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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_HUMAN             Reviewed;         370 AA.
Q9GZP0; A8K9T6; Q9BWV5;
19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 142.
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; ORFNames=MSTP036, UNQ1899/PRO4345;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND TISSUE
SPECIFICITY.
PubMed=11331881; DOI=10.1038/35074588;
Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H.,
Alitalo K., Eriksson U.;
"PDGF-D is a specific, protease-activated ligand for the PDGF beta-
receptor.";
Nat. Cell Biol. 3:512-516(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=11331882; DOI=10.1038/35074593;
LaRochelle W.J., Jeffers M., McDonald W.F., Chillakuru R.A.,
Giese N.A., Lokker N.A., Sullivan C., Boldog F.L., Yang M., Vernet C.,
Burgess C.E., Fernandez E., Deegler L.L., Rittman B., Shimkets J.,
Shimkets R.A., Rothberg J.M., Lichenstein H.S.;
"PDGF D, a novel protease-activated growth factor.";
Nat. Cell Biol. 3:517-521(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Iris;
PubMed=12107412;
Wistow G., Bernstein S.L., Ray S., Wyatt M.K., Behal A.,
Touchman J.W., Bouffard G., Smith D., Peterson K.;
"Expressed sequence tag analysis of adult human iris for the NEIBank
project: steroid-response factors and similarities with retinal
pigment epithelium.";
Mol. Vis. 8:185-195(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Aorta;
Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S.,
Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J.,
Cao H.Q., Zhao Y., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q.,
Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.;
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 64-369, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=12427128; DOI=10.1046/j.1523-1755.2002.00662.x;
Changsirikulchai S., Hudkins K.L., Goodpaster T.A., Volpone J.,
Topouzis S., Gilbertson D.G., Alpers C.E.;
"Platelet-derived growth factor-D expression in developing and mature
human kidneys.";
Kidney Int. 62:2043-2054(2002).
[11]
TISSUE SPECIFICITY.
PubMed=11342471; DOI=10.1161/01.CIR.103.18.2242;
Uutela M., Lauren J., Bergsten E., Li X., Horelli-Kuitunen N.,
Eriksson U., Alitalo K.;
"Chromosomal location, exon structure, and vascular expression
patterns of the human PDGFC and PDGFC genes.";
Circulation 103:2242-2247(2001).
[12]
TISSUE SPECIFICITY.
PubMed=11980634;
LaRochelle W.J., Jeffers M., Corvalan J.R.F., Jia X.-C., Feng X.,
Vanegas S., Vickroy J.D., Yang X.-D., Chen F., Gazit G., Mayotte J.,
Macaluso J., Rittman B., Wu F., Dhanabal M., Herrmann J.,
Lichenstein H.S.;
"Platelet-derived growth factor D: tumorigenicity in mice and
dysregulated expression in human cancer.";
Cancer Res. 62:2468-2473(2002).
[13]
TISSUE SPECIFICITY.
PubMed=14514732; DOI=10.1097/01.ASN.0000089828.73014.C8;
Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G.,
Ophascharoensuk V., Truong L., Johnson R.J., Alpers C.E.;
"Obstructive uropathy in mice and humans: potential role for PDGF-D in
the progression of tubulointerstitial injury.";
J. Am. Soc. Nephrol. 14:2544-2555(2003).
[14]
FUNCTION.
PubMed=15271796; DOI=10.1182/blood-2004-04-1485;
Uutela M., Wirzenius M., Paavonen K., Rajantie I., He Y., Karpanen T.,
Lohela M., Wiig H., Salven P., Pajusola K., Eriksson U., Alitalo K.;
"PDGF-D induces macrophage recruitment, increased interstitial
pressure, and blood vessel maturation during angiogenesis.";
Blood 104:3198-3204(2004).
[15]
REVIEW.
PubMed=16279938; DOI=10.1111/j.1742-4658.2005.04989.x;
Reigstad L.J., Varhaug J.E., Lillehaug J.R.;
"Structural and functional specificities of PDGF-C and PDGF-D, the
novel members of the platelet-derived growth factors family.";
FEBS J. 272:5723-5741(2005).
[16]
TISSUE SPECIFICITY, PTM, AND MUTAGENESIS OF ARG-247 AND ARG-249.
