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Serglycin (Hematopoietic proteoglycan core protein) (Platelet proteoglycan core protein) (P.PG) (Secretory granule proteoglycan core protein)

 SRGN_HUMAN              Reviewed;         158 AA.
P10124; B2R4L7; Q5VW06;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 3.
07-JUN-2017, entry version 161.
RecName: Full=Serglycin;
AltName: Full=Hematopoietic proteoglycan core protein;
AltName: Full=Platelet proteoglycan core protein;
Short=P.PG;
AltName: Full=Secretory granule proteoglycan core protein;
Flags: Precursor;
Name=SRGN; Synonyms=PRG, PRG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-31.
PubMed=2835370;
Stevens R.L., Avraham S., Gartner M.C., Bruns G.A.P., Austen K.F.,
Weis J.H.;
"Isolation and characterization of a cDNA that encodes the peptide
core of the secretory granule proteoglycan of human promyelocytic
leukemia HL-60 cells.";
J. Biol. Chem. 263:7287-7291(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-31.
PubMed=2798108; DOI=10.1093/nar/17.18.7523;
Stellrecht C.M., Saunders G.F.;
"Nucleotide sequence of a cDNA encoding a hemopoietic proteoglycan
core protein.";
Nucleic Acids Res. 17:7523-7523(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-31.
PubMed=2180935;
Nicodemus C.F., Avraham S., Austen K.F., Purdy S., Jablonski J.,
Stevens R.L.;
"Characterization of the human gene that encodes the peptide core of
secretory granule proteoglycans in promyelocytic leukemia HL-60 cells
and analysis of the translated product.";
J. Biol. Chem. 265:5889-5896(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1377686;
Humphries D.E., Nicodemus C.F., Schiller V., Stevens R.L.;
"The human serglycin gene. Nucleotide sequence and methylation pattern
in human promyelocytic leukemia HL-60 cells and T-lymphoblast Molt-4
cells.";
J. Biol. Chem. 267:13558-13563(1992).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-31.
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-31.
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-31.
TISSUE=Lung;
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).
[9]
PROTEIN SEQUENCE OF 28-158, NUCLEOTIDE SEQUENCE [MRNA] OF 34-158, AND
GLYCOSYLATION AT SER-94 AND SER-96.
PubMed=3402609; DOI=10.1016/0014-5793(88)80298-9;
Alliel P.M., Perin J.-P., Maillet P., Bonnet F., Rosa J.-P.,
Jolles P.;
"Complete amino acid sequence of a human platelet proteoglycan.";
FEBS Lett. 236:123-126(1988).
[10]
PROTEIN SEQUENCE OF 28-93.
PubMed=3214420; DOI=10.1042/bj2551007;
Perin J.-P., Bonnet F., Maillet P., Jolles P.;
"Characterization and N-terminal sequence of human platelet
proteoglycan.";
Biochem. J. 255:1007-1013(1988).
[11]
SUBCELLULAR LOCATION.
PubMed=11154222; DOI=10.1182/blood.V97.2.449;
Schick B.P., Gradowski J.F., San Antonio J.D.;
"Synthesis, secretion, and subcellular localization of serglycin
proteoglycan in human endothelial cells.";
Blood 97:449-458(2001).
[12]
FUNCTION, AND INTERACTION WITH GZMB.
PubMed=11911826; DOI=10.1016/S1074-7613(02)00286-8;
Metkar S.S., Wang B., Aguilar-Santelises M., Raja S.M.,
Uhlin-Hansen L., Podack E., Trapani J.A., Froelich C.J.;
"Cytotoxic cell granule-mediated apoptosis: perforin delivers granzyme
B-serglycin complexes into target cells without plasma membrane pore
formation.";
Immunity 16:417-428(2002).
[13]
INTERACTION WITH GZMB.
PubMed=12388539; DOI=10.1074/jbc.M209607200;
Raja S.M., Wang B., Dantuluri M., Desai U.R., Demeler B., Spiegel K.,
Metkar S.S., Froelich C.J.;
"Cytotoxic cell granule-mediated apoptosis. Characterization of the
macromolecular complex of granzyme B with serglycin.";
J. Biol. Chem. 277:49523-49530(2002).
[14]
SUBCELLULAR LOCATION.
PubMed=15136585; DOI=10.1189/jlb.1003502;
Niemann C.U., Cowland J.B., Klausen P., Askaa J., Calafat J.,
Borregaard N.;
"Localization of serglycin in human neutrophil granulocytes and their
precursors.";
J. Leukoc. Biol. 76:406-415(2004).
[15]
FUNCTION.
