PDGFD_HUMAN
ID PDGFD_HUMAN Reviewed; 370 AA.
AC Q9GZP0; A8K9T6; Q9BWV5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
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; ORFNames=MSTP036, UNQ1899/PRO4345;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=11331881; DOI=10.1038/35074588;
RA Bergsten E., Uutela M., Li X., Pietras K., Oestman A., Heldin C.-H.,
RA Alitalo K., Eriksson U.;
RT "PDGF-D is a specific, protease-activated ligand for the PDGF beta-
RT receptor.";
RL Nat. Cell Biol. 3:512-516(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11331882; DOI=10.1038/35074593;
RA LaRochelle W.J., Jeffers M., McDonald W.F., Chillakuru R.A., Giese N.A.,
RA Lokker N.A., Sullivan C., Boldog F.L., Yang M., Vernet C., Burgess C.E.,
RA Fernandez E., Deegler L.L., Rittman B., Shimkets J., Shimkets R.A.,
RA Rothberg J.M., Lichenstein H.S.;
RT "PDGF D, a novel protease-activated growth factor.";
RL Nat. Cell Biol. 3:517-521(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Iris;
RX PubMed=12107412;
RA Wistow G., Bernstein S.L., Ray S., Wyatt M.K., Behal A., Touchman J.W.,
RA Bouffard G., Smith D., Peterson K.;
RT "Expressed sequence tag analysis of adult human iris for the NEIBank
RT project: steroid-response factors and similarities with retinal pigment
RT epithelium.";
RL Mol. Vis. 8:185-195(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Aorta;
RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 64-369, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=12427128; DOI=10.1046/j.1523-1755.2002.00662.x;
RA Changsirikulchai S., Hudkins K.L., Goodpaster T.A., Volpone J.,
RA Topouzis S., Gilbertson D.G., Alpers C.E.;
RT "Platelet-derived growth factor-D expression in developing and mature human
RT kidneys.";
RL Kidney Int. 62:2043-2054(2002).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=11342471; DOI=10.1161/01.cir.103.18.2242;
RA Uutela M., Lauren J., Bergsten E., Li X., Horelli-Kuitunen N., Eriksson U.,
RA Alitalo K.;
RT "Chromosomal location, exon structure, and vascular expression patterns of
RT the human PDGFC and PDGFC genes.";
RL Circulation 103:2242-2247(2001).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=11980634;
RA LaRochelle W.J., Jeffers M., Corvalan J.R.F., Jia X.-C., Feng X.,
RA Vanegas S., Vickroy J.D., Yang X.-D., Chen F., Gazit G., Mayotte J.,
RA Macaluso J., Rittman B., Wu F., Dhanabal M., Herrmann J., Lichenstein H.S.;
RT "Platelet-derived growth factor D: tumorigenicity in mice and dysregulated
RT expression in human cancer.";
RL Cancer Res. 62:2468-2473(2002).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=14514732; DOI=10.1097/01.asn.0000089828.73014.c8;
RA Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G., Ophascharoensuk V.,
RA Truong L., Johnson R.J., Alpers C.E.;
RT "Obstructive uropathy in mice and humans: potential role for PDGF-D in the
RT progression of tubulointerstitial injury.";
RL J. Am. Soc. Nephrol. 14:2544-2555(2003).
RN [14]
RP FUNCTION.
RX PubMed=15271796; DOI=10.1182/blood-2004-04-1485;
RA Uutela M., Wirzenius M., Paavonen K., Rajantie I., He Y., Karpanen T.,
RA Lohela M., Wiig H., Salven P., Pajusola K., Eriksson U., Alitalo K.;
RT "PDGF-D induces macrophage recruitment, increased interstitial pressure,
RT and blood vessel maturation during angiogenesis.";
RL Blood 104:3198-3204(2004).
RN [15]
RP REVIEW.
RX PubMed=16279938; DOI=10.1111/j.1742-4658.2005.04989.x;
RA Reigstad L.J., Varhaug J.E., Lillehaug J.R.;
RT "Structural and functional specificities of PDGF-C and PDGF-D, the novel
RT members of the platelet-derived growth factors family.";
RL FEBS J. 272:5723-5741(2005).
RN [16]
RP TISSUE SPECIFICITY, PTM, AND MUTAGENESIS OF ARG-247 AND ARG-249.
