PLGF_MOUSE
ID PLGF_MOUSE Reviewed; 158 AA.
AC P49764;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Placenta growth factor;
DE Short=PlGF;
DE Flags: Precursor;
GN Name=Pgf; Synonyms=Plgf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8903720; DOI=10.1007/s003359900003;
RA Dipalma T., Tucci M., Russo G., Maglione D., Lago C.T., Romano A.,
RA Saccone S., della Valle G., de Gregorio L., Dragani T.A., Viglietto G.,
RA Persico M.G.;
RT "The placenta growth factor gene of the mouse.";
RL Mamm. Genome 7:6-12(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NIH Swiss;
RX PubMed=9401819; DOI=10.3109/08977199709002113;
RA Achen M.G., Gad J.M., Stacker S.A., Wilks A.F.;
RT "Placenta growth factor and vascular endothelial growth factor are co-
RT expressed during early embryonic development.";
RL Growth Factors 15:69-80(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Growth factor active in angiogenesis and endothelial cell
CC growth, stimulating their proliferation and migration. It binds to the
CC receptor FLT1/VEGFR-1. Also promotes cell tumor growth (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Antiparallel homodimer; disulfide-linked. Also found as
CC heterodimer with VEGFA/VEGF (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; X80171; CAA56453.1; -; mRNA.
DR EMBL; X96793; CAA65587.1; -; mRNA.
DR EMBL; BC016567; AAH16567.1; -; mRNA.
DR CCDS; CCDS49115.1; -.
DR RefSeq; NP_032853.1; NM_008827.3.
DR AlphaFoldDB; P49764; -.
DR SMR; P49764; -.
DR IntAct; P49764; 1.
DR STRING; 10090.ENSMUSP00000004913; -.
DR BindingDB; P49764; -.
DR ChEMBL; CHEMBL1697670; -.
DR GlyGen; P49764; 3 sites.
DR PhosphoSitePlus; P49764; -.
DR PaxDb; P49764; -.
DR PeptideAtlas; P49764; -.
DR PRIDE; P49764; -.
DR ProteomicsDB; 289681; -.
DR Antibodypedia; 12927; 949 antibodies from 43 providers.
DR DNASU; 18654; -.
DR Ensembl; ENSMUST00000004913; ENSMUSP00000004913; ENSMUSG00000004791.
DR GeneID; 18654; -.
DR KEGG; mmu:18654; -.
DR UCSC; uc007ogq.2; mouse.
DR CTD; 5228; -.
DR MGI; MGI:105095; Pgf.
DR VEuPathDB; HostDB:ENSMUSG00000004791; -.
DR eggNOG; ENOG502S2DE; Eukaryota.
DR GeneTree; ENSGT00940000160164; -.
DR HOGENOM; CLU_042996_3_0_1; -.
DR InParanoid; P49764; -.
DR OMA; KQCECRP; -.
DR OrthoDB; 1364454at2759; -.
DR PhylomeDB; P49764; -.
DR TreeFam; TF319554; -.
DR Reactome; R-MMU-194313; VEGF ligand-receptor interactions.
DR Reactome; R-MMU-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR BioGRID-ORCS; 18654; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Pgf; mouse.
DR PRO; PR:P49764; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P49764; protein.
DR Bgee; ENSMUSG00000004791; Expressed in decidua and 143 other tissues.
DR ExpressionAtlas; P49764; baseline and differential.
DR Genevisible; P49764; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0060688; P:regulation of morphogenesis of a branching structure; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; ISO:MGI.
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; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR023581; PD_growth_factor_CS.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR Pfam; PF00341; PDGF; 1.
DR SMART; SM00141; PDGF; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00249; PDGF_1; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..158
FT /note="Placenta growth factor"
FT /id="PRO_0000023421"
FT REGION 136..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..90
FT /evidence="ECO:0000250"
FT DISULFID 73
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 79..125
FT /evidence="ECO:0000250"
FT DISULFID 82
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 83..127
FT /evidence="ECO:0000250"
SQ SEQUENCE 158 AA; 17876 MW; F16128BEA0790438 CRC64;
MLVMKLFTCF LQVLAGLAVH SQGALSAGNN STEVEVVPFN EVWGRSYCRP MEKLVYILDE
YPDEVSHIFS PSCVLLSRCS GCCGDEGLHC VPIKTANITM QILKIPPNRD PHFYVEMTFS
QDVLCECRPI LETTKAERRK TKGKRKRSRN SQTEEPHP