Heparin-binding growth factor 1 precursor

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P03968 (FGF1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 115. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Heparin-binding growth factor 1
Short name=HBGF-1

Alternative name(s):
Acidic eye-derived growth factor II
Short name=EDGF II
Acidic fibroblast growth factor
Short name=aFGF
Endothelial cell growth factor beta and alpha chains
Prostatropin

Gene names

Name:	FGF1
Synonyms:	AFGF, FGF-1, FGFA, HBGF-1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	155 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. Ref.11 Ref.12
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 S100A13. Interacts with FGFBP1 By similarity. Interacts with SYT1. Ref.11
Subcellular location	Secreted. Cytoplasm By similarity. Cytoplasm › cell cortex 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. Ref.11 Ref.12
Sequence similarities	Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation
Cellular component	Cytoplasm Secreted
Ligand	Heparin-binding
Molecular function	Developmental protein Growth factor Mitogen
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW 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 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
Cellular component	cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.4 Ref.5

Chain

2 – 155

154

Endothelial cell growth factor beta

PRO_0000008904

Chain

16 – 155

140

Heparin-binding growth factor 1

PRO_0000008905

Chain

22 – 155

134

Endothelial cell growth factor alpha

PRO_0000008906

Regions

Region

24 – 28

Heparin-binding Potential

Region

113 – 116

Heparin-binding Potential

Amino acid modifications

Modified residue

N-acetylalanine Ref.4

Secondary structure

155

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P03968 [UniParc].

Last modified July 1, 1989. Version 2.
Checksum: F636641F189F9BFD
Show »

FASTA

155

17,493

        10         20         30         40         50         60 
MAEGETTTFT ALTEKFNLPL GNYKKPKLLY CSNGGYFLRI LPDGTVDGTK DRSDQHIQLQ 

        70         80         90        100        110        120 
LCAESIGEVY IKSTETGQFL AMDTDGLLYG SQTPNEECLF LERLEENHYN TYISKKHAEK 

