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Vascular endothelial growth factor A (VEGF-A) (Vascular permeability factor) (VPF)

 VEGFA_RAT               Reviewed;         214 AA.
P16612; Q541S6; Q91ZE1; Q9JKX7; Q9QXG6; Q9QXG7;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
16-NOV-2001, sequence version 2.
07-NOV-2018, entry version 164.
RecName: Full=Vascular endothelial growth factor A;
Short=VEGF-A;
AltName: Full=Vascular permeability factor;
Short=VPF;
Flags: Precursor;
Name=Vegfa; Synonyms=Vegf;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF-A164), AND PROTEIN SEQUENCE
OF 27-190.
PubMed=2320579; DOI=10.1073/pnas.87.7.2628;
Conn G., Bayne M.L., Soderman D.D., Kwok P.W., Sullivan K.A.,
Palisi T.M., Hope D.A., Thomas K.A.;
"Amino acid and cDNA sequences of a vascular endothelial cell mitogen
that is homologous to platelet-derived growth factor.";
Proc. Natl. Acad. Sci. U.S.A. 87:2628-2633(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF-A188; VEGF-A164; VEGF-A144
AND VEGF-A120).
PubMed=11163598; DOI=10.1016/S0003-9969(00)00081-9;
Ishii H., Oota I., Takuma T., Inomata K.;
"Developmental expression of vascular endothelial growth factor in the
masseter muscle of rats.";
Arch. Oral Biol. 46:77-82(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF-A164 AND VEGF-A188).
STRAIN=Sprague-Dawley;
Marion S., Lee T.-C.;
"Cloning of multiple VEGF splice variants from hypoxic neonatal rat
cardiomyocytes.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 27-40, AND HETERODIMERIZATION WITH PGF.
TISSUE=Glial tumor;
PubMed=7706320; DOI=10.1074/jbc.270.13.7717;
DiSalvo J., Bayne M.L., Conn G., Kwok P.W., Trivedi P.G.,
Soderman D.D., Palisi T.M., Sullivan K.A., Thomas K.A.;
"Purification and characterization of a naturally occurring vascular
endothelial growth factor.placenta growth factor heterodimer.";
J. Biol. Chem. 270:7717-7723(1995).
[5]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10878616;
DOI=10.1002/1097-0177(200007)218:3<507::AID-DVDY1012>3.0.CO;2-5;
Pepper M.S., Baetens D., Mandriota S.J., Di Sanza C., Oikemus S.,
Lane T.F., Soriano J.V., Montesano R., Iruela-Arispe M.L.;
"Regulation of VEGF and VEGF receptor expression in the rodent mammary
gland during pregnancy, lactation, and involution.";
Dev. Dyn. 218:507-524(2000).
-!- FUNCTION: Growth factor active in angiogenesis, vasculogenesis and
endothelial cell growth. Induces endothelial cell proliferation,
promotes cell migration, inhibits apoptosis and induces
permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and
KDR/VEGFR2 receptors, heparan sulfate and heparin. May play a role
in increasing vascular permeability during lactation, when
increased transport of molecules from the blood is required for
efficient milk protein synthesis. Binding to NRP1 receptor
initiates a signaling pathway needed for motor neuron axon
guidance and cell body migration, including for the caudal
migration of facial motor neurons from rhombomere 4 to rhombomere
6 during embryonic development (By similarity).
{ECO:0000250|UniProtKB:Q00731, ECO:0000269|PubMed:10878616}.
-!- SUBUNIT: Homodimer; disulfide-linked. Also found as heterodimer
with PGF. Interacts with NRP1 (By similarity).
