Entry name
VEGF_HUMAN
Primary accession number
P15692
Secondary accession number(s)
None
Entered in SWISS-PROT in
Release 14, April 1990
Sequence was last modified in
Release 14, April 1990
Annotations were last modified in
Release 38, July 1999
Protein name
VASCULAR ENDOTHELIAL GROWTH FACTOR [Precursor]
Synonym(s)
VEGF
VASCULAR PERMEABILITY FACTOR
VPF
Gene name(s)
VEGF OR VEGFA
From
Taxonomy
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
[1]
SEQUENCE FROM N.A.
MEDLINE; 90069608. [NCBI,
ExPASy,
Israel,
Japan]
Leung D.W.,
Cachianes G.,
Kuang W.-J.,
Goeddel D.V.,
Ferrara N.;
"Vascular endothelial growth factor is a secreted angiogenic
mitogen.";
Science 246:1306-1309(1989).
[2]
SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
MEDLINE; 90069609. [NCBI,
ExPASy,
Israel,
Japan]
Keck P.J.,
Hauser S.D.,
Krivi G.,
Sanzo K.,
Warren T.,
Feder J.,
Connolly D.T.;
"Vascular permeability factor, an endothelial cell mitogen
related to PDGF.";
Science 246:1309-1312(1989).
[3]
SEQUENCE FROM N.A.
MEDLINE; 91268072. [NCBI,
ExPASy,
Israel,
Japan]
Tischer E.,
Mitchell R.,
Hartman T.,
Silva M.,
Gospodarowicz D.,
Fiddes J.C.,
Abraham J.A.;
"The human gene for vascular endothelial growth factor.
Multiple protein forms are encoded through alternative exon
splicing.";
J.
Biol. Chem. 266:11947-11954(1991).
[4]
SEQUENCE FROM N.A.
MEDLINE; 92231879. [NCBI,
ExPASy,
Israel,
Japan]
Weindel K.,
Marme D.,
Weich H.A.;
"AIDS-associated Kaposi's sarcoma cells in culture express
vascular endothelial growth factor.";
Biochem. Biophys. Res. Commun. 183:1167-1174(1992).
[5]
PRELIMINARY SEQUENCE OF 27-36; 43-50 AND 59-81.
MEDLINE; 90062112. [NCBI,
ExPASy,
Israel,
Japan]
Connolly D.T.,
Olander J.V.,
Heuvelman D.,
Nelson R.,
Monsell R.,
Siegel N.,
Haymore B.L.,
Leimgruber R.,
Feder J.;
"Human vascular permeability factor. Isolation from U937
cells.";
J.
Biol. Chem. 264:20017-20024(1989).
[6]
SEQUENCE OF 27-41.
MEDLINE; 93145946. [NCBI,
ExPASy,
Israel,
Japan]
Fiebich B.L.,
Jaeger B.,
Schoellmann C.,
Weindel K.,
Wilting J.,
Kochs G.,
Marme D.,
Hug H.,
Weich H.A.;
"Synthesis and assembly of functionally active human
vascular endothelial growth factor homodimers in insect
cells.";
Eur. J. Biochem. 211:19-26(1993).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-135.
MEDLINE; 97352774. [NCBI,
ExPASy,
Israel,
Japan]
Muller Y.A.,
Li B.,
Christinger H.W.,
Wells J.A.,
Cunningham B.C.,
de Vos A.M.;
"Vascular endothelial growth factor: crystal structure and
functional mapping of the kinase domain receptor binding
site.";
Proc.
Natl. Acad. Sci. U.S.A. 94:7192-7197(1997).
[8]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 34-135.
MEDLINE; 98035455. [NCBI,
ExPASy,
Israel,
Japan]
Muller Y.A.,
Christinger H.W.,
Keyt B.A.,
de Vos A.M.;
"The crystal structure of vascular endothelial growth factor
(VEGF) refined to 1.93-A resolution: multiple copy
flexibility and receptor binding.";
Structure 5:1325-1338(1997).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 39-134.
MEDLINE; 99119204. [NCBI,
ExPASy,
Israel,
Japan]
Wiesmann C.,
Christinger H.W.,
Cochran A.G.,
Cunningham B.C.,
Fairbrother W.J.,
Keenan C.J.,
Meng G.,
de Vos A.M.;
"Crystal structure of the complex between VEGF and a
receptor-blocking peptide.";
Biochemistry 37:17765-17772(1998).
[10]
STRUCTURE BY NMR OF 34-135.
MEDLINE; 97477915. [NCBI,
ExPASy,
Israel,
Japan]
Fairbrother W.J.,
Champe M.A.,
Christinger H.W.,
Keyt B.A.,
Starovasnik M.A.;
"1H, 13C, and 15N backbone assignment and secondary
structure of the receptor-binding domain of vascular
endothelial growth factor.";
Protein Sci. 6:2250-2260(1997).
[11]
STRUCTURE BY NMR OF 137-215.
MEDLINE; 98298440. [NCBI,
ExPASy,
Israel,
Japan]
Fairbrother W.J.,
Champe M.A.,
Christinger H.W.,
Keyt B.A.,
Starovasnik M.A.;
"Solution structure of the heparin-binding domain of
vascular endothelial growth factor.";
Structure 6:637-648(1998).
- FUNCTION: GROWTH FACTOR ACTIVE IN ANGIOGENESIS, AND ENDOTHELIAL CELL GROWTH. INDUCES ENDOTHELIAL PROLIFERATION AND VASCULAR PERMEABILITY.
- SUBUNIT: HOMODIMER, DISULFIDE-LINKED.
- SUBCELLULAR LOCATION: SECRETED BUT REMAINS ASSOCIATED TO CELLS OR TO THE EXTRACELLULAR MATRIX UNLESS RELEASED BY HEPARIN (BY SIMILARITY).
- ALTERNATIVE PRODUCTS: FOUR FORMS OF VEGF ARE PRODUCED BY ALTERNATIVE SPLICING OF THE SAME GENE (VEGF-121, VEGF-165, VEGF-189 AND VEGF-215).
- SIMILARITY: BELONGS TO THE PDGF/VEGF FAMILY OF GROWTH FACTORS.
Copyright
This SWISS-PROT entry is copyright. It is produced through a collaboration between the Swiss Institute of Bioinformatics and the EMBL outstation - the European Bioinformatics Institute. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://www.isb-sib.ch/announce/ or send an email to license@isb-sib.ch).
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EMBL |
M32977; AAA35789.1; -. [EMBL
/ GenBank
/ DDBJ]
[CoDingSequence] |
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PIR |
A34492; A34492. |
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PDB |
1VGH; 08-APR-98. [ExPASy
/ RCSB] |
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SWISS-3DIMAGE |
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MIM |
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GeneCards |
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PROSITE |
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PFAM |
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PRODOM |
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BLOCKS |
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DOMO |
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PROTOMAP |
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PRESAGE |
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SWISS-2DPAGE |
Mitogen; Growth factor; Glycoprotein; Alternative splicing; Signal; 3D-structure.
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SIGNAL 1 26 |
FT
table viewer |
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Length: 215 AA [This is the length of the unprocessed precursor] |
Molecular weight: 25173 Da [This is the Mw of the unprocessed precursor] |
CRC64: 7B9759AD5871FF33 [This is a checksum on the sequence] |
10 20 30 40 50 60
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MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD
70 80 90 100 110 120
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IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM
130 140 150 160 170 180
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SFLQHNKCEC RPKKDRARQE KKSVRGKGKG QKRKRKKSRY KSWSVPCGPC SERRKHLFVQ
190 200 210 215
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DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR
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P15692 in FASTA format |