RX PubMed=15988036; DOI=10.1128/mcb.25.14.6279-6288.2005;
RA Ustach C.V., Kim H.-R.C.;
RT "Platelet-derived growth factor D is activated by urokinase plasminogen
RT activator in prostate carcinoma cells.";
RL Mol. Cell. Biol. 25:6279-6288(2005).
RN [17]
RP REVIEW.
RX PubMed=20434526; DOI=10.1016/j.bbcan.2010.04.003;
RA Wang Z., Ahmad A., Li Y., Kong D., Azmi A.S., Banerjee S., Sarkar F.H.;
RT "Emerging roles of PDGF-D signaling pathway in tumor development and
RT progression.";
RL Biochim. Biophys. Acta 1806:122-130(2010).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] TYR-202.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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, ECO:0000269|PubMed:11331881,
CC ECO:0000269|PubMed:15271796}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PDGFRB homodimers,
CC and with heterodimers formed by PDGFRA and PDGFRB.
CC {ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:11331882}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11331882}.
CC Note=Released by platelets upon wounding.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long, SCDGF-B-L;
CC IsoId=Q9GZP0-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, SCDGF-B-S;
CC IsoId=Q9GZP0-2; Sequence=VSP_020615;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the heart, pancreas,
CC adrenal gland and ovary and at low levels in placenta, liver, kidney,
CC prostate, testis, small intestine, spleen and colon. In the kidney,
CC expressed by the visceral epithelial cells of the glomeruli. A
CC widespread expression is also seen in the medial smooth muscle cells of
CC arteries and arterioles, as well as in smooth muscle cells of vasa
CC rectae in the medullary area. Expressed in the adventitial connective
CC tissue surrounding the suprarenal artery. In chronic obstructive
CC nephropathy, a persistent expression is seen in glomerular visceral
CC epithelial cells and vascular smooth muscle cells, as well as de novo
CC expression by periglomerular interstitial cells and by some neointimal
CC cells of atherosclerotic vessels. Expression in normal prostate is seen
CC preferentially in the mesenchyme of the gland while expression is
CC increased and more profuse in prostate carcinoma. Expressed in many
CC ovarian, lung, renal and brain cancer-derived cell lines.
CC {ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:11331882,
CC ECO:0000269|PubMed:11342471, ECO:0000269|PubMed:11980634,
CC ECO:0000269|PubMed:12427128, ECO:0000269|PubMed:14514732,
CC ECO:0000269|PubMed:15988036}.
CC -!- DEVELOPMENTAL STAGE: Not detectable in the earliest stages of
CC glomerulogenesis, and not detected in the metanephric blastema or
CC surrounding cortical interstitial cells. In later stages of
CC glomerulogenesis, localized to epithelial cells transitioning from the
CC early developing nephrons of the comma- and S-shaped stages to the
CC visceral epithelial cells of differentiated glomeruli. In the
CC developing pelvis, expressed at the basement membrane of immature
CC collecting ducts and by presumptive fibroblastic cells in the
CC interstitium. {ECO:0000269|PubMed:12427128}.
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.
CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family.
CC {ECO:0000305}.
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DR EMBL; AB033832; BAB18903.1; -; mRNA.
DR EMBL; AF336376; AAK56136.1; -; mRNA.
DR EMBL; AF335584; AAK38840.1; -; mRNA.
DR EMBL; AY027517; AAK20081.1; -; mRNA.
DR EMBL; AY027518; AAK20082.1; -; mRNA.
DR EMBL; AF113216; AAG39287.1; -; mRNA.
DR EMBL; AY359116; AAQ89474.1; -; mRNA.
DR EMBL; AK292801; BAF85490.1; -; mRNA.
DR EMBL; CH471065; EAW67045.1; -; Genomic_DNA.
DR EMBL; BC030645; AAH30645.1; -; mRNA.
DR CCDS; CCDS41703.1; -. [Q9GZP0-1]
DR CCDS; CCDS8326.1; -. [Q9GZP0-2]
DR PIR; JC7591; JC7591.
DR RefSeq; NP_079484.1; NM_025208.4. [Q9GZP0-1]
DR RefSeq; NP_149126.1; NM_033135.3. [Q9GZP0-2]
DR AlphaFoldDB; Q9GZP0; -.
DR SMR; Q9GZP0; -.
DR BioGRID; 123223; 22.
DR ComplexPortal; CPX-2880; Platelet-derived growth factor DD complex.
