PDGFD_PONAB
ID PDGFD_PONAB Reviewed; 370 AA.
AC Q5RA73;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Platelet-derived growth factor D;
DE Short=PDGF-D;
DE Contains:
DE RecName: Full=Platelet-derived growth factor D, latent form;
DE Short=PDGFD latent form;
DE Contains:
DE RecName: Full=Platelet-derived growth factor D, receptor-binding form;
DE Short=PDGFD receptor-binding form;
DE Flags: Precursor;
GN Name=PDGFD;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Growth factor that plays an essential role in the regulation
CC of embryonic development, cell proliferation, cell migration, survival
CC and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays
CC an important role in wound healing. Induces macrophage recruitment,
CC increased interstitial pressure, and blood vessel maturation during
CC angiogenesis. Can initiate events that lead to a mesangial
CC proliferative glomerulonephritis, including influx of monocytes and
CC macrophages and production of extracellular matrix (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRB homodimers,
CC and with heterodimers formed by PDGFRA and PDGFRB (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released by
CC platelets upon wounding. {ECO:0000250}.
CC -!- PTM: Activated by proteolytic cleavage. Proteolytic removal of the N-
CC terminal CUB domain releasing the core domain is necessary for
CC unmasking the receptor-binding epitopes of the core domain. Cleavage
CC after Arg-247 or Arg-249 by urokinase plasminogen activator gives rise
CC to the active form (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; CR859146; CAH91337.1; -; mRNA.
DR RefSeq; NP_001125790.1; NM_001132318.1.
DR AlphaFoldDB; Q5RA73; -.
DR SMR; Q5RA73; -.
DR STRING; 9601.ENSPPYP00000004370; -.
DR Ensembl; ENSPPYT00000004545; ENSPPYP00000004370; ENSPPYG00000003821.
DR GeneID; 100172718; -.
DR KEGG; pon:100172718; -.
DR CTD; 80310; -.
DR eggNOG; ENOG502QPQY; Eukaryota.
DR GeneTree; ENSGT00940000159575; -.
DR HOGENOM; CLU_037859_1_0_1; -.
DR InParanoid; Q5RA73; -.
DR OMA; FVYTLVC; -.
DR OrthoDB; 962163at2759; -.
DR TreeFam; TF332130; -.
DR Proteomes; UP000001595; Chromosome 11.
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:0005161; F:platelet-derived growth factor receptor binding; IEA:InterPro.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:InterPro.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00135; PDGF; 1.
DR Gene3D; 2.10.90.10; -; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR000072; PDGF/VEGF_dom.
DR InterPro; IPR027123; PDGFD.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR11633:SF4; PTHR11633:SF4; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00341; PDGF; 1.
DR SMART; SM00042; CUB; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50278; PDGF_2; 1.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Developmental protein; Disulfide bond;
KW Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..370
FT /note="Platelet-derived growth factor D, latent form"
FT /id="PRO_0000250192"
FT CHAIN 250..370
FT /note="Platelet-derived growth factor D, receptor-binding
FT form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000250193"
FT DOMAIN 52..170
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT SITE 247..248
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT SITE 249..250
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 296
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 302..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 306..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 370 AA; 42802 MW; 47B6027F2B699DB3 CRC64;
MHRLIFVCTL VCANFCSCRD TSATPQSASI KALRNANLRR DESNHLTDLY RRDETIQVRG
NGYVQSPRFP NSYPRNLLLT WRLHSQENTR IQLVFDNQFG LEEAENDICR YDFVEVEDIS
ETSTIIRGRW CGHKEVPPRI KSRTNQIKIT FKSDDYFVAK PGFKIYYSLL EDFQPAAASE
TNWESVTSSI SGVSYNSPSV TDPTLIADAL DKKIAEFDTV EDLLKYFNPE SWQEDLENMY
LDTPRYRGRS YHDRKSKVDL DRLNDDAKRY SCTPRNYSVN IREELKLANV VFFPRCLLVQ
RCGGNCGCGT VNWRSCTCNS GKTVKKYHEV LQFEPGHIKR RGRAKTMALV DIQLDHHERC
DCICSSRPPR
