Cd Length: 127  Bit Score: 41.80  E-value: 1.02e-05
                        10        20        30
                ....*....|....*....|....*....|
gi 15055549  87 RTGSLYCRVGigFHLQIYPDGKVNGSHEAN 116
Cdd:cd00058   1 RLVRLYSRTG--YFLQILPDGTVNGTKDEN 28
beta-trefoil_FGF1-like cd23304
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 1 (FGF1)-like family; The ...
91-116 5.47e-05

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.


Pssm-ID: 466990  Cd Length: 127  Bit Score: 39.73  E-value: 5.47e-05
                        10        20
                ....*....|....*....|....*.
gi 15055549  91 LYCRVGiGFHLQIYPDGKVNGSHEAN 116
Cdd:cd23304   5 LYCSNG-GYHLRILPDGTVDGTREES 29
beta-trefoil_FGF9-like cd23308
FGF domain, beta-trefoil fold, found in the fibroblast growth factor 9 (FGF9)-like family; The ...
87-114 2.49e-04

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.


Pssm-ID: 466994  Cd Length: 130  Bit Score: 38.16  E-value: 2.49e-04
                        10        20
                ....*....|....*....|....*...
gi 15055549  87 RTGSLYCRVGigFHLQIYPDGKVNGSHE 114
Cdd:cd23308   1 RRRQLYCRTG--FHLEILPNGTVQGTRQ 26
beta-trefoil_FGF20 cd23327
FGF domain, beta-trefoil fold, found in fibroblast growth factor 20 (FGF20) and similar ...
87-114 7.55e-04

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.


Pssm-ID: 467013  Cd Length: 153  Bit Score: 37.25  E-value: 7.55e-04
                        10        20
                ....*....|....*....|....*...
gi 15055549  87 RTGSLYCRVGigFHLQIYPDGKVNGSHE 114
Cdd:cd23327  10 RRRQLYCRTG--FHLEILPDGSVQGTRK 35
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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