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Platelet-derived growth factor D (PDGF-D) (Iris-expressed growth factor) (Spinal cord-derived growth factor B) (SCDGF-B) [Cleaved into: Platelet-derived growth factor D, latent form (PDGFD latent form); Platelet-derived growth factor D, receptor-binding form (PDGFD receptor-binding form)]

 PDGFD_RAT               Reviewed;         370 AA.
Q9EQT1;
19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 97.
RecName: Full=Platelet-derived growth factor D;
Short=PDGF-D;
AltName: Full=Iris-expressed growth factor;
AltName: Full=Spinal cord-derived growth factor B;
Short=SCDGF-B;
Contains:
RecName: Full=Platelet-derived growth factor D, latent form;
Short=PDGFD latent form;
Contains:
RecName: Full=Platelet-derived growth factor D, receptor-binding form;
Short=PDGFD receptor-binding form;
Flags: Precursor;
Name=Pdgfd; Synonyms=Iegf, Scdgfb;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=11162582; DOI=10.1006/bbrc.2000.4187;
Hamada T., Ui-Tei K., Imaki J., Miyata Y.;
"Molecular cloning of SCDGF-B, a novel growth factor homologous to
SCDGF/PDGF-C/fallotein.";
Biochem. Biophys. Res. Commun. 280:733-737(2001).
[2]
IDENTIFICATION OF ISOFORM 2, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=11850188; DOI=10.1016/S0925-4773(01)00625-6;
Hamada T., Ui-Tei K., Imaki J., Takahashi F., Onodera H., Mishima T.,
Miyata Y.;
"The expression of SCDGF/PDGF-C/fallotein and SCDGF-B/PDGF-D in the
rat central nervous system.";
Mech. Dev. 112:161-164(2002).
[3]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12937299; DOI=10.1097/01.ASN.0000083393.00959.02;
Ostendorf T., van Roeyen C.R.C., Peterson J.D., Kunter U., Eitner F.,
Hamad A.J., Chan G., Jia X.-C., Macaluso J., Gazit-Bornstein G.,
Keyt B.A., Lichenstein H.S., LaRochelle W.J., Floege J.;
"A fully human monoclonal antibody (CR002) identifies PDGF-D as a
novel mediator of mesangioproliferative glomerulonephritis.";
J. Am. Soc. Nephrol. 14:2237-2247(2003).
[4]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15611105; DOI=10.1074/jbc.M413570200;
Ray S., Gao C., Wyatt K., Fariss R.N., Bundek A., Zelenka P.,
Wistow G.;
"Platelet-derived growth factor D, tissue-specific expression in the
eye, and a key role in control of lens epithelial cell
proliferation.";
J. Biol. Chem. 280:8494-8502(2005).
-!- FUNCTION: Growth factor that plays an essential role in the
regulation of embryonic development, cell proliferation, cell
migration, survival and chemotaxis. Potent mitogen for cells of
mesenchymal origin. Plays an important role in wound healing.
Induces macrophage recruitment, increased interstitial pressure,
and blood vessel maturation during angiogenesis (By similarity).
May play an important role in control of lens epithelial cell
proliferation. Can initiate events that lead to a mesangial
proliferative glomerulonephritis, including influx of monocytes
and macrophages and production of extracellular matrix.
{ECO:0000250, ECO:0000269|PubMed:12937299,
ECO:0000269|PubMed:15611105}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRB
homodimers, and with heterodimers formed by PDGFRA and PDGFRB (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released by
platelets upon wounding. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9EQT1-1; Sequence=Displayed;
Name=2;
IsoId=Q9EQT1-2; Sequence=VSP_020619;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in
the kidney, adrenal glands, eye and CNS. In the kidney the
localization is confined to arterial and arteriolar vascular
smooth muscle cells and is also detected at low levels in the
glomeruli In the eye in the anterior segment it is localized to
the iris and ciliary body. In the retina localizes intensely to
the outer plexiform layer, which contains photoreceptor axons and
the synaptic layer between photoreceptors and second order
neurons. In the spinal cord, prominently expressed in the
motorneurons. {ECO:0000269|PubMed:11850188,
ECO:0000269|PubMed:12937299, ECO:0000269|PubMed:15611105}.
