VTNC_MOUSE
ID VTNC_MOUSE Reviewed; 478 AA.
AC P29788; Q5SYG4; Q8VII4; Q91X32; Q9D080;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Vitronectin;
DE Short=VN;
DE AltName: Full=S-protein;
DE AltName: Full=Serum-spreading factor;
DE Flags: Precursor;
GN Name=Vtn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7505250; DOI=10.1016/0378-1119(93)90113-h;
RA Seiffert D., Poenninger J., Binder B.R.;
RT "Organization of the gene encoding mouse vitronectin.";
RL Gene 134:303-304(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1719529; DOI=10.1073/pnas.88.21.9402;
RA Seiffert D., Keeton M., Eguchi Y., Sawdey M., Loskutoff D.J.;
RT "Detection of vitronectin mRNA in tissues and cells of the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9402-9406(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Ehrlich H.J., Richter B., von der Ahe D., Preissner K.T.;
RT "Primary structure of vitronectins and homology with other proteins.";
RL (In) Preissner K.T., Rosenblatt S., Kost C., Wegerhoff J., Mosher D.F.
RL (eds.);
RL Biology of vitronectins, pp.1-1, Elsevier, Amsterdam (1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Lai D.-Z.;
RT "Construction of a robust CHO cell-line for biopharmaceutical production.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Gall bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [9]
RP PROTEIN SEQUENCE OF 20-44.
RX PubMed=1372829; DOI=10.1016/0167-4838(92)90417-c;
RA Nakashima N., Miyazaki K., Ishikawa M., Yatohgo T., Ogawa H., Uchibori H.,
RA Matsumoto I., Seno N., Hayashi M.;
RT "Vitronectin diversity in evolution but uniformity in ligand binding and
RT size of the core polypeptide.";
RL Biochim. Biophys. Acta 1120:1-10(1992).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-241.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Vitronectin is a cell adhesion and spreading factor found in
CC serum and tissues. Vitronectin interact with glycosaminoglycans and
CC proteoglycans. Is recognized by certain members of the integrin family
CC and serves as a cell-to-substrate adhesion molecule. Inhibitor of the
CC membrane-damaging effect of the terminal cytolytic complement pathway.
CC -!- SUBUNIT: Interacts with SERPINE1/PAI1, insulin and C1QBP.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- DOMAIN: The SMB domain mediates interaction with SERPINE1/PAI1. The
CC heparin-binding domain mediates interaction with insulin (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:P04004}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250}.
CC -!- PTM: It has been suggested that the active SMB domain may be permitted
CC considerable disulfide bond heterogeneity or variability, thus two
CC alternate disulfide patterns based on 3D structures are described with
CC 1 disulfide bond conserved in both.
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DR EMBL; X72091; CAA50981.1; -; Genomic_DNA.
DR EMBL; M77123; AAA40558.1; -; mRNA.
DR EMBL; X63003; CAA44732.1; -; mRNA.
DR EMBL; AF440693; AAL34534.1; -; mRNA.
DR EMBL; AK011736; BAB27809.1; -; mRNA.
DR EMBL; AK090325; BAC41171.1; -; mRNA.
DR EMBL; AL591177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL15582.1; -; Genomic_DNA.
DR EMBL; BC012690; AAH12690.1; -; mRNA.
DR CCDS; CCDS25106.1; -.
DR PIR; S19894; SGMSV.
DR RefSeq; NP_035837.1; NM_011707.2.
DR AlphaFoldDB; P29788; -.
DR SMR; P29788; -.
DR BioGRID; 204539; 2.
DR ComplexPortal; CPX-492; Vitronectin-PAI-1 complex.
DR ComplexPortal; CPX-526; uPA-uPAR-vitronectin complex.
DR ELM; P29788; -.
DR IntAct; P29788; 2.
DR STRING; 10090.ENSMUSP00000017488; -.
DR GlyGen; P29788; 3 sites.
DR iPTMnet; P29788; -.
DR PhosphoSitePlus; P29788; -.
DR CPTAC; non-CPTAC-3512; -.
DR CPTAC; non-CPTAC-3513; -.
DR jPOST; P29788; -.
DR MaxQB; P29788; -.
DR PaxDb; P29788; -.
DR PeptideAtlas; P29788; -.
DR PRIDE; P29788; -.
DR ProteomicsDB; 297829; -.
DR DNASU; 22370; -.
DR Ensembl; ENSMUST00000017488; ENSMUSP00000017488; ENSMUSG00000017344.
DR GeneID; 22370; -.
DR KEGG; mmu:22370; -.