{ECO:0000250|UniProtKB:Q00731}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=VEGF-A120 is
acidic and freely secreted. VEGF-A164 is more basic, has heparin-
binding properties and, although a signicant proportion remains
cell-associated, most is freely secreted. VEGF-A188 is very basic,
it is cell-associated after secretion and is bound avidly by
heparin and the extracellular matrix, although it may be released
as a soluble form by heparin, heparinase or plasmin (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=VEGF-A188;
IsoId=P16612-1; Sequence=Displayed;
Name=VEGF-A164;
IsoId=P16612-2; Sequence=VSP_004629, VSP_004630;
Name=VEGF-A144;
IsoId=P16612-3; Sequence=VSP_004632;
Name=VEGF-A120;
IsoId=P16612-4; Sequence=VSP_004631;
-!- TISSUE SPECIFICITY: Expressed in the pituitary, in brain, in
particularly in supraoptic and paraventricular nuclei and the
choroid plexus. Also found abundantly in the corpus luteum of the
ovary and in kidney glomeruli. Expressed in the ductal epithelial
cells of post-pubertal mammary glands. Expressed in the ductal and
alveolar epithelial cells throughout the whole period of
gestational evolution, lactation and involution.
{ECO:0000269|PubMed:10878616}.
-!- DEVELOPMENTAL STAGE: Increases during pregnancy (5.0-fold increase
on day 12 with a subsequent decrease on day 18) and during
lactation (18.5-fold increase on day 7). Levels appear to be
minimally altered during involution.
{ECO:0000269|PubMed:10878616}.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M32167; AAA41211.1; -; mRNA.
EMBL; AF215725; AAF19211.1; -; mRNA.
EMBL; AF215726; AAF19212.1; -; mRNA.
EMBL; AF222779; AAF25958.1; -; mRNA.
EMBL; AY033506; AAL07526.1; -; mRNA.
EMBL; AY033508; AAL07528.1; -; mRNA.
PIR; A35987; A35987.
RefSeq; NP_001103804.1; NM_001110334.2.
RefSeq; NP_001274036.1; NM_001287107.1. [P16612-1]
RefSeq; NP_001274037.1; NM_001287108.1. [P16612-2]
RefSeq; NP_001274039.1; NM_001287110.1. [P16612-4]
RefSeq; NP_001274040.1; NM_001287111.1.
RefSeq; NP_001274041.1; NM_001287112.1. [P16612-3]
RefSeq; NP_001274043.1; NM_001287114.1.
RefSeq; NP_114024.2; NM_031836.3.
UniGene; Rn.1923; -.
ProteinModelPortal; P16612; -.
SMR; P16612; -.
BioGrid; 249830; 1.
STRING; 10116.ENSRNOP00000026637; -.
PhosphoSitePlus; P16612; -.
PaxDb; P16612; -.
PRIDE; P16612; -.
GeneID; 83785; -.
KEGG; rno:83785; -.
UCSC; RGD:619991; rat. [P16612-1]
CTD; 7422; -.
RGD; 619991; Vegfa.
eggNOG; ENOG410IGCM; Eukaryota.
eggNOG; ENOG410ZWYU; LUCA.
HOGENOM; HOG000072704; -.
HOVERGEN; HBG000105; -.
InParanoid; P16612; -.
KO; K05448; -.
PhylomeDB; P16612; -.
PRO; PR:P16612; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P16612; RN.
GO; GO:0005604; C:basement membrane; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0042056; F:chemoattractant activity; IMP:RGD.
GO; GO:0008083; F:growth factor activity; IDA:RGD.
GO; GO:0019838; F:growth factor binding; IPI:RGD.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0043183; F:vascular endothelial growth factor receptor 1 binding; IBA:GO_Central.
GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IMP:RGD.
GO; GO:0043185; F:vascular endothelial growth factor receptor 3 binding; IBA:GO_Central.
GO; GO:0005172; F:vascular endothelial growth factor receptor binding; TAS:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0001525; P:angiogenesis; IMP:RGD.
GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; IMP:RGD.
GO; GO:0001974; P:blood vessel remodeling; IMP:RGD.
GO; GO:0060326; P:cell chemotaxis; IMP:RGD.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0030212; P:hyaluronan metabolic process; IEP:RGD.
GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
GO; GO:0048286; P:lung alveolus development; IMP:RGD.
GO; GO:0097475; P:motor neuron migration; ISS:UniProtKB.
GO; GO:0048255; P:mRNA stabilization; IDA:RGD.
GO; GO:0045779; P:negative regulation of bone resorption; IMP:RGD.
GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
GO; GO:0043069; P:negative regulation of programmed cell death; IMP:RGD.
GO; GO:0007399; P:nervous system development; IDA:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:RGD.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IBA:GO_Central.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0031334; P:positive regulation of protein complex assembly; ISS:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0009967; P:positive regulation of signal transduction; IDA:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
GO; GO:0043117; P:positive regulation of vascular permeability; IMP:RGD.
GO; GO:0009409; P:response to cold; IEP:RGD.
GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0051593; P:response to folic acid; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
GO; GO:0070482; P:response to oxygen levels; IEP:RGD.
GO; GO:0032570; P:response to progesterone; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
GO; GO:0042088; P:T-helper 1 type immune response; IDA:RGD.
GO; GO:0035148; P:tube formation; ISS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:RGD.
GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IBA:GO_Central.
GO; GO:0042060; P:wound healing; IEP:RGD.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.160.10; -; 1.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR023581; PD_growth_factor_CS.
InterPro; IPR000072; PDGF/VEGF_dom.
InterPro; IPR027928; VEGF_C.
InterPro; IPR036841; VEGF_C_sf.
Pfam; PF00341; PDGF; 1.
Pfam; PF14554; VEGF_C; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF57501; SSF57501; 1.
SUPFAM; SSF57593; SSF57593; 1.
PROSITE; PS00249; PDGF_1; 1.
PROSITE; PS50278; PDGF_2; 1.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Complete proteome;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; Glycoprotein; Growth factor; Heparin-binding; Mitogen;
Reference proteome; Secreted; Signal.
SIGNAL 1 26 {ECO:0000269|PubMed:2320579,
ECO:0000269|PubMed:7706320}.
CHAIN 27 214 Vascular endothelial growth factor A.
/FTId=PRO_0000023390.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
DISULFID 51 93 {ECO:0000250}.
DISULFID 76 76 Interchain. {ECO:0000250}.
DISULFID 82 127 {ECO:0000250}.
DISULFID 85 85 Interchain. {ECO:0000250}.
DISULFID 86 129 {ECO:0000250}.
VAR_SEQ 140 140 K -> N (in isoform VEGF-A164).
{ECO:0000303|PubMed:11163598,
ECO:0000303|PubMed:2320579,
ECO:0000303|Ref.3}.
/FTId=VSP_004629.
VAR_SEQ 141 208 Missing (in isoform VEGF-A120).
{ECO:0000303|PubMed:11163598}.
/FTId=VSP_004631.
VAR_SEQ 141 164 Missing (in isoform VEGF-A164).
{ECO:0000303|PubMed:11163598,
ECO:0000303|PubMed:2320579,
ECO:0000303|Ref.3}.
/FTId=VSP_004630.
VAR_SEQ 165 208 Missing (in isoform VEGF-A144).
{ECO:0000303|PubMed:11163598}.
/FTId=VSP_004632.
CONFLICT 101 101 V -> A (in Ref. 2; AAF19212).
{ECO:0000305}.
SEQUENCE 214 AA; 25239 MW; 60FBB876F5304946 CRC64;
MNFLLSWVHW TLALLLYLHH AKWSQAAPTT EGEQKAHEVV KFMDVYQRSY CRPIETLVDI
FQEYPDEIEY IFKPSCVPLM RCAGCCNDEA LECVPTSESN VTMQIMRIKP HQSQHIGEMS
FLQHSRCECR PKKDRTKPEK KSVRGKGKGQ KRKRKKSRFK SWSVHCEPCS ERRKHLFVQD
PQTCKCSCKN TDSRCKARQL ELNERTCRCD KPRR


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