PubMed=15988036; DOI=10.1128/MCB.25.14.6279-6288.2005;
Ustach C.V., Kim H.-R.C.;
"Platelet-derived growth factor D is activated by urokinase
plasminogen activator in prostate carcinoma cells.";
Mol. Cell. Biol. 25:6279-6288(2005).
[17]
REVIEW.
PubMed=20434526; DOI=10.1016/j.bbcan.2010.04.003;
Wang Z., Ahmad A., Li Y., Kong D., Azmi A.S., Banerjee S.,
Sarkar F.H.;
"Emerging roles of PDGF-D signaling pathway in tumor development and
progression.";
Biochim. Biophys. Acta 1806:122-130(2010).
[18]
VARIANT [LARGE SCALE ANALYSIS] TYR-202.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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. Can initiate
events that lead to a mesangial proliferative glomerulonephritis,
including influx of monocytes and macrophages and production of
extracellular matrix (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:15271796}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRB
homodimers, and with heterodimers formed by PDGFRA and PDGFRB.
{ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:11331882}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11331882}.
Note=Released by platelets upon wounding.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long, SCDGF-B-L;
IsoId=Q9GZP0-1; Sequence=Displayed;
Name=2; Synonyms=Short, SCDGF-B-S;
IsoId=Q9GZP0-2; Sequence=VSP_020615;
-!- TISSUE SPECIFICITY: Expressed at high levels in the heart,
pancreas, adrenal gland and ovary and at low levels in placenta,
liver, kidney, prostate, testis, small intestine, spleen and
colon. In the kidney, expressed by the visceral epithelial cells
of the glomeruli. A widespread expression is also seen in the
medial smooth muscle cells of arteries and arterioles, as well as
in smooth muscle cells of vasa rectae in the medullary area.
Expressed in the adventitial connective tissue surrounding the
suprarenal artery. In chronic obstructive nephropathy, a
persistent expression is seen in glomerular visceral epithelial
cells and vascular smooth muscle cells, as well as de novo
expression by periglomerular interstitial cells and by some
neointimal cells of atherosclerotic vessels. Expression in normal
prostate is seen preferentially in the mesenchyme of the gland
while expression is increased and more profuse in prostate
carcinoma. Expressed in many ovarian, lung, renal and brain
cancer-derived cell lines. {ECO:0000269|PubMed:11331881,
ECO:0000269|PubMed:11331882, ECO:0000269|PubMed:11342471,
ECO:0000269|PubMed:11980634, ECO:0000269|PubMed:12427128,
ECO:0000269|PubMed:14514732, ECO:0000269|PubMed:15988036}.
-!- DEVELOPMENTAL STAGE: Not detectable in the earliest stages of
glomerulogenesis, and not detected in the metanephric blastema or
surrounding cortical interstitial cells. In later stages of
glomerulogenesis, localized to epithelial cells transitioning from
the early developing nephrons of the comma- and S-shaped stages to
the visceral epithelial cells of differentiated glomeruli. In the
developing pelvis, expressed at the basement membrane of immature
collecting ducts and by presumptive fibroblastic cells in the
interstitium. {ECO:0000269|PubMed:12427128}.
-!- 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.
-!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
{ECO:0000305}.
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EMBL; AB033832; BAB18903.1; -; mRNA.
EMBL; AF336376; AAK56136.1; -; mRNA.
EMBL; AF335584; AAK38840.1; -; mRNA.
EMBL; AY027517; AAK20081.1; -; mRNA.
EMBL; AY027518; AAK20082.1; -; mRNA.
EMBL; AF113216; AAG39287.1; -; mRNA.
EMBL; AY359116; AAQ89474.1; -; mRNA.
EMBL; AK292801; BAF85490.1; -; mRNA.
EMBL; CH471065; EAW67045.1; -; Genomic_DNA.
EMBL; BC030645; AAH30645.1; -; mRNA.
CCDS; CCDS41703.1; -. [Q9GZP0-1]
CCDS; CCDS8326.1; -. [Q9GZP0-2]
PIR; JC7591; JC7591.
RefSeq; NP_079484.1; NM_025208.4. [Q9GZP0-1]
RefSeq; NP_149126.1; NM_033135.3. [Q9GZP0-2]
UniGene; Hs.352298; -.
ProteinModelPortal; Q9GZP0; -.
SMR; Q9GZP0; -.
BioGrid; 123223; 21.
