ID VISTA_HUMAN Reviewed; 311 AA. AC Q9H7M9; A1L0X9; A4ZYV1; A8MVH5; Q6UXF3; Q8WUG3; Q8WYZ8; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 3. DT 24-JAN-2024, entry version 167. DE RecName: Full=V-type immunoglobulin domain-containing suppressor of T-cell activation {ECO:0000303|PubMed:24691993}; DE AltName: Full=Platelet receptor Gi24 {ECO:0000303|Ref.1}; DE AltName: Full=Stress-induced secreted protein-1 {ECO:0000303|Ref.2}; DE Short=Sisp-1 {ECO:0000303|Ref.2}; DE AltName: Full=V-set domain-containing immunoregulatory receptor {ECO:0000250|UniProtKB:Q9D659}; DE AltName: Full=V-set immunoregulatory receptor {ECO:0000312|HGNC:HGNC:30085}; DE Flags: Precursor; GN Name=VSIR {ECO:0000312|HGNC:HGNC:30085}; GN Synonyms=C10orf54, SISP1 {ECO:0000303|Ref.2}, VISTA; GN ORFNames=PP2135, UNQ730/PRO1412; 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], AND VARIANT GLU-187. RA Sachs U.J., Eva O., Clemetson K.J., Santoso S.; RT "Gi24, a novel platelet receptor."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-187. RA Yang Y.-S., Seo Y.-S.; RT "SISP1, a novel P53 target gene."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-187. RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-187. RC TISSUE=Spleen; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-187. 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [8] RP PROTEIN SEQUENCE OF 33-47. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-248, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND CLEAVAGE BY MMP14. RX PubMed=20666777; DOI=10.1111/j.1349-7006.2010.01675.x; RA Sakr M.A., Takino T., Domoto T., Nakano H., Wong R.W., Sasaki M., RA Nakanuma Y., Sato H.; RT "GI24 enhances tumor invasiveness by regulating cell surface membrane-type RT 1 matrix metalloproteinase."; RL Cancer Sci. 101:2368-2374(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-248, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=24691993; DOI=10.1158/0008-5472.can-13-1504; RA Lines J.L., Pantazi E., Mak J., Sempere L.F., Wang L., O'Connell S., RA Ceeraz S., Suriawinata A.A., Yan S., Ernstoff M.S., Noelle R.; RT "VISTA is an immune checkpoint molecule for human T cells."; RL Cancer Res. 74:1924-1932(2014). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Immunoregulatory receptor which inhibits the T-cell response CC (PubMed:24691993). May promote differentiation of embryonic stem cells, CC by inhibiting BMP4 signaling (By similarity). May stimulate MMP14- CC mediated MMP2 activation (PubMed:20666777). CC {ECO:0000250|UniProtKB:Q9D659, ECO:0000269|PubMed:20666777, CC ECO:0000269|PubMed:24691993}. CC -!- INTERACTION: CC Q9H7M9; P05090: APOD; NbExp=3; IntAct=EBI-744988, EBI-715495; CC Q9H7M9; P07306: ASGR1; NbExp=3; IntAct=EBI-744988, EBI-1172335; CC Q9H7M9; P27449: ATP6V0C; NbExp=3; IntAct=EBI-744988, EBI-721179; CC Q9H7M9; O95393: BMP10; NbExp=3; IntAct=EBI-744988, EBI-3922513; CC Q9H7M9; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-744988, EBI-10271156; CC Q9H7M9; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-744988, EBI-11989440; CC Q9H7M9; A0PK11: CLRN2; NbExp=3; IntAct=EBI-744988, EBI-12813623; CC Q9H7M9; Q8TBE1: CNIH3; NbExp=3; IntAct=EBI-744988, EBI-12208021; CC Q9H7M9; Q9UPQ8: DOLK; NbExp=3; IntAct=EBI-744988, EBI-8645574; CC Q9H7M9; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-744988, EBI-12070086; CC Q9H7M9; Q8N912: NRAC; NbExp=3; IntAct=EBI-744988, EBI-12051377; CC Q9H7M9; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-744988, EBI-11721828; CC Q9H7M9; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-744988, EBI-12955265; CC Q9H7M9; P78383: SLC35B1; NbExp=3; IntAct=EBI-744988, EBI-12147661; CC Q9H7M9; Q969S0: SLC35B4; NbExp=3; IntAct=EBI-744988, EBI-10281213; CC Q9H7M9; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-744988, EBI-8640191; CC Q9H7M9; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-744988, EBI-8644968; CC Q9H7M9; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-744988, EBI-2339195; CC Q9H7M9; A2RU14: TMEM218; NbExp=3; IntAct=EBI-744988, EBI-10173151; CC Q9H7M9; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-744988, EBI-12195227; CC