PubMed=16420477; DOI=10.1111/j.1742-4658.2005.05085.x;
Zernichow L., Dalen K.T., Prydz K., Winberg J.-O., Kolset S.O.;
"Secretion of proteases in serglycin transfected Madin-Darby canine
kidney cells.";
FEBS J. 273:536-547(2006).
[16]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16870619; DOI=10.1074/jbc.M601061200;
Theocharis A.D., Seidel C., Borset M., Dobra K., Baykov V.,
Labropoulou V., Kanakis I., Dalas E., Karamanos N.K., Sundan A.,
Hjerpe A.;
"Serglycin constitutively secreted by myeloma plasma cells is a potent
inhibitor of bone mineralization in vitro.";
J. Biol. Chem. 281:35116-35128(2006).
-!- FUNCTION: Plays a role in formation of mast cell secretory
granules and mediates storage of various compounds in secretory
vesicles. Required for storage of some proteases in both
connective tissue and mucosal mast cells and for storage of
granzyme B in T-lymphocytes. Plays a role in localizing neutrophil
elastase in azurophil granules of neutrophils. Mediates processing
of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis
by forming a complex with granzyme B which is delivered to cells
by perforin to induce apoptosis. Regulates the secretion of TNF-
alpha and may also regulate protease secretion. Inhibits bone
mineralization. {ECO:0000269|PubMed:11911826,
ECO:0000269|PubMed:16420477, ECO:0000269|PubMed:16870619}.
-!- SUBUNIT: Binds to activated CD44 and to GZMB.
-!- INTERACTION:
P10144:GZMB; NbExp=2; IntAct=EBI-744915, EBI-2505785;
O43765:SGTA; NbExp=8; IntAct=EBI-744915, EBI-347996;
Q9UMX0:UBQLN1; NbExp=5; IntAct=EBI-744915, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-744915, EBI-10173939;
-!- SUBCELLULAR LOCATION: Cytoplasmic granule
{ECO:0000269|PubMed:11154222}. Secreted, extracellular space
{ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:16870619}. Golgi
apparatus {ECO:0000269|PubMed:11154222,
ECO:0000269|PubMed:15136585}. Note=Found in mast cell granules and
in cytoplasmic granules of cytolytic T lymphocytes from where it
is secreted upon cell activation (By similarity). Secreted
constitutively by endothelial cells and macrophages
(PubMed:11154222). Located to Golgi apparatus during neutrophil
differentiation (PubMed:15136585). {ECO:0000250|UniProtKB:P13609,
ECO:0000269|PubMed:11154222, ECO:0000269|PubMed:15136585}.
-!- INDUCTION: By Epstein-Barr virus (EBV).
-!- PTM: O-glycosylated; contains chondroitin sulfate and heparan
sulfate. {ECO:0000250}.
-!- SIMILARITY: Belongs to the serglycin family. {ECO:0000305}.
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EMBL; J03223; AAA60179.1; -; mRNA.
EMBL; X17042; CAA34900.1; -; mRNA.
EMBL; M33651; AAA60322.1; -; Genomic_DNA.
EMBL; M33649; AAA60322.1; JOINED; Genomic_DNA.
EMBL; M33650; AAA60322.1; JOINED; Genomic_DNA.
EMBL; M90058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK311873; BAG34814.1; -; mRNA.
EMBL; AL442635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54309.1; -; Genomic_DNA.
EMBL; BC015516; AAH15516.1; -; mRNA.
EMBL; X12765; CAA31255.1; -; mRNA.
CCDS; CCDS7285.1; -.
PIR; A35183; A28058.
RefSeq; NP_001307982.1; NM_001321053.1.
RefSeq; NP_001307983.1; NM_001321054.1.
RefSeq; NP_002718.2; NM_002727.3.
RefSeq; XP_016871881.1; XM_017016392.1.
UniGene; Hs.1908; -.
ProteinModelPortal; P10124; -.
BioGrid; 111543; 10.
IntAct; P10124; 21.
MINT; MINT-1466608; -.
STRING; 9606.ENSP00000242465; -.
BioMuta; SRGN; -.
DMDM; 269849659; -.
EPD; P10124; -.
MaxQB; P10124; -.
PaxDb; P10124; -.
PeptideAtlas; P10124; -.
PRIDE; P10124; -.
DNASU; 5552; -.
Ensembl; ENST00000242465; ENSP00000242465; ENSG00000122862.
GeneID; 5552; -.
KEGG; hsa:5552; -.
UCSC; uc001joz.4; human.
CTD; 5552; -.
