PDGFD_RAT
ID PDGFD_RAT Reviewed; 370 AA.
AC Q9EQT1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Platelet-derived growth factor D;
DE Short=PDGF-D;
DE AltName: Full=Iris-expressed growth factor;
DE AltName: Full=Spinal cord-derived growth factor B;
DE Short=SCDGF-B;
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; Synonyms=Iegf, Scdgfb;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=11162582; DOI=10.1006/bbrc.2000.4187;
RA Hamada T., Ui-Tei K., Imaki J., Miyata Y.;
RT "Molecular cloning of SCDGF-B, a novel growth factor homologous to
RT SCDGF/PDGF-C/fallotein.";
RL Biochem. Biophys. Res. Commun. 280:733-737(2001).
RN [2]
RP IDENTIFICATION OF ISOFORM 2, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11850188; DOI=10.1016/s0925-4773(01)00625-6;
RA Hamada T., Ui-Tei K., Imaki J., Takahashi F., Onodera H., Mishima T.,
RA Miyata Y.;
RT "The expression of SCDGF/PDGF-C/fallotein and SCDGF-B/PDGF-D in the rat
RT central nervous system.";
RL Mech. Dev. 112:161-164(2002).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12937299; DOI=10.1097/01.asn.0000083393.00959.02;
RA Ostendorf T., van Roeyen C.R.C., Peterson J.D., Kunter U., Eitner F.,
RA Hamad A.J., Chan G., Jia X.-C., Macaluso J., Gazit-Bornstein G., Keyt B.A.,
RA Lichenstein H.S., LaRochelle W.J., Floege J.;
RT "A fully human monoclonal antibody (CR002) identifies PDGF-D as a novel
RT mediator of mesangioproliferative glomerulonephritis.";
RL J. Am. Soc. Nephrol. 14:2237-2247(2003).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15611105; DOI=10.1074/jbc.m413570200;
RA Ray S., Gao C., Wyatt K., Fariss R.N., Bundek A., Zelenka P., Wistow G.;
RT "Platelet-derived growth factor D, tissue-specific expression in the eye,
RT and a key role in control of lens epithelial cell proliferation.";
RL J. Biol. Chem. 280:8494-8502(2005).
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 (By similarity). May play an important role in control of
CC lens epithelial cell proliferation. Can initiate events that lead to a
CC mesangial proliferative glomerulonephritis, including influx of
CC monocytes and macrophages and production of extracellular matrix.
CC {ECO:0000250, ECO:0000269|PubMed:12937299,
CC ECO:0000269|PubMed:15611105}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EQT1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EQT1-2; Sequence=VSP_020619;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the
CC kidney, adrenal glands, eye and CNS. In the kidney the localization is
CC confined to arterial and arteriolar vascular smooth muscle cells and is
CC also detected at low levels in the glomeruli In the eye in the anterior
CC segment it is localized to the iris and ciliary body. In the retina
CC localizes intensely to the outer plexiform layer, which contains
CC photoreceptor axons and the synaptic layer between photoreceptors and
CC second order neurons. In the spinal cord, prominently expressed in the
CC motorneurons. {ECO:0000269|PubMed:11850188,
CC ECO:0000269|PubMed:12937299, ECO:0000269|PubMed:15611105}.
CC -!- DEVELOPMENTAL STAGE: Not detected in the spinal cord at E21. Expressed
CC weakly at postnatal day 1 (P1) and a strong expression seen at P21 and
CC this continues into adulthood. {ECO:0000269|PubMed:11850188}.
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; AB052170; BAB18920.1; -; mRNA.
DR PIR; JC7592; JC7592.
DR RefSeq; NP_076452.1; NM_023962.2. [Q9EQT1-1]
DR AlphaFoldDB; Q9EQT1; -.
DR SMR; Q9EQT1; -.
DR STRING; 10116.ENSRNOP00000068187; -.
DR GlyGen; Q9EQT1; 1 site.
DR PaxDb; Q9EQT1; -.
DR PRIDE; Q9EQT1; -.
DR Ensembl; ENSRNOT00000076529; ENSRNOP00000068187; ENSRNOG00000029148. [Q9EQT1-2]
DR GeneID; 66018; -.
DR KEGG; rno:66018; -.
DR UCSC; RGD:621880; rat. [Q9EQT1-1]
DR CTD; 80310; -.
DR RGD; 621880; Pdgfd.
DR VEuPathDB; HostDB:ENSRNOG00000029148; -.
DR eggNOG; ENOG502QPQY; Eukaryota.
DR GeneTree; ENSGT00940000159575; -.
DR HOGENOM; CLU_037859_1_0_1; -.
DR InParanoid; Q9EQT1; -.
DR OMA; FVYTLVC; -.
DR OrthoDB; 962163at2759; -.
DR PhylomeDB; Q9EQT1; -.
DR Reactome; R-RNO-186797; Signaling by PDGF.
DR PRO; PR:Q9EQT1; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000029148; Expressed in stomach and 17 other tissues.
DR ExpressionAtlas; Q9EQT1; baseline and differential.
DR Genevisible; Q9EQT1; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0070851; F:growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IBA:GO_Central.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:RGD.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IMP:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
DR GO; GO:2000439; P:positive regulation of monocyte extravasation; IMP:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; IMP:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:RGD.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
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 SMART; SM00141; PDGF; 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 Alternative splicing; Cleavage on pair of basic residues;
KW Developmental protein; Disulfide bond; Glycoprotein; Growth factor;
KW Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..370
FT /note="Platelet-derived growth factor D, latent form"
FT /id="PRO_0000250196"
FT CHAIN 250..370
FT /note="Platelet-derived growth factor D, receptor-binding
FT form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000250197"
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"
FT VAR_SEQ 42..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_020619"
SQ SEQUENCE 370 AA; 42809 MW; 7BE8A251F679BF73 CRC64;
MHRLILVSIL VCANFCCYRD TFATPQSASI KALRNANLRR DESNHLTDLY RRDENIRVTG
TGHVQSPRFP NSYPRNLLLT WRLHSQEKTR IQLAFDHQFG LEEAENDICR YDFVEVEDVS
ESSTVVRGRW CGHKEIPPRI TSRTNQIKIT FQSDDYFVAK PGFKIYYSFV EDFQPEAASE
INWESVTSSF SGVSYHSPSV MDSTLTADAL DKAIAEFDTV EDLLKYFNPA SWQDDLENLY
MDTPRYRGRS YHERKSKVDL DRLNDDVKRY SCTPRNHSVN LREELKLTNA VFFPRCLLVQ
RCGGNCGCGT LNWKSCTCSS GKTVKKYHEV LKFEPGHFKR RGKAKNMALV DIQLDHHERC
DCICSSRPPR
