VISTA_MOUSE
ID VISTA_MOUSE Reviewed; 308 AA.
AC Q9D659; A3RLQ7; E9PUF5; Q6KAT9;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=V-type immunoglobulin domain-containing suppressor of T-cell activation {ECO:0000303|PubMed:21383057};
DE AltName: Full=Platelet receptor Gi24 {ECO:0000250|UniProtKB:Q9H7M9};
DE AltName: Full=V-set domain-containing immunoregulatory receptor {ECO:0000312|MGI:MGI:1921298};
DE AltName: Full=V-set immunoregulatory receptor {ECO:0000312|MGI:MGI:1921298};
DE Flags: Precursor;
GN Name=Vsir {ECO:0000312|MGI:MGI:1921298};
GN Synonyms=Dies1 {ECO:0000303|PubMed:20042595},
GN PD-1H {ECO:0000303|PubMed:21768399}, VISTA {ECO:0000303|PubMed:21383057};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, Pituitary, Skin, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-277.
RC STRAIN=NMRI {ECO:0000312|EMBL:ABO15002.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:ABO15002.1};
RA Sachs U.J.H., Berghoefer H., Santoso S.;
RT "Mus musculus receptor Gi24 (murine Gi24R).";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
RX PubMed=20042595; DOI=10.1074/jbc.m109.077156;
RA Aloia L., Parisi S., Fusco L., Pastore L., Russo T.;
RT "Differentiation of embryonic stem cells 1 (Dies1) is a component of bone
RT morphogenetic protein 4 (BMP4) signaling pathway required for proper
RT differentiation of mouse embryonic stem cells.";
RL J. Biol. Chem. 285:7776-7783(2010).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21383057; DOI=10.1084/jem.20100619;
RA Wang L., Rubinstein R., Lines J.L., Wasiuk A., Ahonen C., Guo Y., Lu L.F.,
RA Gondek D., Wang Y., Fava R.A., Fiser A., Almo S., Noelle R.J.;
RT "VISTA, a novel mouse Ig superfamily ligand that negatively regulates T
RT cell responses.";
RL J. Exp. Med. 208:577-592(2011).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=21768399; DOI=10.4049/jimmunol.1100660;
RA Flies D.B., Wang S., Xu H., Chen L.;
RT "Cutting edge: A monoclonal antibody specific for the programmed death-1
RT homolog prevents graft-versus-host disease in mouse models.";
RL J. Immunol. 187:1537-1541(2011).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24743150; DOI=10.1172/jci74589;
RA Flies D.B., Han X., Higuchi T., Zheng L., Sun J., Ye J.J., Chen L.;
RT "Coinhibitory receptor PD-1H preferentially suppresses CD4[+] T cell-
RT mediated immunity.";
RL J. Clin. Invest. 124:1966-1975(2014).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25267631; DOI=10.1073/pnas.1407447111;
RA Wang L., Le Mercier I., Putra J., Chen W., Liu J., Schenk A.D., Nowak E.C.,
RA Suriawinata A.A., Li J., Noelle R.J.;
RT "Disruption of the immune-checkpoint VISTA gene imparts a proinflammatory
RT phenotype with predisposition to the development of autoimmunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:14846-14851(2014).
CC -!- FUNCTION: Immunoregulatory receptor which inhibits the T-cell response
CC (PubMed:21383057, PubMed:24743150, PubMed:25267631). May promote
CC differentiation of embryonic stem cells, by inhibiting BMP4 signaling
CC (PubMed:20042595). May stimulate MMP14-mediated MMP2 activation (By
CC similarity). {ECO:0000250|UniProtKB:Q9H7M9,
CC ECO:0000269|PubMed:20042595, ECO:0000269|PubMed:21383057,
CC ECO:0000269|PubMed:24743150, ECO:0000269|PubMed:25267631}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20042595,
CC ECO:0000269|PubMed:21768399}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, bone marrow, lymph
CC node, and in T-cells within the lamina propria of the small intestine
CC (PubMed:21768399). Detected on CD4+ and CD8+ T-cells, bone marrow-
CC derived dendritic cells (BMDCs), peritoneal macrophages, neutrophils,
CC and natural killer (NK) cells (PubMed:21768399). In spleen and lymph
CC nodes, highly expressed on CD4+ T-cell populations, and at lower levels
CC on CD8+ T-cells (PubMed:21383057). In thymus, has low expression on
CC CD4+ cells and CD8+ cells, and not detected on CD4+CD8+ cells
CC (PubMed:21383057). Expressed in splenic and peritoneal CD11b cells
CC (PubMed:21383057). Not detected in most B cells and NK cells (at
CC protein level) (PubMed:21383057). Also detected at lower levels in non-
CC hematopoeitic tissues such as heart, brain, lung, kidney, muscle,
CC ovary, and testis (PubMed:21768399, PubMed:21383057).
CC {ECO:0000269|PubMed:21383057, ECO:0000269|PubMed:21768399}.
CC -!- DEVELOPMENTAL STAGE: Detected in 7-day and 17-day embryos.
CC {ECO:0000269|PubMed:21768399}.
CC -!- INDUCTION: Up-regulated by phorbol 12-myristate 13-acetate (PMA) and
CC the cytokine IFNG. {ECO:0000269|PubMed:21768399}.