-!- DEVELOPMENTAL STAGE: Not detected in the spinal cord at E21.
Expressed weakly at postnatal day 1 (P1) and a strong expression
seen at P21 and this continues into adulthood.
{ECO:0000269|PubMed:11850188}.
-!- PTM: Activated by proteolytic cleavage. Proteolytic removal of the
N-terminal CUB domain releasing the core domain is necessary for
unmasking the receptor-binding epitopes of the core domain.
Cleavage after Arg-247 or Arg-249 by urokinase plasminogen
activator gives rise to the active form (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB052170; BAB18920.1; -; mRNA.
PIR; JC7592; JC7592.
RefSeq; NP_076452.1; NM_023962.2. [Q9EQT1-1]
UniGene; Rn.64493; -.
ProteinModelPortal; Q9EQT1; -.
SMR; Q9EQT1; -.
STRING; 10116.ENSRNOP00000039308; -.
PaxDb; Q9EQT1; -.
PRIDE; Q9EQT1; -.
Ensembl; ENSRNOT00000049325; ENSRNOP00000039308; ENSRNOG00000029148. [Q9EQT1-2]
Ensembl; ENSRNOT00000076529; ENSRNOP00000068187; ENSRNOG00000029148. [Q9EQT1-1]
GeneID; 66018; -.
KEGG; rno:66018; -.
UCSC; RGD:621880; rat. [Q9EQT1-1]
CTD; 80310; -.
RGD; 621880; Pdgfd.
eggNOG; ENOG410IGUN; Eukaryota.
eggNOG; ENOG41106HA; LUCA.
GeneTree; ENSGT00390000005171; -.
HOGENOM; HOG000214105; -.
HOVERGEN; HBG057324; -.
InParanoid; Q9EQT1; -.
KO; K05450; -.
OMA; YHSPSVT; -.
OrthoDB; EOG091G08SH; -.
PhylomeDB; Q9EQT1; -.
Reactome; R-RNO-186797; Signaling by PDGF.
PRO; PR:Q9EQT1; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000029148; -.
ExpressionAtlas; Q9EQT1; baseline.
Genevisible; Q9EQT1; RN.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IBA:GO_Central.
GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:RGD.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:RGD.
GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IMP:RGD.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
GO; GO:2000439; P:positive regulation of monocyte extravasation; IMP:RGD.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IBA:GO_Central.
GO; GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:RGD.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
CDD; cd00041; CUB; 1.
CDD; cd00135; PDGF; 1.
Gene3D; 2.10.90.10; -; 1.
Gene3D; 2.60.120.290; -; 1.
InterPro; IPR000859; CUB_dom.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR000072; PDGF/VEGF_dom.
InterPro; IPR027123; PDGFD.
InterPro; IPR035914; Sperma_CUB_dom_sf.
PANTHER; PTHR11633:SF4; PTHR11633:SF4; 1.
Pfam; PF00431; CUB; 1.
Pfam; PF00341; PDGF; 1.
SMART; SM00042; CUB; 1.
SMART; SM00141; PDGF; 1.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS50278; PDGF_2; 1.
2: Evidence at transcript level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Developmental protein; Disulfide bond;
Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted;
Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 370 Platelet-derived growth factor D, latent
form.
/FTId=PRO_0000250196.
CHAIN 250 370 Platelet-derived growth factor D,
receptor-binding form. {ECO:0000255}.
/FTId=PRO_0000250197.
DOMAIN 52 170 CUB. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
SITE 247 248 Cleavage. {ECO:0000255}.
SITE 249 250 Cleavage. {ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 109 131 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 296 296 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DISULFID 302 360 {ECO:0000255|PROSITE-ProRule:PRU00059}.
DISULFID 306 362 {ECO:0000255|PROSITE-ProRule:PRU00059}.
VAR_SEQ 42 47 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_020619.
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


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