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Q7M303 (FGF1_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibroblast growth factor 1

Short name=FGF-1
Alternative name(s):
Acidic fibroblast growth factor
Short name=aFGF
Heparin-binding growth factor 1
Short name=HBGF-1
Gene names
Name:FGF1
OrganismOvis aries (Sheep) [Reference proteome]
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as potent mitogen in vitro By similarity.

Subunit structure

Monomer. Homodimer. 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. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP1. Part of a Cu2+-dependent multiprotein aggregate containing FGF1, S100A13 and SYT1. Interacts with SYT1. Interacts with S100A13 By similarity. Interacts with LRRC59 By similarity. Interacts with CSNKA, CSNKB and FIBP By similarity. While binding with LRRC59, CSNKA and FIBP seem mutually exclusive, CSNKB and FIBP may cooperatively interact with FGF1 By similarity.

Subcellular location

Secreted. Cytoplasm By similarity. Cytoplasmcell cortex By similarity. Cytoplasmcytosol By similarity. Nucleus By similarity. Note: Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu2+ ions and S100A13. Secreted in a complex with SYT1. Binding of exogenous FGF1 to FGFR facilitates endocytosis followed by translocation of FGF1 across endosomal membrane into the cytosol. Nuclear import from the cytosol requires the classical nuclear import machinery, involving proteins KPNA1 and KPNB1, as well as LRRC59 By similarity.

Post-translational modification

In the nucleus, phosphorylated by PKC/PRKCD By similarity.

Sequence similarities

Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
   Cellular componentCytoplasm
Nucleus
Secreted
   LigandHeparin-binding
   Molecular functionDevelopmental protein
Growth factor
Mitogen
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

branch elongation involved in ureteric bud branching

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to heat

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

lung development

Inferred from electronic annotation. Source: Ensembl

mesonephric epithelium development

Inferred from sequence or structural similarity. Source: UniProtKB

organ induction

Inferred from electronic annotation. Source: Ensembl

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell division

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cholesterol biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionS100 protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

growth factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

heparin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Propeptide2 – 1514 By similarity
PRO_0000008918
Chain16 – 155140Fibroblast growth factor 1
PRO_0000008919

Regions

Region127 – 14317Heparin-binding By similarity

Sites

Binding site331Heparin By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7M303 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: FE7CDEC3D35008EF

FASTA15517,557
        10         20         30         40         50         60 
MAEGETTTFR ALTEKFNLPL GNYKKPKLLY CSNGGYFLRI LPDGRVDGTK DRSDQHIQLQ 

        70         80         90        100        110        120 
LYAESIGEVY IKSTETGQFL AMDTNGLLYG SQTPSEECLF LERLEENHYN TYISKKHAEK 

       130        140        150 
NWFIGLKKNG SSKLGPRTHF GQKAILFLPL PVSSD 

« Hide

References

[1]"Primary structure of ovine fibroblast growth factor-1 deduced by protein and cDNA analysis."
Grieb T.W., Ring M., Brown E., Palmer C., Belle N., Donjerkovic D., Chang H., Yun J., Subramanian R., Forozan F., Guo Y., Vertes A., Winkles J.A., Burgess W.H.
Biochem. Biophys. Res. Commun. 246:182-191(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

PIRJW0055.
RefSeqXP_004008958.1. XM_004008909.1.
XP_004008959.1. XM_004008910.1.

3D structure databases

ProteinModelPortalQ7M303.
SMRQ7M303. Positions 5-155.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOART00000001988; ENSOARP00000001941; ENSOARG00000001851.
GeneID101109353.

Organism-specific databases

CTD2246.

Phylogenomic databases

GeneTreeENSGT00730000110923.
HOVERGENHBG007580.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR028210. FGF1.
IPR002209. Fibroblast_GF_fam.
IPR028142. IL-1_fam/FGF_fam.
[Graphical view]
PANTHERPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF65. PTHR11486:SF65. 1 hit.
PfamPF00167. FGF. 1 hit.
[Graphical view]
PRINTSPR00263. HBGFFGF.
PR00262. IL1HBGF.
SMARTSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFGF1_SHEEP
AccessionPrimary (citable) accession number: Q7M303
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 15, 2003
Last modified: July 9, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families