DisGeNET; 5552; -.
GeneCards; SRGN; -.
HGNC; HGNC:9361; SRGN.
HPA; HPA000759; -.
MIM; 177040; gene.
neXtProt; NX_P10124; -.
OpenTargets; ENSG00000122862; -.
PharmGKB; PA33733; -.
eggNOG; ENOG410J42T; Eukaryota.
eggNOG; ENOG4111DTK; LUCA.
GeneTree; ENSGT00390000000885; -.
HOGENOM; HOG000154415; -.
HOVERGEN; HBG008180; -.
InParanoid; P10124; -.
KO; K06849; -.
OMA; QWVRCNP; -.
OrthoDB; EOG091G19FW; -.
PhylomeDB; P10124; -.
TreeFam; TF336310; -.
Reactome; R-HSA-114608; Platelet degranulation.
ChiTaRS; SRGN; human.
GeneWiki; SRGN; -.
GenomeRNAi; 5552; -.
PRO; PR:P10124; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000122862; -.
CleanEx; HS_SRGN; -.
Genevisible; P10124; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0042629; C:mast cell granule; ISS:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0042588; C:zymogen granule; IEA:Ensembl.
GO; GO:0005518; F:collagen binding; IEA:Ensembl.
GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
GO; GO:0008626; P:granzyme-mediated apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0033382; P:maintenance of granzyme B location in T cell secretory granule; ISS:UniProtKB.
GO; GO:0033373; P:maintenance of protease location in mast cell secretory granule; ISS:UniProtKB.
GO; GO:0033364; P:mast cell secretory granule organization; ISS:UniProtKB.
GO; GO:0030502; P:negative regulation of bone mineralization; IDA:UniProtKB.
GO; GO:0050710; P:negative regulation of cytokine secretion; ISS:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0033368; P:protease localization to mast cell secretory granule; IBA:GO_Central.
GO; GO:0016485; P:protein processing; ISS:UniProtKB.
GO; GO:0033371; P:T cell secretory granule organization; ISS:UniProtKB.
InterPro; IPR007455; Serglycin.
Pfam; PF04360; Serglycin; 1.
1: Evidence at protein level;
Apoptosis; Biomineralization; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Golgi apparatus; Polymorphism; Proteoglycan; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 27 {ECO:0000269|PubMed:3214420,
ECO:0000269|PubMed:3402609}.
CHAIN 28 158 Serglycin.
/FTId=PRO_0000026679.
REPEAT 94 95 1.
REPEAT 96 97 2.
REPEAT 98 99 3.
REPEAT 100 101 4.
REPEAT 102 103 5.
REPEAT 104 105 6.
REPEAT 106 107 7.
REPEAT 108 109 8.
REPEAT 110 111 9.
REGION 94 111 9 X 2 AA tandem repeats of [SF]-G.
CARBOHYD 94 94 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000269|PubMed:3402609}.
CARBOHYD 96 96 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000269|PubMed:3402609}.
CARBOHYD 100 100 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000255}.
CARBOHYD 102 102 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000255}.
CARBOHYD 104 104 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000255}.
CARBOHYD 106 106 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000255}.
CARBOHYD 108 108 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000255}.
CARBOHYD 110 110 O-linked (Xyl...) (glycosaminoglycan)
serine. {ECO:0000255}.
DISULFID 40 49 {ECO:0000255}.
VARIANT 31 31 R -> Q (in dbSNP:rs2805910).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2180935,
ECO:0000269|PubMed:2798108,
ECO:0000269|PubMed:2835370,
ECO:0000269|Ref.7}.
/FTId=VAR_032761.
CONFLICT 139 139 N -> S (in Ref. 9; CAA31255).
{ECO:0000305}.
SEQUENCE 158 AA; 17652 MW; BD7767F39FFBC477 CRC64;
MMQKLLKCSR LVLALALILV LESSVQGYPT RRARYQWVRC NPDSNSANCL EEKGPMFELL
PGESNKIPRL RTDLFPKTRI QDLNRIFPLS EDYSGSGFGS GSGSGSGSGS GFLTEMEQDY
QLVDESDAFH DNLRSLDRNL PSDSQDLGQH GLEEDFML


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U1817r CLIA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan, 96T
E1817b ELISA kit Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Ver 96T
E1817r ELISA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan 96T
E1817b ELISA Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Versican 96T
U1817r CLIA Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan,Versi 96T
U1817b CLIA kit Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Vers 96T
U1817h CLIA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Homo sapiens,Human,Large fibroblast proteoglycan,PG-M,VCAN,Ver 96T


 

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