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VEGFA_BOVIN
ID   VEGFA_BOVIN             Reviewed;         190 AA.
AC   P15691;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Vascular endothelial growth factor A;
DE            Short=VEGF-A;
DE   AltName: Full=Vascular permeability factor;
DE            Short=VPF;
DE   Flags: Precursor;
GN   Name=VEGFA; Synonyms=VEGF;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 27-47.
RX   PubMed=2479986; DOI=10.1126/science.2479986;
RA   Leung D.W., Cachianes G., Kuang W.-J., Goeddel D.V., Ferrara N.;
RT   "Vascular endothelial growth factor is a secreted angiogenic mitogen.";
RL   Science 246:1306-1309(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 27-190 (ISOFORMS ALPHA AND BETA).
RX   PubMed=2610687; DOI=10.1016/0006-291x(89)92729-0;
RA   Tischer E., Gospodarowicz D., Mitchell R., Silva M., Schilling J., Lau K.,
RA   Crisp T., Fiddes J.C., Abraham J.A.;
RT   "Vascular endothelial growth factor: a new member of the platelet-derived
RT   growth factor gene family.";
RL   Biochem. Biophys. Res. Commun. 165:1198-1206(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 27-31.
RX   PubMed=2735925; DOI=10.1016/0006-291x(89)92678-8;
RA   Ferrara N., Henzel W.J.;
RT   "Pituitary follicular cells secrete a novel heparin-binding growth factor
RT   specific for vascular endothelial cells.";
RL   Biochem. Biophys. Res. Commun. 161:851-858(1989).
CC   -!- FUNCTION: Growth factor active in angiogenesis, vasculogenesis and
CC       endothelial cell growth. Induces endothelial cell proliferation,
CC       promotes cell migration, inhibits apoptosis and induces
CC       permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and
CC       KDR/VEGFR2 receptors, heparan sulfate and heparin (By similarity).
CC       Binding to NRP1 receptor initiates a signaling pathway needed for motor
CC       neuron axon guidance and cell body migration, including for the caudal
CC       migration of facial motor neurons from rhombomere 4 to rhombomere 6
CC       during embryonic development (By similarity). Also binds the
CC       DEAR/FBXW7-AS1 receptor (By similarity). {ECO:0000250|UniProtKB:P15692,
CC       ECO:0000250|UniProtKB:Q00731}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Also found as
CC       heterodimer with PGF (By similarity). Interacts with NRP1 (By
CC       similarity). Interacts with BSG (By similarity).
CC       {ECO:0000250|UniProtKB:P15692, ECO:0000250|UniProtKB:P16612}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted but remains
CC       associated to cells or to the extracellular matrix unless released by
CC       heparin. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha;
CC         IsoId=P15691-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=P15691-2; Sequence=VSP_004613, VSP_004614;
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC       {ECO:0000305}.
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DR   EMBL; M32976; AAA30502.1; -; mRNA.
DR   EMBL; M31836; AAA30804.1; -; mRNA.
DR   EMBL; M33750; AAA30805.1; -; mRNA.
DR   PIR; A33787; A33787.
DR   PIR; B40080; B40080.
DR   RefSeq; NP_001303884.1; NM_001316955.1.
DR   RefSeq; NP_001303885.1; NM_001316956.1.
DR   RefSeq; NP_001303921.1; NM_001316992.1.
DR   RefSeq; NP_001303922.1; NM_001316993.1.
DR   RefSeq; NP_776641.1; NM_174216.2. [P15691-1]
DR   AlphaFoldDB; P15691; -.
DR   SMR; P15691; -.
DR   CORUM; P15691; -.
DR   STRING; 9913.ENSBTAP00000056005; -.
DR   PaxDb; P15691; -.
DR   Ensembl; ENSBTAT00000007026; ENSBTAP00000007026; ENSBTAG00000005339. [P15691-1]
DR   GeneID; 281572; -.
DR   KEGG; bta:281572; -.
DR   CTD; 7422; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005339; -.
DR   eggNOG; ENOG502QVI8; Eukaryota.
DR   GeneTree; ENSGT00940000157284; -.
DR   InParanoid; P15691; -.
DR   OrthoDB; 1364454at2759; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000005339; Expressed in cardiac atrium and 102 other tissues.
DR   ExpressionAtlas; P15691; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR   GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR   GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; IBA:GO_Central.
DR   GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IBA:GO_Central.
DR   GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IBA:GO_Central.
DR   GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
DR   GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
DR   GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR   GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
DR   GO; GO:0035148; P:tube formation; ISS:UniProtKB.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IBA:GO_Central.
DR   CDD; cd00135; PDGF; 1.
DR   Gene3D; 2.10.160.10; -; 1.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR023581; PD_growth_factor_CS.
DR   InterPro; IPR000072; PDGF/VEGF_dom.
DR   InterPro; IPR027928; VEGF_C.
DR   InterPro; IPR036841; VEGF_C_sf.
DR   Pfam; PF00341; PDGF; 1.
DR   Pfam; PF14554; VEGF_C; 1.
DR   SMART; SM00141; PDGF; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   SUPFAM; SSF57593; SSF57593; 1.
DR   PROSITE; PS00249; PDGF_1; 1.
DR   PROSITE; PS50278; PDGF_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Angiogenesis; Developmental protein; Differentiation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor;
KW   Heparin-binding; Mitogen; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:2479986,
FT                   ECO:0000269|PubMed:2735925"
FT   CHAIN           27..190
FT                   /note="Vascular endothelial growth factor A"
FT                   /id="PRO_0000023383"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..93
FT                   /evidence="ECO:0000250"
FT   DISULFID        76
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..127
FT                   /evidence="ECO:0000250"
FT   DISULFID        85
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..129
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         139..183
FT                   /note="Missing (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:2610687"
FT                   /id="VSP_004613"
FT   VAR_SEQ         184
FT                   /note="R -> K (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:2610687"
FT                   /id="VSP_004614"
SQ   SEQUENCE   190 AA;  22310 MW;  EDBF903E46E24789 CRC64;
     MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGQKPHEVV KFMDVYQRSF CRPIETLVDI
     FQEYPDEIEF IFKPSCVPLM RCGGCCNDES LECVPTEEFN ITMQIMRIKP HQSQHIGEMS
     FLQHNKCECR PKKDKARQEN PCGPCSERRK HLFVQDPQTC KCSCKNTDSR CKARQLELNE
     RTCRCDKPRR
 
 
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