GENTAUR Molecular Products.

 PDGFD_MOUSE             Reviewed;         370 AA.
 Q925I7; Q3URF6; Q8K2L3; Q9D1L8;
 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
 01-DEC-2001, sequence version 1.
 28-FEB-2018, entry version 119.
 RecName: Full=Platelet-derived growth factor D;
          Short=PDGF-D;
 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=Scdgfb;
 Mus musculus (Mouse).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
 Muroidea; Muridae; Murinae; Mus; Mus.
 NCBI_TaxID=10090;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
 STRAIN=BALB/cJ;
 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).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
 PubMed=12890490; DOI=10.1016/S0006-291X(03)01346-9;
 Zhuo Y., Hoyle G.W., Zhang J., Morris G., Lasky J.A.;
 "A novel murine PDGF-D splicing variant results in significant
 differences in peptide expression and function.";
 Biochem. Biophys. Res. Commun. 308:126-132(2003).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
 STRAIN=C57BL/6J; TISSUE=Hippocampus;
 PubMed=16141072; DOI=10.1126/science.1112014;
 Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
 Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
 Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
 Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
 Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
 Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
 Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
 Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
 di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
 Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
 Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
 Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
 Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
 Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
 Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
 Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
 Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
 Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
 Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
 Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
 Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
 Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
 Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
 Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
 Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
 Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
 Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
 Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
 Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
 Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
 Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
 Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
 Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
 Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
 Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
 Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
 Hayashizaki Y.;
 "The transcriptional landscape of the mammalian genome.";
 Science 309:1559-1563(2005).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
 STRAIN=FVB/N; TISSUE=Mammary gland;
 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).
 [5]
 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).
 [6]
 FUNCTION.
 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).
 [7]
 REVIEW.
 PubMed=15207812; DOI=10.1016/j.cytogfr.2004.03.003;
 Tallquist M., Kazlauskas A.;
 "PDGF signaling in cells and mice.";
 Cytokine Growth Factor Rev. 15:205-213(2004).
 [8]
 FUNCTION, AND TISSUE SPECIFICITY.
 PubMed=14747375; DOI=10.1097/01.ASN.0000108522.79652.63;
 Hudkins K.L., Gilbertson D.G., Carling M., Taneda S., Hughes S.D.,
 Holdren M.S., Palmer T.E., Topouzis S., Haran A.C., Feldhaus A.L.,
 Alpers C.E.;
 "Exogenous PDGF-D is a potent mesangial cell mitogen and causes a
 severe mesangial proliferative glomerulopathy.";
 J. Am. Soc. Nephrol. 15:286-298(2004).
 [9]
 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).
 [10]
 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).
 -!- 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 (By
     similarity). Has oncogenic potential and can induce tumor
     formation. 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. {ECO:0000250,
     ECO:0000269|PubMed:11980634, ECO:0000269|PubMed:14747375,
     ECO:0000269|PubMed:15271796}.
 -!- 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=3;
     Name=1; Synonyms=Long;
       IsoId=Q925I7-1; Sequence=Displayed;
     Name=2;
       IsoId=Q925I7-2; Sequence=VSP_020616;
     Name=3; Synonyms=Short;
       IsoId=Q925I7-3; Sequence=VSP_020617, VSP_020618;
 -!- TISSUE SPECIFICITY: Expressed at high levels in developing heart,
     lung, kidney and some muscle derivatives. Moderately expressed in
     liver, brain and testis. In the kidney, localized to glomerular
     mesangial cells and vascular smooth muscle cells. Up-regulated in
     areas of renal fibrosis. In mice with unilateral ureteral
     obstruction, expressed in interstitial cells at day 4, with an
     increased to maximal expression at day 14.
     {ECO:0000269|PubMed:11331881, ECO:0000269|PubMed:12890490,
     ECO:0000269|PubMed:14514732, ECO:0000269|PubMed:14747375}.
 -!- 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}.
 -----------------------------------------------------------------------
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 EMBL; AF335583; AAK38839.1; -; mRNA.
 EMBL; AK003359; BAB22735.2; -; mRNA.
 EMBL; AK141551; BAE24732.1; -; mRNA.
 EMBL; BC030896; AAH30896.1; -; mRNA.
 CCDS; CCDS22801.1; -. [Q925I7-1]
 RefSeq; NP_082200.1; NM_027924.2. [Q925I7-1]
 RefSeq; XP_006509948.1; XM_006509885.3.