CC -!- PTM: At the cell surface, may be cleaved by MMP14. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20042595}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:24743150,
CC PubMed:25267631). At birth, lymphocyte populations in bone marrow,
CC spleen and lymph nodes appear to be normal (PubMed:24743150,
CC PubMed:25267631). Frequencies of activated peripheral T-cells are
CC increased in older animals (PubMed:24743150, PubMed:25267631). Levels
CC of the inflammatory cytokines CCL11, CXCL10, CCL2 and CXCL9 are
CC significantly increased (PubMed:25267631). Tissues show signs of
CC chronic inflammation, however this does not progress to overt
CC autoimmune disease (PubMed:25267631). {ECO:0000269|PubMed:24743150,
CC ECO:0000269|PubMed:25267631}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABO15002.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC27847.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD21368.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK014600; BAB29455.1; -; mRNA.
DR EMBL; AK030479; BAC26981.1; -; mRNA.
DR EMBL; AK032383; BAC27847.1; ALT_FRAME; mRNA.
DR EMBL; AK079734; BAC37735.1; -; mRNA.
DR EMBL; AK131118; BAD21368.1; ALT_INIT; mRNA.
DR EMBL; BC003967; AAH03967.1; -; mRNA.
DR EMBL; AC079082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; EF426799; ABO15002.1; ALT_FRAME; mRNA.
DR CCDS; CCDS48569.1; -.
DR RefSeq; NP_001153044.1; NM_001159572.1.
DR RefSeq; NP_083008.1; NM_028732.4.
DR AlphaFoldDB; Q9D659; -.
DR SMR; Q9D659; -.
DR STRING; 10090.ENSMUSP00000020301; -.
DR GlyGen; Q9D659; 3 sites.
DR iPTMnet; Q9D659; -.
DR PhosphoSitePlus; Q9D659; -.
DR EPD; Q9D659; -.
DR MaxQB; Q9D659; -.
DR PaxDb; Q9D659; -.
DR PRIDE; Q9D659; -.
DR ProteomicsDB; 297923; -.
DR ABCD; Q9D659; 4 sequenced antibodies.
DR Antibodypedia; 2331; 450 antibodies from 26 providers.
DR DNASU; 74048; -.
DR Ensembl; ENSMUST00000105460; ENSMUSP00000101100; ENSMUSG00000020101.
DR GeneID; 74048; -.
DR KEGG; mmu:74048; -.
DR UCSC; uc007few.2; mouse.
DR UCSC; uc007fex.2; mouse.
DR CTD; 64115; -.
DR MGI; MGI:1921298; Vsir.
DR VEuPathDB; HostDB:ENSMUSG00000020101; -.
DR eggNOG; ENOG502QWBS; Eukaryota.
DR GeneTree; ENSGT00940000163256; -.
DR InParanoid; Q9D659; -.
DR OrthoDB; 1024898at2759; -.
DR TreeFam; TF332066; -.
DR BioGRID-ORCS; 74048; 2 hits in 43 CRISPR screens.
DR ChiTaRS; Vsir; mouse.
DR PRO; PR:Q9D659; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D659; protein.
DR Bgee; ENSMUSG00000020101; Expressed in granulocyte and 222 other tissues.
DR ExpressionAtlas; Q9D659; baseline and differential.
DR Genevisible; Q9D659; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0061133; F:endopeptidase activator activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
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; IDA:MGI.
DR GO; GO:2000565; P:negative regulation of CD8-positive, alpha-beta T cell proliferation; ISO:MGI.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:MGI.
DR GO; GO:0032700; P:negative regulation of interleukin-17 production; ISO:MGI.
DR GO; GO:0002725; P:negative regulation of T cell cytokine production; IDA:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0120158; P:positive regulation of collagen catabolic process; ISO:MGI.
DR GO; GO:0010950; P:positive regulation of endopeptidase activity; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:MGI.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IGI:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IMP:MGI.
DR GO; GO:0031638; P:zymogen activation; ISO:MGI.
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 Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..308
FT /note="V-type immunoglobulin domain-containing suppressor
FT of T-cell activation"
FT /id="PRO_0000014766"
FT TOPO_DOM 33..191
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:20042595"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 33..167
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT REGION 230..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7M9"
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 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 82
FT /note="M -> I (in Ref. 1; BAC27847 and 5; ABO15002)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="S -> SS (in Ref. 1; BAB29455/BAC26981/BAC27847/
FT BAC37735, 3; AAH03967 and 5; ABO15002)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 33559 MW; B9B60FCA19C76CA0 CRC64;
MGVPAVPEAS SPRWGTLLLA IFLAASRGLV AAFKVTTPYS LYVCPEGQNA TLTCRILGPV
SKGHDVTIYK TWYLSSRGEV QMCKEHRPIR NFTLQHLQHH GSHLKANASH DQPQKHGLEL
ASDHHGNFSI TLRNVTPRDS GLYCCLVIEL KNHHPEQRFY GSMELQVQAG KGSGSTCMAS
NEQDSDSITA AALATGACIV GILCLPLILL LVYKQRQVAS HRRAQELVRM DSNTQGIENP
GFETTPPFQG MPEAKTRPPL SYVAQRQPSE SGRYLLSDPS TPLSPPGPGD VFFPSLDPVP
DSPNSEAI
