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PLGF_RAT
ID   PLGF_RAT                Reviewed;         158 AA.
AC   Q63434;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Placenta growth factor;
DE            Short=PlGF;
DE   Flags: Precursor;
GN   Name=Pgf; Synonyms=Plgf;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND
RP   HETERODIMERIZATION WITH VEGFA.
RX   PubMed=7706320; DOI=10.1074/jbc.270.13.7717;
RA   DiSalvo J., Bayne M.L., Conn G., Kwok P.W., Trivedi P.G., Soderman D.D.,
RA   Palisi T.M., Sullivan K.A., Thomas K.A.;
RT   "Purification and characterization of a naturally occurring vascular
RT   endothelial growth factor.placenta growth factor heterodimer.";
RL   J. Biol. Chem. 270:7717-7723(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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.
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; L40030; AAA97426.1; -; mRNA.
DR   EMBL; BC087006; AAH87006.1; -; mRNA.
DR   PIR; A56125; A56125.
DR   RefSeq; NP_446047.1; NM_053595.2.
DR   AlphaFoldDB; Q63434; -.
DR   SMR; Q63434; -.
DR   STRING; 10116.ENSRNOP00000007790; -.
DR   GlyGen; Q63434; 3 sites.
DR   PaxDb; Q63434; -.
DR   GeneID; 94203; -.
DR   KEGG; rno:94203; -.
DR   UCSC; RGD:619850; rat.
DR   CTD; 5228; -.
DR   RGD; 619850; Pgf.
DR   VEuPathDB; HostDB:ENSRNOG00000005650; -.
DR   eggNOG; ENOG502S2DE; Eukaryota.
DR   HOGENOM; CLU_042996_3_0_1; -.
DR   InParanoid; Q63434; -.
DR   OMA; KQCECRP; -.
DR   OrthoDB; 1364454at2759; -.
DR   PhylomeDB; Q63434; -.
DR   TreeFam; TF319554; -.
DR   Reactome; R-RNO-194313; VEGF ligand-receptor interactions.
DR   Reactome; R-RNO-195399; VEGF binds to VEGFR leading to receptor dimerization.
DR   PRO; PR:Q63434; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000005650; Expressed in skeletal muscle tissue and 17 other tissues.
DR   Genevisible; Q63434; RN.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
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; IPI:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IBA:GO_Central.
DR   GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR   GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IDA:RGD.
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; IMP:RGD.
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; ISO:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0002040; P:sprouting angiogenesis; IDA:RGD.
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   1: Evidence at protein level;
KW   Angiogenesis; Developmental protein; Differentiation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Growth factor;
KW   Mitogen; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /note="Or 26"
FT   CHAIN           24..158
FT                   /note="Placenta growth factor"
FT                   /id="PRO_0000023422"
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   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
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;  17681 MW;  B4771373A82E15B9 CRC64;
     MLAMKLFTCF LQVLAGLAVH SQGALSAGNN STEMEVVPFN EVWGRSYCRP MEKLVYIADE
     HPNEVSHIFS PSCVLLSRCS GCCGDEGLHC VALKTANITM QILKIPPNRD PHSYVEMTFS
     QDVLCECRPI LETTKAERRK TKGKRKQSKT PQTEEPHL
 
 
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