ComplexPortal; CPX-2880; Platelet-derived growth factor DD complex.
ComplexPortal; CPX-2889; PDGF receptor beta - PDGF-DD complex.
ComplexPortal; CPX-2890; PDGF receptor alpha-beta - PDGF-DD complex.
STRING; 9606.ENSP00000376865; -.
DrugBank; DB05139; CR002.
DrugBank; DB05465; MLN-518.
iPTMnet; Q9GZP0; -.
PhosphoSitePlus; Q9GZP0; -.
BioMuta; PDGFD; -.
DMDM; 74717921; -.
PaxDb; Q9GZP0; -.
PeptideAtlas; Q9GZP0; -.
PRIDE; Q9GZP0; -.
ProteomicsDB; 80102; -.
ProteomicsDB; 80103; -. [Q9GZP0-2]
DNASU; 80310; -.
Ensembl; ENST00000302251; ENSP00000302193; ENSG00000170962. [Q9GZP0-2]
Ensembl; ENST00000393158; ENSP00000376865; ENSG00000170962. [Q9GZP0-1]
GeneID; 80310; -.
KEGG; hsa:80310; -.
UCSC; uc001php.4; human. [Q9GZP0-1]
CTD; 80310; -.
DisGeNET; 80310; -.
EuPathDB; HostDB:ENSG00000170962.12; -.
GeneCards; PDGFD; -.
HGNC; HGNC:30620; PDGFD.
HPA; HPA046183; -.
HPA; HPA066271; -.
MIM; 609673; gene.
neXtProt; NX_Q9GZP0; -.
OpenTargets; ENSG00000170962; -.
PharmGKB; PA134892327; -.
eggNOG; ENOG410IGUN; Eukaryota.
eggNOG; ENOG41106HA; LUCA.
GeneTree; ENSGT00940000159575; -.
HOGENOM; HOG000261610; -.
HOVERGEN; HBG057324; -.
InParanoid; Q9GZP0; -.
KO; K05450; -.
OMA; LYRKEET; -.
OrthoDB; EOG091G08SH; -.
PhylomeDB; Q9GZP0; -.
TreeFam; TF332130; -.
Reactome; R-HSA-186797; Signaling by PDGF.
SignaLink; Q9GZP0; -.
ChiTaRS; PDGFD; human.
GeneWiki; PDGFD; -.
GenomeRNAi; 80310; -.
PMAP-CutDB; Q9GZP0; -.
PRO; PR:Q9GZP0; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000170962; Expressed in 199 organ(s), highest expression level in adrenal gland.
CleanEx; HS_PDGFD; -.
ExpressionAtlas; Q9GZP0; baseline and differential.
Genevisible; Q9GZP0; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
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:0030335; P:positive regulation of cell migration; IBA:GO_Central.
GO; GO:0008284; P:positive regulation of cell proliferation; IBA:GO_Central.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
GO; GO:2000439; P:positive regulation of monocyte extravasation; IEA:Ensembl.
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; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
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.
SUPFAM; SSF49854; SSF49854; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS01180; CUB; 1.
PROSITE; PS50278; PDGF_2; 1.
1: Evidence at protein level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Developmental protein; Disulfide bond;
Glycoprotein; Growth factor; Mitogen; Polymorphism; Proto-oncogene;
Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 370 Platelet-derived growth factor D, latent
form.
/FTId=PRO_0000250188.
CHAIN 250 370 Platelet-derived growth factor D,
receptor-binding form. {ECO:0000255}.
/FTId=PRO_0000250189.
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:0000303|PubMed:11162582,
ECO:0000303|PubMed:12107412,
ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_020615.
VARIANT 190 190 I -> V (in dbSNP:rs35045740).
/FTId=VAR_051563.
VARIANT 202 202 D -> Y (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036418.
MUTAGEN 247 247 R->A: Abolishes cleavage into active
form; when associated with A-249.
{ECO:0000269|PubMed:15988036}.
MUTAGEN 249 249 R->A: Abolishes cleavage into active
form; when associated with A-247.
{ECO:0000269|PubMed:15988036}.
SEQUENCE 370 AA; 42848 MW; D387F485E7BB7674 CRC64;
MHRLIFVYTL ICANFCSCRD TSATPQSASI KALRNANLRR DESNHLTDLY RRDETIQVKG
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


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