Q9H7M9; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-744988, EBI-12111910; CC Q9H7M9; P01375: TNF; NbExp=3; IntAct=EBI-744988, EBI-359977; CC Q9H7M9; O60636: TSPAN2; NbExp=3; IntAct=EBI-744988, EBI-3914288; CC Q9H7M9; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-744988, EBI-12195249; CC Q9H7M9; Q15836: VAMP3; NbExp=3; IntAct=EBI-744988, EBI-722343; CC Q9H7M9; Q9H7M9: VSIR; NbExp=4; IntAct=EBI-744988, EBI-744988; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20666777, CC ECO:0000269|PubMed:24691993}; Single-pass type I membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Expressed in spleen. Detected on a number of CC myeloid cells including CD11b monocytes, CD66b+ neutrophils, at low CC levels on CD4+ and CD8+ T-cells, and in a subset of NK cells. Not CC detected on B cells (at protein level). Expressed at high levels in CC placenta, spleen, plasma blood leukocytes, and lung. Expressed at CC moderate levels in lymph node, bone marrow, fat, uterus, and trachea. CC Has low expression levels in other tissues. CC {ECO:0000269|PubMed:24691993}. CC -!- PTM: At the cell surface, may be cleaved by MMP14. CC {ECO:0000269|PubMed:20666777}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9D659}. CC -!- SEQUENCE CAUTION: CC Sequence=AAL55778.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; CC Sequence=AAL55778.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305}; CC Sequence=BAB15739.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY265805; AAP03084.1; -; mRNA. DR EMBL; EF506490; ABP88253.1; -; mRNA. DR EMBL; AF289594; AAL55778.1; ALT_SEQ; mRNA. DR EMBL; AK024449; BAB15739.1; ALT_INIT; mRNA. DR EMBL; AY358379; AAQ88745.1; -; mRNA. DR EMBL; AL731541; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020568; AAH20568.1; -; mRNA. DR EMBL; BC127257; AAI27258.1; -; mRNA. DR CCDS; CCDS31218.1; -. DR RefSeq; NP_071436.1; NM_022153.1. DR PDB; 6MVL; X-ray; 1.61 A; A=32-194. DR PDB; 6OIL; X-ray; 1.85 A; A=33-194. DR PDB; 6U6V; X-ray; 1.90 A; A=33-193. DR PDBsum; 6MVL; -. DR PDBsum; 6OIL; -. DR PDBsum; 6U6V; -. DR AlphaFoldDB; Q9H7M9; -. DR SMR; Q9H7M9; -. DR BioGRID; 122071; 31. DR DIP; DIP-57562N; -. DR IntAct; Q9H7M9; 28. DR MINT; Q9H7M9; -. DR STRING; 9606.ENSP00000378409; -. DR BindingDB; Q9H7M9; -. DR ChEMBL; CHEMBL4523457; -. DR GlyCosmos; Q9H7M9; 4 sites, 1 glycan. DR GlyGen; Q9H7M9; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9H7M9; -. DR PhosphoSitePlus; Q9H7M9; -. DR BioMuta; VSIR; -. DR DMDM; 311033449; -. DR EPD; Q9H7M9; -. DR jPOST; Q9H7M9; -. DR MassIVE; Q9H7M9; -. DR MaxQB; Q9H7M9; -. DR PaxDb; 9606-ENSP00000378409; -. DR PeptideAtlas; Q9H7M9; -. DR ProteomicsDB; 81130; -. DR Pumba; Q9H7M9; -. DR ABCD; Q9H7M9; 2 sequenced antibodies. DR Antibodypedia; 2331; 558 antibodies from 28 providers. DR CPTC; Q9H7M9; 1 antibody. DR DNASU; 64115; -. DR Ensembl; ENST00000394957.8; ENSP00000378409.3; ENSG00000107738.20. DR GeneID; 64115; -. DR KEGG; hsa:64115; -. DR MANE-Select; ENST00000394957.8; ENSP00000378409.3; NM_022153.2; NP_071436.1. DR UCSC; uc001jsd.5; human. DR AGR; HGNC:30085; -. DR CTD; 64115; -. DR DisGeNET; 64115; -. DR GeneCards; VSIR; -. DR HGNC; HGNC:30085; VSIR. DR HPA; ENSG00000107738; Tissue enhanced (bone marrow, lymphoid tissue). DR MIM; 615608; gene. DR neXtProt; NX_Q9H7M9; -. DR OpenTargets; ENSG00000107738; -. DR PharmGKB; PA142672307; -. DR VEuPathDB; HostDB:ENSG00000107738; -. DR eggNOG; ENOG502QWBS; Eukaryota. DR GeneTree; ENSGT00940000163256; -. DR HOGENOM; CLU_078121_0_0_1; -. DR InParanoid; Q9H7M9; -. DR OMA; GLQNCTF; -. DR OrthoDB; 5347249at2759; -. DR PhylomeDB; Q9H7M9; -. DR TreeFam; TF332066; -. DR PathwayCommons; Q9H7M9; -. DR SignaLink; Q9H7M9; -. DR BioGRID-ORCS; 64115; 6 hits in 1142 CRISPR screens. DR ChiTaRS; C10orf54; human. DR GeneWiki; C10orf54; -. DR GenomeRNAi; 64115; -. DR Pharos; Q9H7M9; Tbio. DR PRO; PR:Q9H7M9; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9H7M9; Protein. DR Bgee; ENSG00000107738; Expressed in granulocyte and 186 other cell types or tissues. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0061133; F:endopeptidase activator activity; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046636; P:negative regulation of alpha-beta T cell activation; IBA:GO_Central. DR GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IMP:UniProtKB. DR GO; GO:2000565; P:negative regulation of CD8-positive, alpha-beta T cell proliferation; IMP:UniProtKB. DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IDA:UniProtKB. DR GO; GO:0032700; P:negative regulation of interleukin-17 production; IDA:UniProtKB. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB. DR GO; GO:0032689; P:negative regulation of type II interferon production; IDA:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB. DR GO; GO:0120158; P:positive regulation of collagen catabolic process; IDA:UniProtKB. DR GO; GO:0010950; P:positive regulation of endopeptidase activity; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IMP:UniProtKB. DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro. DR GO; GO:0031638; P:zymogen activation; IDA:UniProtKB. DR CDD; cd20980; IgV_VISTA; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR042473; VISTA. DR PANTHER; PTHR44819; V-TYPE IMMUNOGLOBULIN DOMAIN-CONTAINING SUPPRESSOR OF T-CELL ACTIVATION; 1. DR PANTHER; PTHR44819:SF1; V-TYPE IMMUNOGLOBULIN DOMAIN-CONTAINING SUPPRESSOR OF T-CELL ACTIVATION; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; Q9H7M9; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein; Receptor; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..32 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 33..311 FT /note="V-type immunoglobulin domain-containing suppressor FT of T-cell activation" FT /id="PRO_0000014765" FT TOPO_DOM 33..194 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:Q9D659" FT TRANSMEM 195..215 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 216..311 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:Q9D659" FT DOMAIN 33..168 FT /note="Ig-like V-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT REGION 267..311 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 267..281 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 235 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 248 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT CARBOHYD 49 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 91 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 128 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 54..146 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VARIANT 187 FT /note="D -> E (in dbSNP:rs3747869)" FT /evidence="ECO:0000269|PubMed:12975309, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15498874, FT ECO:0000269|Ref.1, ECO:0000269|Ref.2" FT /id="VAR_028036" FT CONFLICT 33 FT /note="F -> L (in Ref. 3; AAL55778)" FT /evidence="ECO:0000305" FT CONFLICT 85 FT /note="E -> K (in Ref. 3; AAL55778)" FT /evidence="ECO:0000305" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 40..45 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 50..57 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 66..74 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:6MVL" FT TURN 94..97 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 99..102 FT /evidence="ECO:0007829|PDB:6OIL" FT HELIX 112..116 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 125..133 FT /evidence="ECO:0007829|PDB:6MVL" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 142..152 FT /evidence="ECO:0007829|PDB:6MVL" FT TURN 153..155 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 156..169 FT /evidence="ECO:0007829|PDB:6MVL" FT STRAND 171..174 FT /evidence="ECO:0007829|PDB:6OIL" FT STRAND 179..182 FT /evidence="ECO:0007829|PDB:6OIL" SQ SEQUENCE 311 AA; 33908 MW; 321862EC650623CD CRC64; MGVPTALEAG SWRWGSLLFA LFLAASLGPV AAFKVATPYS LYVCPEGQNV TLTCRLLGPV DKGHDVTFYK TWYRSSRGEV QTCSERRPIR NLTFQDLHLH HGGHQAANTS HDLAQRHGLE SASDHHGNFS ITMRNLTLLD SGLYCCLVVE IRHHHSEHRV HGAMELQVQT GKDAPSNCVV YPSSSQDSEN ITAAALATGA CIVGILCLPL ILLLVYKQRQ AASNRRAQEL VRMDSNIQGI ENPGFEASPP AQGIPEAKVR HPLSYVAQRQ PSESGRHLLS EPSTPLSPPG PGDVFFPSLD PVPDSPNFEV I //