DR ComplexPortal; CPX-2889; PDGF receptor beta - PDGF-DD complex.
DR ComplexPortal; CPX-2890; PDGF receptor alpha-beta - PDGF-DD complex.
DR IntAct; Q9GZP0; 19.
DR STRING; 9606.ENSP00000376865; -.
DR DrugBank; DB05139; CR002.
DR DrugBank; DB05465; Tandutinib.
DR GlyGen; Q9GZP0; 5 sites, 3 O-linked glycans (4 sites).
DR iPTMnet; Q9GZP0; -.
DR PhosphoSitePlus; Q9GZP0; -.
DR BioMuta; PDGFD; -.
DR DMDM; 74717921; -.
DR MassIVE; Q9GZP0; -.
DR PaxDb; Q9GZP0; -.
DR PeptideAtlas; Q9GZP0; -.
DR PRIDE; Q9GZP0; -.
DR ProteomicsDB; 80102; -. [Q9GZP0-1]
DR ProteomicsDB; 80103; -. [Q9GZP0-2]
DR Antibodypedia; 31835; 285 antibodies from 27 providers.
DR DNASU; 80310; -.
DR Ensembl; ENST00000302251.9; ENSP00000302193.5; ENSG00000170962.13. [Q9GZP0-2]
DR Ensembl; ENST00000393158.7; ENSP00000376865.2; ENSG00000170962.13. [Q9GZP0-1]
DR GeneID; 80310; -.
DR KEGG; hsa:80310; -.
DR MANE-Select; ENST00000393158.7; ENSP00000376865.2; NM_025208.5; NP_079484.1.
DR UCSC; uc001php.4; human. [Q9GZP0-1]
DR CTD; 80310; -.
DR DisGeNET; 80310; -.
DR GeneCards; PDGFD; -.
DR HGNC; HGNC:30620; PDGFD.
DR HPA; ENSG00000170962; Tissue enhanced (adrenal gland, ovary).
DR MIM; 609673; gene.
DR neXtProt; NX_Q9GZP0; -.
DR OpenTargets; ENSG00000170962; -.
DR PharmGKB; PA134892327; -.
DR VEuPathDB; HostDB:ENSG00000170962; -.
DR eggNOG; ENOG502QPQY; Eukaryota.
DR GeneTree; ENSGT00940000159575; -.
DR HOGENOM; CLU_037859_1_0_1; -.
DR InParanoid; Q9GZP0; -.
DR OMA; FVYTLVC; -.
DR OrthoDB; 962163at2759; -.
DR PhylomeDB; Q9GZP0; -.
DR TreeFam; TF332130; -.
DR PathwayCommons; Q9GZP0; -.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR SignaLink; Q9GZP0; -.
DR BioGRID-ORCS; 80310; 10 hits in 1072 CRISPR screens.
DR ChiTaRS; PDGFD; human.
DR GeneWiki; PDGFD; -.
DR GenomeRNAi; 80310; -.
DR Pharos; Q9GZP0; Tbio.
DR PRO; PR:Q9GZP0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9GZP0; protein.
DR Bgee; ENSG00000170962; Expressed in periodontal ligament and 169 other tissues.
DR ExpressionAtlas; Q9GZP0; baseline and differential.
DR Genevisible; Q9GZP0; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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; IEA:Ensembl.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
DR GO; GO:2000439; P:positive regulation of monocyte extravasation; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
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 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Developmental protein; Disulfide bond; Glycoprotein; Growth factor;
KW Mitogen; Proto-oncogene; 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_0000250188"
FT CHAIN 250..370
FT /note="Platelet-derived growth factor D, receptor-binding
FT form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000250189"
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:0000303|PubMed:11162582,
FT ECO:0000303|PubMed:12107412, ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_020615"
FT VARIANT 190
FT /note="I -> V (in dbSNP:rs35045740)"
FT /id="VAR_051563"
FT VARIANT 202
FT /note="D -> Y (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036418"
FT MUTAGEN 247
FT /note="R->A: Abolishes cleavage into active form; when
FT associated with A-249."
FT /evidence="ECO:0000269|PubMed:15988036"
FT MUTAGEN 249
FT /note="R->A: Abolishes cleavage into active form; when
FT associated with A-247."
FT /evidence="ECO:0000269|PubMed:15988036"
SQ 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
