Reviewed,
UniProtKB/Swiss-Prot P03968 (FGF1_BOVIN)
Last modified
June 16, 2009.
Version 93.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Heparin-binding growth factor 1 Short name=HBGF-1 Alternative name(s): Acidic fibroblast growth factor Short name=aFGF Prostatropin Endothelial cell growth factor beta and alpha chains Acidic eye-derived growth factor II Short name=EDGF II Cleaved into the following 2 chains: 1- Recommended name: Endothelial cell growth factor beta 2- Recommended name: Endothelial cell growth factor alpha | ||||
| Gene names |
| ||||
| 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 | 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 structure | 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. |
| Sequence similarities | Belongs to the heparin-binding growth factors family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Angiogenesis Differentiation |
| Ligand | Heparin-binding |
| Molecular function | Developmental protein Growth factor Mitogen |
| PTM | Acetylation |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cell proliferationInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW heparin bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | 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 | 5 | Heparin-binding Potential | ||||||||||||||||||||||||||||||||||
| Region | 113 – 116 | 4 | Heparin-binding Potential | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.4 | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 27 – 31 | 5 | |||||||||||||||||||||||||||||||||||
| Turn | 32 – 34 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 37 – 40 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 46 – 50 | 5 | |||||||||||||||||||||||||||||||||||
| Helix | 55 – 57 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 61 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 65 – 67 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 71 – 76 | 6 | |||||||||||||||||||||||||||||||||||
| Beta strand | 79 – 82 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 86 – 93 | 8 | |||||||||||||||||||||||||||||||||||
| Helix | 96 – 98 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 113 – 115 | 3 | |||||||||||||||||||||||||||||||||||
| Turn | 116 – 121 | 6 | |||||||||||||||||||||||||||||||||||
| Helix | 135 – 137 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 147 – 150 | 4 | |||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide '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] | "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 | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 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. | ||||||||||||||||||
| UniGene | Bt.5038 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| |||||||||||||||||||
| SMR | P03968. Positions 5-155. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSBTAG00000005198. Bos taurus. [Contig view] | ||||||||||||||||||
| GeneID | 281160. | ||||||||||||||||||
| KEGG | bta:281160. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | P03968. | ||||||||||||||||||
| OMA | P03968. PSEECLF. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR002209. GF_heparin_bd. IPR002348. IL1_HBGF. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR11486. IL1_HBGF. 1 hit. | ||||||||||||||||||
| Pfam | PF00167. FGF. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00263. HBGFFGF. PR00262. IL1HBGF. | ||||||||||||||||||
| ProDom | PD000831. IL1_HBGF. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||
| SMART | SM00442. FGF. 1 hit. [Graphical view] | ||||||||||||||||||
| 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 |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