DR UCSC; uc007kjk.2; mouse.
DR CTD; 7448; -.
DR MGI; MGI:98940; Vtn.
DR VEuPathDB; HostDB:ENSMUSG00000017344; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00530000063751; -.
DR HOGENOM; CLU_046227_0_0_1; -.
DR InParanoid; P29788; -.
DR OMA; FNADKKC; -.
DR OrthoDB; 419397at2759; -.
DR PhylomeDB; P29788; -.
DR TreeFam; TF332780; -.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000170; Syndecan interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-977606; Regulation of Complement cascade.
DR BioGRID-ORCS; 22370; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Vtn; mouse.
DR PRO; PR:P29788; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P29788; protein.
DR Bgee; ENSMUSG00000017344; Expressed in retinal neural layer and 208 other tissues.
DR Genevisible; P29788; MM.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005796; C:Golgi lumen; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:1904090; C:peptidase inhibitor complex; ISO:MGI.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; ISO:MGI.
DR GO; GO:0048237; C:rough endoplasmic reticulum lumen; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR GO; GO:0035987; P:endodermal cell differentiation; ISO:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
DR GO; GO:0051918; P:negative regulation of fibrinolysis; IC:ComplexPortal.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IDA:CACAO.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0051258; P:protein polymerization; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:MGI.
DR GO; GO:0061302; P:smooth muscle cell-matrix adhesion; ISO:MGI.
DR CDD; cd00094; HX; 1.
DR Gene3D; 2.110.10.10; -; 2.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR InterPro; IPR020436; SMB_chordata.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF01033; Somatomedin_B; 1.
DR PRINTS; PR00022; SOMATOMEDINB.
DR SMART; SM00120; HX; 4.
DR SMART; SM00201; SO; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR SUPFAM; SSF90188; SSF90188; 1.
DR PROSITE; PS00024; HEMOPEXIN; 2.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00524; SMB_1; 1.
DR PROSITE; PS50958; SMB_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Heparin-binding; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal; Sulfation.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1372829"
FT CHAIN 20..478
FT /note="Vitronectin"
FT /id="PRO_0000036398"
FT DOMAIN 20..63
FT /note="SMB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT REPEAT 157..201
FT /note="Hemopexin 1"
FT REPEAT 202..249
FT /note="Hemopexin 2"
FT REPEAT 250..304
FT /note="Hemopexin 3"
FT REPEAT 420..473
FT /note="Hemopexin 4"
FT REGION 82..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..399
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT MOTIF 64..66
FT /note="Cell attachment site"
FT COMPBIAS 82..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..393
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04004"
FT MOD_RES 75
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 78
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 80
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 278
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 281
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04004"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 398
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P04004"
FT MOD_RES 416
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 419
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 421
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT DISULFID 24..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 24..28
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 28..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 38..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 38..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 44..50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 51..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 292..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT CONFLICT 179..180
FT /note="CY -> RC (in Ref. 4; AAL34534)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="A -> T (in Ref. 8; AAH12690)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="Y -> H (in Ref. 4; AAL34534)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="A -> T (in Ref. 5; BAB27809)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="K -> P (in Ref. 4; AAL34534)"
FT /evidence="ECO:0000305"
FT CONFLICT 383..384
FT /note="Missing (in Ref. 2; AAA40558)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="Y -> K (in Ref. 2; AAA40558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 54849 MW; EB0C772F8BD6A166 CRC64;
MAPLRPFFIL ALVAWVSLAD QESCKGRCTQ GFMASKKCQC DELCTYYQSC CADYMEQCKP
QVTRGDVFTM PEDDYWSYDY VEEPKNNTNT GVQPENTSPP GDLNPRTDGT LKPTAFLDPE
EQPSTPAPKV EQQEEILRPD TTDQGTPEFP EEELCSGKPF DAFTDLKNGS LFAFRGQYCY
ELDETAVRPG YPKLIQDVWG IEGPIDAAFT RINCQGKTYL FKGSQYWRFE DGVLDPGYPR
NISEGFSGIP DNVDAAFALP AHRYSGRERV YFFKGKQYWE YEFQQQPSQE ECEGSSLSAV
FEHFALLQRD SWENIFELLF WGRSSDGARE PQFISRNWHG VPGKVDAAMA GRIYVTGSLS
HSAQAKKQKS KRRSRKRYRS RRGRGHRRSQ SSNSRRSSRS IWFSLFSSEE SGLGTYNNYD
YDMDWLVPAT CEPIQSVYFF SGDKYYRVNL RTRRVDSVNP PYPRSIAQYW LGCPTSEK
