VISTA_HUMAN
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 03-AUG-2022, entry version 159.
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};
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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 ChEMBL; CHEMBL4523457; -.
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; Q9H7M9; -.
DR PeptideAtlas; Q9H7M9; -.
DR PRIDE; Q9H7M9; -.
DR ProteomicsDB; 81130; -.
DR ABCD; Q9H7M9; 2 sequenced antibodies.
DR Antibodypedia; 2331; 450 antibodies from 26 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 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; CIAYPSS; -.
DR OrthoDB; 1024898at2759; -.
DR PhylomeDB; Q9H7M9; -.
DR TreeFam; TF332066; -.
DR PathwayCommons; Q9H7M9; -.
DR SignaLink; Q9H7M9; -.
DR BioGRID-ORCS; 64115; 4 hits in 1065 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 185 other tissues.
DR Genevisible; Q9H7M9; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0032689; P:negative regulation of interferon-gamma production; IDA: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: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 Gene3D; 2.60.40.10; -; 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; PTHR44819; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
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
