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VEGFA_PROFL
ID   VEGFA_PROFL             Reviewed;         216 AA.
AC   P67860; C0K3N7; Q68BI2; Q68BI3; Q68BI4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Vascular endothelial growth factor A;
DE            Short=VEGF-A;
DE   AltName: Full=Vascular permeability factor;
DE            Short=VPF;
DE   Flags: Precursor;
OS   Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX   NCBI_TaxID=88087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF-122; VEGF-166 AND VEGF-190),
RP   INTERACTION WITH FLT1; KDR; HEPARAN SULFATE AND HEPARIN, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=15328352; DOI=10.1074/jbc.m403687200;
RA   Takahashi H., Hattori S., Iwamatsu A., Takizawa H., Shibuya M.;
RT   "A novel snake venom vascular endothelial growth factor (VEGF)
RT   predominantly induces vascular permeability through preferential signaling
RT   via VEGF receptor-1.";
RL   J. Biol. Chem. 279:46304-46314(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF-190).
RC   TISSUE=Venom gland;
RX   PubMed=19208624; DOI=10.1074/jbc.m809071200;
RA   Yamazaki Y., Matsunaga Y., Tokunaga Y., Obayashi S., Saito M., Morita T.;
RT   "Snake venom vascular endothelial growth factors (VEGF-Fs) exclusively vary
RT   their structures and functions among species.";
RL   J. Biol. Chem. 284:9885-9891(2009).
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. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Also found as heterodimer with
CC       PGF (By similarity). Interacts to the FLT1/VEGFR1 and KDR/VEGFR2
CC       receptors, heparan sulfate and heparin. {ECO:0000250,
CC       ECO:0000269|PubMed:15328352}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=VEGF-190;
CC         IsoId=P67860-1; Sequence=Displayed;
CC       Name=VEGF-166;
CC         IsoId=P67860-2; Sequence=VSP_011751;
CC       Name=VEGF-122;
CC         IsoId=P67860-3; Sequence=VSP_011752;
CC   -!- TISSUE SPECIFICITY: Expressed in venom gland, heart, brain, liver,
CC       skeletal muscle and kidney. {ECO:0000269|PubMed:15328352}.
CC   -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC       {ECO:0000305}.
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DR   EMBL; AB154418; BAD38845.1; -; mRNA.
DR   EMBL; AB154419; BAD38846.1; -; mRNA.
DR   EMBL; AB154420; BAD38847.1; -; mRNA.
DR   EMBL; FJ554641; ACN22044.1; -; Genomic_DNA.
DR   AlphaFoldDB; P67860; -.
DR   SMR; P67860; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB.
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   Disulfide bond; Glycoprotein; Growth factor; Heparin-binding; Mitogen;
KW   Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..216
FT                   /note="Vascular endothelial growth factor A"
FT                   /id="PRO_0000023396"
FT   REGION          140..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..161
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..94
FT                   /evidence="ECO:0000250"
FT   DISULFID        77
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        83..128
FT                   /evidence="ECO:0000250"
FT   DISULFID        86
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        87..130
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         142..166
FT                   /note="KKSKREKGKGQKRKRKRGRYKPQNF -> N (in isoform VEGF-
FT                   166)"
FT                   /evidence="ECO:0000303|PubMed:15328352"
FT                   /id="VSP_011751"
FT   VAR_SEQ         143..210
FT                   /note="Missing (in isoform VEGF-122)"
FT                   /evidence="ECO:0000303|PubMed:15328352"
FT                   /id="VSP_011752"
SQ   SEQUENCE   216 AA;  25511 MW;  F2A3D98C503E8191 CRC64;
     MNFLLTWIHW GLAALLYFHN AKVLQAAPAQ GDGDRQQSEV IPFMTVYERS VCRPIETMVD
     IFQDYPDEVE YILKPPCVAL MRCGGCCNDE ALECVPTELY NVTMEIMKLK PYQSQHIHPM
     SFQQHSKCEC RPKKETRIIQ EKKSKREKGK GQKRKRKRGR YKPQNFHCEP CSERRKHLYK
     QDPLTCKCSC KFTDSRCKSK QLELNERTCR CEKPRR
 
 
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