 RefSeq; XP_006509949.1; XM_006509886.3.
 UniGene; Mm.390122; -.
 ProteinModelPortal; Q925I7; -.
 SMR; Q925I7; -.
 STRING; 10090.ENSMUSP00000128388; -.
 PhosphoSitePlus; Q925I7; -.
 PaxDb; Q925I7; -.
 PeptideAtlas; Q925I7; -.
 PRIDE; Q925I7; -.
 Ensembl; ENSMUST00000058692; ENSMUSP00000056240; ENSMUSG00000032006. [Q925I7-2]
 Ensembl; ENSMUST00000168039; ENSMUSP00000128388; ENSMUSG00000032006. [Q925I7-1]
 Ensembl; ENSMUST00000214892; ENSMUSP00000149162; ENSMUSG00000032006. [Q925I7-3]
 GeneID; 71785; -.
 KEGG; mmu:71785; -.
 UCSC; uc009oby.1; mouse. [Q925I7-1]
 UCSC; uc009obz.1; mouse. [Q925I7-2]
 UCSC; uc012gnq.1; mouse. [Q925I7-3]
 CTD; 80310; -.
 MGI; MGI:1919035; Pdgfd.
 eggNOG; ENOG410IGUN; Eukaryota.
 eggNOG; ENOG41106HA; LUCA.
 GeneTree; ENSGT00390000005171; -.
 HOGENOM; HOG000261610; -.
 HOVERGEN; HBG057324; -.
 InParanoid; Q925I7; -.
 KO; K05450; -.
 OMA; YHSPSVT; -.
 OrthoDB; EOG091G08SH; -.
 PhylomeDB; Q925I7; -.
 TreeFam; TF332130; -.
 Reactome; R-MMU-186797; Signaling by PDGF.
 PRO; PR:Q925I7; -.
 Proteomes; UP000000589; Chromosome 9.
 Bgee; ENSMUSG00000032006; -.
 CleanEx; MM_PDGFD; -.
 Genevisible; Q925I7; MM.
 GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
 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; ISO:MGI.
 GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
 GO; GO:0009987; P:cellular process; ISO:MGI.
 GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
 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; IDA:MGI.
 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; Proto-oncogene;
 Reference proteome; Secreted; Signal.
 SIGNAL        1     23       {ECO:0000255}.
 CHAIN        24    370       Platelet-derived growth factor D, latent
                              form.
                              /FTId=PRO_0000250190.
 CHAIN       250    370       Platelet-derived growth factor D,
                              receptor-binding form. {ECO:0000255}.
                              /FTId=PRO_0000250191.
 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:16141072}.
                              /FTId=VSP_020616.
 VAR_SEQ     258    261       VDLD -> GIEV (in isoform 3).
                              {ECO:0000303|PubMed:12890490,
                              ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_020617.
 VAR_SEQ     262    370       Missing (in isoform 3).
                              {ECO:0000303|PubMed:12890490,
                              ECO:0000303|PubMed:15489334}.
                              /FTId=VSP_020618.
 CONFLICT    173    173       F -> S (in Ref. 4; AAH30896).
                              {ECO:0000305}.
 SEQUENCE   370 AA;  42809 MW;  9E80B4CF6813BFBE CRC64;
 MQRLVLVSIL LCANFSCYPD TFATPQRASI KALRNANLRR DESNHLTDLY QREENIQVTS
 NGHVQSPRFP NSYPRNLLLT WWLRSQEKTR IQLSFDHQFG LEEAENDICR YDFVEVEEVS
 ESSTVVRGRW CGHKEIPPRI TSRTNQIKIT FKSDDYFVAK PGFKIYYSFV EDFQPEAASE
 TNWESVTSSF SGVSYHSPSI TDPTLTADAL DKTVAEFDTV EDLLKHFNPV SWQDDLENLY
 LDTPHYRGRS YHDRKSKVDL DRLNDDVKRY SCTPRNHSVN LREELKLTNA VFFPRCLLVQ
 RCGGNCGCGT VNWKSCTCSS GKTVKKYHEV LKFEPGHFKR RGKAKNMALV DIQLDHHERC
 DCICSSRPPR

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