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Placenta growth factor (PlGF)

 PLGF_HUMAN              Reviewed;         221 AA.
P49763; Q07101; Q9BV78; Q9Y6S8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
16-NOV-2001, sequence version 2.
20-JUN-2018, entry version 168.
RecName: Full=Placenta growth factor;
Short=PlGF;
Flags: Precursor;
Name=PGF; Synonyms=PGFL, PLGF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLGF-1).
TISSUE=Placenta;
PubMed=1924389; DOI=10.1073/pnas.88.20.9267;
Maglione D., Guerriero V., Viglietto G., Delli-Bovi P., Persico M.G.;
"Isolation of a human placenta cDNA coding for a protein related to
the vascular permeability factor.";
Proc. Natl. Acad. Sci. U.S.A. 88:9267-9271(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLGF-2).
TISSUE=Placenta;
PubMed=8148155; DOI=10.3109/08977199308991586;
Hauser S.D., Weich H.A.;
"A heparin-binding form of placenta growth factor (PlGF-2) is
expressed in human umbilical vein endothelial cells and in placenta.";
Growth Factors 9:259-268(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLGF-3).
TISSUE=Placenta;
PubMed=9207183; DOI=10.1006/bbrc.1997.6813;
Cao Y., Ji W.-R., Qi P., Rosin A., Cao Y.;
"Placenta growth factor: identification and characterization of a
novel isoform generated by RNA alternative splicing.";
Biochem. Biophys. Res. Commun. 235:493-498(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLGF-4).
TISSUE=Placenta;
PubMed=14568677; DOI=10.1016/S0165-0378(03)00082-2;
Yang W., Ahn H., Hinrichs M., Torry R.J., Torry D.S.;
"Evidence of a novel isoform of placenta growth factor (PlGF-4)
expressed in human trophoblast and endothelial cells.";
J. Reprod. Immunol. 60:53-60(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PLGF-2).
TISSUE=Muscle, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 19-24, AND CHARACTERIZATION.
PubMed=7929268;
Park J.E., Chen H.H., Winer J., Houck K.A., Ferrara N.;
"Placenta growth factor. Potentiation of vascular endothelial growth
factor bioactivity, in vitro and in vivo, and high affinity binding to
Flt-1 but not to Flk-1/KDR.";
J. Biol. Chem. 269:25646-25654(1994).
[8]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM PLGF-2).
PubMed=7681160;
Maglione D., Guerriero V., Viglietto G., Ferraro M.G., Aprelikova O.,
Alitalo K., del Vecchio S., Lei K.-J., Chou J.Y., Persico M.G.;
"Two alternative mRNAs coding for the angiogenic factor, placenta
growth factor (PlGF), are transcribed from a single gene of chromosome
14.";
Oncogene 8:925-931(1993).
[9]
FUNCTION AS A TUMOR ACTIVATOR.
PubMed=21215706; DOI=10.1016/j.ccr.2010.11.009;
Rolny C., Mazzone M., Tugues S., Laoui D., Johansson I., Coulon C.,
Squadrito M.L., Segura I., Li X., Knevels E., Costa S., Vinckier S.,
Dresselaer T., Akerud P., De Mol M., Salomaki H., Phillipson M.,
Wyns S., Larsson E., Buysschaert I., Botling J., Himmelreich U.,
Van Ginderachter J.A., De Palma M., Dewerchin M., Claesson-Welsh L.,
Carmeliet P.;
"HRG inhibits tumor growth and metastasis by inducing macrophage
polarization and vessel normalization through downregulation of
PlGF.";
Cancer Cell 19:31-44(2011).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) (ISOFORM PLGF-1).
PubMed=11069911; DOI=10.1074/jbc.M008055200;
Iyer S., Leonidas D.D., Swaminathan G.J., Maglione D., Battisti M.,
Tucci M., Persico M.G., Acharya K.R.;
"The crystal structure of human placenta growth factor-1 (PlGF-1), an
angiogenic protein, at 2.0 A resolution.";
J. Biol. Chem. 276:12153-12161(2001).
-!- FUNCTION: Growth factor active in angiogenesis and endothelial
cell growth, stimulating their proliferation and migration. It
binds to the receptor FLT1/VEGFR-1. Isoform PlGF-2 binds
NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent
manner. Also promotes cell tumor growth.