       130        140        150 
HWFVGLKKNG RSKLGPRTHF GQKAILFLPL PVSSD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of bovine acidic fibroblast growth factor cDNA." Halley C., Courtois Y., Laurent M. Nucleic Acids Res. 16:10913-10913(1988) [PubMed: 3205724] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[2]	"Characterization of a bovine acidic FGF cDNA clone and its expression in brain and retina." Alterio J., Halley C., Brou C., Soussi T., Courtois Y., Laurent M. FEBS Lett. 242:41-46(1988) [PubMed: 2849564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Heart ventricle.
[4]	"Structural evidence that endothelial cell growth factor beta is the precursor of both endothelial cell growth factor alpha and acidic fibroblast growth factor." Burgess W.H., Mehlman T., Marshak D.R., Fraser B.A., Maciag T. Proc. Natl. Acad. Sci. U.S.A. 83:7216-7220(1986) [PubMed: 3532107] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-155, ACETYLATION AT ALA-2.
[5]	"Complete primary structure of prostatropin, a prostate epithelial cell growth factor." Crabb J.W., Armes L.G., Carr S.A., Johnson C.M., Roberts G.D., Bordoli R.S., McKeehan W.L. Biochemistry 25:4988-4993(1986) [PubMed: 3768327] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-155.
[6]	"Brain-derived acidic fibroblast growth factor: complete amino acid sequence and homologies." Gimenez-Gallego G., Rodkey J., Bennett C., Rios-Candelore M., Disalvo J., Thomas K. Science 230:1385-1388(1985) [PubMed: 4071057] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-155.
[7]	"Acidic fibroblast growth factor (FGF) from bovine brain: amino-terminal sequence and comparison with basic FGF." Boehlen P., Esch F., Baird A., Gospodarowicz D. EMBO J. 4:1951-1956(1985) [PubMed: 4065099] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-44, AMINO-ACID COMPOSITION.
[8]	"Nucleotide sequence of a bovine clone encoding the angiogenic protein, basic fibroblast growth factor." Abraham J.A., Mergia A., Whang J.L., Tumolo A., Friedman J., Hjerrild K.A., Gospodarowicz D., Fiddes J.C. Science 233:545-548(1986) [PubMed: 2425435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-56.
[9]	"Isolation of heparin-binding growth factors from bovine, porcine and canine hearts." Quinkler W., Maasberg M., Bernotat-Danielowski S., Luethe N., Sharma H.S., Schaper W. Eur. J. Biochem. 181:67-73(1989) [PubMed: 2714282] [Abstract] Cited for: PROTEIN SEQUENCE OF 16-45.
[10]	"Cloning of two different 5' untranslated exons of bovine acidic fibroblast growth factor by the single strand ligation to single-stranded cDNA methodology." Philippe J.-M., Renaud F., Desset S., Laurent M., Mallet J., Courtois Y., Edwards J.B. Biochem. Biophys. Res. Commun. 188:843-850(1992) [PubMed: 1280126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-18.
[11]	"The extravesicular domain of synaptotagmin-1 is released with the latent fibroblast growth factor-1 homodimer in response to heat shock." Tarantini F., LaVallee T., Jackson A., Gamble S., Mouta Carreira C., Garfinkel S., Burgess W.H., Maciag T. J. Biol. Chem. 273:22209-22216(1998) [PubMed: 9712834] [Abstract] Cited for: INTERACTION WITH SYT1, FUNCTION, HEPARIN BINDING, SUBCELLULAR LOCATION.
[12]	"Regulation of proliferation-survival decisions is controlled by FGF1 secretion in retinal pigmented epithelial cells." Bryckaert M., Guillonneau X., Hecquet C., Perani P., Courtois Y., Mascarelli F. Oncogene 19:4917-4929(2000) [PubMed: 11039909] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"Three-dimensional structures of acidic and basic fibroblast growth factors." Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T., Hsu B.T., Rees D.C. Science 251:90-93(1991) [PubMed: 1702556] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X13221 mRNA. Translation: CAA31610.1.
X14032 mRNA. Translation: CAA32192.1.
M35608 mRNA. Translation: AAA30517.1.
BC103225 mRNA. Translation: AAI03226.1.
M13439 Genomic DNA. Translation: AAA30516.1.
X66446 mRNA. Translation: CAA47063.1.
M97660 mRNA. Translation: AAA30563.1.
M97661 mRNA. Translation: AAA30564.1.

IPI

IPI00708726.

PIR

GKBOA. JH0613.

RefSeq

NP_776480.1. NM_174055.2.

UniGene

Bt.5038.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AFC	X-ray	2.70	A/B/C/D/E/F/G/H	16-155	[»]
1BAR	X-ray	2.70	A/B	16-155	[»]

ProteinModelPortal

P03968.

SMR

P03968. Positions 5-155.

ModBase

Search...

Protein-protein interaction databases

STRING

P03968.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000043056; ENSBTAP00000040651; ENSBTAG00000005198.

GeneID

281160.

KEGG

bta:281160.

Organism-specific databases

CTD

2246.

Phylogenomic databases

eggNOG

maNOG11540.

GeneTree

ENSGT00600000084030.

HOVERGEN

HBG007580.

InParanoid

P03968.

OMA

PSEECLF.

OrthoDB

EOG48KRCM.

PhylomeDB

P03968.

Family and domain databases

InterPro

IPR008996. Cytokine_IL1-like.
IPR002209. GF_heparin-bd.
IPR002348. IL1_HBGF.
[Graphical view]

K04358.

PANTHER

PTHR11486. IL1_HBGF. 1 hit.

Pfam

PF00167. FGF. 1 hit.
[Graphical view]

PRINTS

PR00263. HBGFFGF.
PR00262. IL1HBGF.

SMART

SM00442. FGF. 1 hit.
[Graphical view]

SUPFAM

SSF50353. Cytok_IL1_like. 1 hit.

PROSITE

PS00247. HBGF_FGF. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FGF1_BOVIN

Accession

Primary (citable) accession number: P03968
Secondary accession number(s): Q3ZBL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	July 1, 1989
Last modified:	November 16, 2011
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents