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UniProtKB/Swiss-Prot entry P03968

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FGF1_BOVIN
Primary accession number P03968
Secondary accession number Q3ZBL8
Integrated into Swiss-Prot on October 23, 1986
Sequence was last modified on July 1, 1989 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 89)
Name and origin of the protein
Protein name Heparin-binding growth factor 1 [Precursor]
Synonyms HBGF-1
Acidic fibroblast growth factor
aFGF
Prostatropin
Endothelial cell growth factor beta and alpha chains
Acidic eye-derived growth factor II
EDGF II
Contains Endothelial cell growth factor beta
Endothelial cell growth factor alpha
Gene name
Name: FGF1
Synonyms: AFGF, FGF-1, FGFA, HBGF-1
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Retina;
DOI=10.1093/nar/16.22.10913; PubMed=3205724 [NCBI, ExPASy, EBI, Israel, Japan]
Halley C., Courtois Y., Laurent M.;
"Nucleotide sequence of bovine acidic fibroblast growth factor cDNA.";
Nucleic Acids Res. 16:10913-10913(1988).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Retina;
DOI=10.1016/0014-5793(88)80981-5; PubMed=2849564 [NCBI, ExPASy, EBI, Israel, Japan]
Alterio J., Halley C., Brou C., Soussi T., Courtois Y., Laurent M.;
"Characterization of a bovine acidic FGF cDNA clone and its expression in brain and retina.";
FEBS Lett. 242:41-46(1988).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford;
TISSUE=Heart ventricle;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
 PROTEIN SEQUENCE OF 2-155.
PubMed=3532107 [NCBI, ExPASy, EBI, Israel, Japan]
Burgess W.H., Mehlman T., Marshak D.R., Fraser B.A., Maciag T.;
"Structural evidence that endothelial cell growth factor beta is the precursor of both endothelial cell growth factor alpha and acidic fibroblast growth factor.";
Proc. Natl. Acad. Sci. U.S.A. 83:7216-7220(1986).
[5]
 PROTEIN SEQUENCE OF 2-155.
DOI=10.1021/bi00366a003; PubMed=3768327 [NCBI, ExPASy, EBI, Israel, Japan]
Crabb J.W., Armes L.G., Carr S.A., Johnson C.M., Roberts G.D., Bordoli R.S., McKeehan W.L.;
"Complete primary structure of prostatropin, a prostate epithelial cell growth factor.";
Biochemistry 25:4988-4993(1986).
[6]
 PROTEIN SEQUENCE OF 16-155.
PubMed=4071057 [NCBI, ExPASy, EBI, Israel, Japan]
Gimenez-Gallego G., Rodkey J., Bennett C., Rios-Candelore M., Disalvo J., Thomas K.;
"Brain-derived acidic fibroblast growth factor: complete amino acid sequence and homologies.";
Science 230:1385-1388(1985).
[7]
 PROTEIN SEQUENCE OF 16-44, AND AMINO-ACID COMPOSITION.
PubMed=4065099 [NCBI, ExPASy, EBI, Israel, Japan]
Boehlen P., Esch F., Baird A., Gospodarowicz D.;
"Acidic fibroblast growth factor (FGF) from bovine brain: amino-terminal sequence and comparison with basic FGF.";
EMBO J. 4:1951-1956(1985).
[8]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-56.
PubMed=2425435 [NCBI, ExPASy, EBI, Israel, Japan]
Abraham J.A., Mergia A., Whang J.L., Tumolo A., Friedman J., Hjerrild K.A., Gospodarowicz D., Fiddes J.C.;
"Nucleotide sequence of a bovine clone encoding the angiogenic protein, basic fibroblast growth factor.";
Science 233:545-548(1986).
[9]
 PROTEIN SEQUENCE OF 16-45.
PubMed=2714282 [NCBI, ExPASy, EBI, Israel, Japan]
Quinkler W., Maasberg M., Bernotat-Danielowski S., Luethe N., Sharma H.S., Schaper W.;
"Isolation of heparin-binding growth factors from bovine, porcine and canine hearts.";
Eur. J. Biochem. 181:67-73(1989).
[10]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1-18.
DOI=10.1016/0006-291X(92)91133-B; PubMed=1280126 [NCBI, ExPASy, EBI, Israel, Japan]
Philippe J.-M., Renaud F., Desset S., Laurent M., Mallet J., Courtois Y., Edwards J.B.;
"Cloning of two different 5' untranslated exons of bovine acidic fibroblast growth factor by the single strand ligation to single-stranded cDNA methodology.";
Biochem. Biophys. Res. Commun. 188:843-850(1992).
[11]
 X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=1702556 [NCBI, ExPASy, EBI, Israel, Japan]
Zhu X., Komiya H., Chirino A., Faham S., Fox G.M., Arakawa T., Hsu B.T., Rees D.C.;
"Three-dimensional structures of acidic and basic fibroblast growth factors.";
Science 251:90-93(1991).
Comments
  • FUNCTION: The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
  • SUBUNIT: Monomer. Binds FGFR2. Forms a ternary complex containing 2 molecules each of FGFR2 and FGF1 for 1 heparin molecule. Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP1 (By similarity).
  • MISCELLANEOUS: This protein binds heparin, although less strongly than does bFGF.
  • SIMILARITY: Belongs to the heparin-binding growth factors family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X13221; CAA31610.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X14032; CAA32192.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M35608; AAA30517.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC103225; AAI03226.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M13439; AAA30516.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X66446; CAA47063.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M97660; AAA30563.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M97661; AAA30564.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JH0613; GKBOA.
RefSeq NP_776480.1; -.
UniGene Bt.5038
3D structure databases
PDB
1AFC; X-ray; 2.70 A; A/B/C/D/E/F/G/H=16-155.[ExPASy / RCSB / EBI]
1BAR; X-ray; 2.70 A; A/B=16-155.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AFC; -.
1BAR; -.
SMR P03968; 5-155.
ModBase P03968.
Ontologies
GO
GO:0008083; Molecular function: growth factor activity (inferred from electronic annotation from InterPro).
GO:0008201; Molecular function: heparin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0001525; Biological process: angiogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002209; GF_heparin_bd.
IPR002348; IL1_HBGF.
Graphical view of domain structure.
PANTHER PTHR11486; IL1_HBGF; 1.
Pfam PF00167; FGF; 1.
Pfam graphical view of domain structure.
PRINTS PR00263; HBGFFGF.
PR00262; IL1HBGF.
ProDom PD000831; IL1_HBGF; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00442; FGF; 1.
SMART graphical view of domain structure.
PROSITE PS00247; HBGF_FGF; 1.
ProtoNet P03968.
Genome annotation databases
Ensembl ENSBTAG00000005198; Bos taurus. [Contig view]
GeneID 281160; -.
KEGG bta:281160; -.
Phylogenomic databases
HOVERGEN P03968; -.
Other
LinkHub P03968; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Angiogenesis; Developmental protein; Differentiation; Direct protein sequencing; Growth factor; Heparin-binding; Mitogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
PROPEP   1    15  15      PRO_0000008903
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
REGION   24    28  5     Heparin-binding (Potential). 
REGION   113   116  4     Heparin-binding (Potential). 
MOD_RES   2     2        N-acetylalanine. 
STRAND   27    31  5      
TURN   32    34  3      
STRAND   37    40  4      
STRAND   46    50  5      
HELIX   55    57  3      
STRAND   59    61  3      
STRAND   65    67  3      
STRAND   71    76  6      
STRAND   79    82  4      
STRAND   86    93  8      
HELIX   96    98  3      
STRAND   113   115  3      
TURN   116   121  6      
HELIX   135   137  3      
STRAND   147   150  4      
Sequence information
Length: 155 AA [This is the length of the unprocessed precursor] Molecular weight: 17493 Da [This is the MW of the unprocessed precursor] CRC64: F636641F189F9BFD [This is a checksum on the sequence] 
        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
P03968 in FASTA format

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