{ECO:0000269|PubMed:21215706}.
-!- SUBUNIT: Antiparallel homodimer; disulfide-linked. Also found as
heterodimer with VEGFA/VEGF. Isoform PlGF-3 is found both as
homodimer and as monomer.
-!- INTERACTION:
P17948:FLT1; NbExp=2; IntAct=EBI-1037633, EBI-1026718;
-!- SUBCELLULAR LOCATION: Secreted. Note=The three isoforms are
secreted but PlGF-2 appears to remain cell attached unless
released by heparin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=PlGF-3 {ECO:0000303|PubMed:9207183}; Synonyms=PlGF-203;
IsoId=P49763-1; Sequence=Displayed;
Name=PlGF-1 {ECO:0000303|PubMed:9207183}; Synonyms=PlGF-131;
IsoId=P49763-2; Sequence=VSP_004644;
Name=PlGF-2 {ECO:0000303|PubMed:8148155}; Synonyms=PlGF-152;
IsoId=P49763-3; Sequence=VSP_004644, VSP_004645;
Name=PlGF-4 {ECO:0000303|PubMed:14568677}; Synonyms=PlGF-224;
IsoId=P49763-4; Sequence=VSP_004645;
-!- TISSUE SPECIFICITY: While the three isoforms are present in most
placental tissues, PlGF-2 is specific to early (8 week) placenta
and only PlGF-1 is found in the colon and mammary carcinomas.
-!- DOMAIN: Isoform PlGF-2 contains a basic insert which acts as a
cell retention signal.
-!- PTM: N-glycosylated.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB25832.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X54936; CAA38698.1; -; mRNA.
EMBL; S72960; AAB30462.2; -; mRNA.
EMBL; AC006530; AAD30179.1; -; Genomic_DNA.
EMBL; BC001422; AAH01422.1; -; mRNA.
EMBL; BC007789; AAH07789.1; -; mRNA.
EMBL; BC007255; AAH07255.1; -; mRNA.
EMBL; S57152; AAB25832.2; ALT_SEQ; Genomic_DNA.
CCDS; CCDS55932.1; -. [P49763-2]
CCDS; CCDS9835.1; -. [P49763-3]
PIR; A41236; A41236.
RefSeq; NP_001193941.1; NM_001207012.1. [P49763-2]
RefSeq; NP_002623.2; NM_002632.5. [P49763-3]
UniGene; Hs.252820; -.
PDB; 1FZV; X-ray; 2.00 A; A/B=19-131, A/B=204-221.
PDB; 1RV6; X-ray; 2.45 A; V/W=37-136.
PDBsum; 1FZV; -.
PDBsum; 1RV6; -.
ProteinModelPortal; P49763; -.
SMR; P49763; -.
BioGrid; 111249; 4.
DIP; DIP-5752N; -.
IntAct; P49763; 2.
STRING; 9606.ENSP00000451040; -.
BindingDB; P49763; -.
ChEMBL; CHEMBL1697671; -.
DrugBank; DB08885; Aflibercept.
iPTMnet; P49763; -.
PhosphoSitePlus; P49763; -.
BioMuta; PGF; -.
DMDM; 17380553; -.
PaxDb; P49763; -.
PeptideAtlas; P49763; -.
PRIDE; P49763; -.
ProteomicsDB; 56100; -.
ProteomicsDB; 56101; -. [P49763-2]
ProteomicsDB; 56102; -. [P49763-3]
DNASU; 5228; -.
Ensembl; ENST00000405431; ENSP00000385365; ENSG00000119630. [P49763-1]
Ensembl; ENST00000553716; ENSP00000451413; ENSG00000119630. [P49763-2]
Ensembl; ENST00000555567; ENSP00000451040; ENSG00000119630. [P49763-3]
GeneID; 5228; -.
KEGG; hsa:5228; -.
UCSC; uc001xrb.4; human. [P49763-1]
CTD; 5228; -.
DisGeNET; 5228; -.
EuPathDB; HostDB:ENSG00000119630.13; -.
GeneCards; PGF; -.
HGNC; HGNC:8893; PGF.
HPA; HPA041624; -.
MIM; 601121; gene.
neXtProt; NX_P49763; -.
OpenTargets; ENSG00000119630; -.
PharmGKB; PA33231; -.
eggNOG; ENOG410IY55; Eukaryota.
eggNOG; ENOG410YNR0; LUCA.
GeneTree; ENSGT00730000110791; -.
HOGENOM; HOG000230896; -.
InParanoid; P49763; -.
KO; K16859; -.
OMA; RCECRPL; -.
OrthoDB; EOG091G0G6M; -.
PhylomeDB; P49763; -.
TreeFam; TF319554; -.
Reactome; R-HSA-194313; VEGF ligand-receptor interactions.
Reactome; R-HSA-195399; VEGF binds to VEGFR leading to receptor dimerization.
EvolutionaryTrace; P49763; -.
GeneWiki; Placental_growth_factor; -.
GenomeRNAi; 5228; -.
PRO; PR:P49763; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000119630; -.
CleanEx; HS_PGF; -.
ExpressionAtlas; P49763; baseline and differential.
Genevisible; P49763; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0008083; F:growth factor activity; IMP:UniProtKB.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IBA:GO_Central.
GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IBA:GO_Central.
GO; GO:0060754; P:positive regulation of mast cell chemotaxis; IBA:GO_Central.
GO; GO:0060688; P:regulation of morphogenesis of a branching structure; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0002040; P:sprouting angiogenesis; IEA:Ensembl.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IBA:GO_Central.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR023581; PD_growth_factor_CS.
InterPro; IPR000072; PDGF/VEGF_dom.
Pfam; PF00341; PDGF; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00249; PDGF_1; 1.
PROSITE; PS50278; PDGF_2; 1.
1: Evidence at protein level;
3D-structure; 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 18 {ECO:0000269|PubMed:7929268}.
CHAIN 19 221 Placenta growth factor.
/FTId=PRO_0000023420.
REGION 193 213 Heparin-binding. {ECO:0000305}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 52 94
DISULFID 77 77 Interchain.
DISULFID 83 128
DISULFID 86 86 Interchain.
DISULFID 87 130
VAR_SEQ 132 203 Missing (in isoform PlGF-1 and isoform
PlGF-2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1924389,
ECO:0000303|PubMed:8148155}.
/FTId=VSP_004644.
VAR_SEQ 213 213 R -> RRRPKGRGKRRREKQRPTDCHL (in isoform
PlGF-2 and isoform PlGF-4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8148155,
ECO:0000305|PubMed:14568677}.
/FTId=VSP_004645.
CONFLICT 91 91 N -> D (in Ref. 2; AAB30462).
{ECO:0000305}.
HELIX 43 50 {ECO:0000244|PDB:1FZV}.
STRAND 51 60 {ECO:0000244|PDB:1FZV}.
HELIX 62 64 {ECO:0000244|PDB:1FZV}.
STRAND 65 67 {ECO:0000244|PDB:1FZV}.
STRAND 73 84 {ECO:0000244|PDB:1FZV}.
STRAND 92 108 {ECO:0000244|PDB:1FZV}.
STRAND 111 113 {ECO:0000244|PDB:1RV6}.
STRAND 116 132 {ECO:0000244|PDB:1FZV}.
SEQUENCE 221 AA; 24789 MW; D364C6A73C1C6987 CRC64;
MPVMRLFPCF LQLLAGLALP AVPPQQWALS AGNGSSEVEV VPFQEVWGRS YCRALERLVD
VVSEYPSEVE HMFSPSCVSL LRCTGCCGDE NLHCVPVETA NVTMQLLKIR SGDRPSYVEL
TFSQHVRCEC RHSPGRQSPD MPGDFRADAP SFLPPRRSLP MLFRMEWGCA LTGSQSAVWP
SSPVPEEIPR MHPGRNGKKQ QRKPLREKMK PERCGDAVPR R


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