VTCN1_MOUSE
ID VTCN1_MOUSE Reviewed; 283 AA.
AC Q7TSP5; Q7TPH5; Q8K091;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=V-set domain containing T-cell activation inhibitor 1;
DE AltName: Full=B7 homolog 4;
DE Short=B7-H4;
DE AltName: Full=Immune costimulatory protein B7-H4;
DE AltName: Full=Protein B7S1;
DE AltName: Full=T cell costimulatory molecule B7x;
DE Flags: Precursor;
GN Name=Vtcn1 {ECO:0000312|MGI:MGI:3039619};
GN Synonyms=B7h4 {ECO:0000250|UniProtKB:Q7Z7D3};
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] {ECO:0000305, ECO:0000312|EMBL:AAP37284.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAP37284.1};
RC TISSUE=Spleen {ECO:0000269|PubMed:12818165};
RX PubMed=12818165; DOI=10.1016/s1074-7613(03)00152-3;
RA Sica G.L., Choi I.-H., Zhu G., Tamada K., Wang S.-D., Tamura H.,
RA Chapoval A.I., Flies D.B., Bajorath J., Chen L.;
RT "B7-H4, a molecule of the B7 family, negatively regulates T cell
RT immunity.";
RL Immunity 18:849-861(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAP88965.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP GPI-ANCHOR.
RX PubMed=12818166; DOI=10.1016/s1074-7613(03)00147-x;
RA Prasad D.V.R., Richards S., Mai X.M., Dong C.;
RT "B7S1, a novel B7 family member that negatively regulates T cell
RT activation.";
RL Immunity 18:863-873(2003).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAQ24205.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAQ24205.1};
RX PubMed=12920180; DOI=10.1073/pnas.1434299100;
RA Zang X., Loke P., Kim J., Murphy K., Waitz R., Allison J.P.;
RT "B7x: a widely expressed B7 family member that inhibits T cell
RT activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10388-10392(2003).
RN [4] {ECO:0000312|EMBL:BAE25330.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE25330.1};
RC TISSUE=Blastocyst {ECO:0000312|EMBL:BAE26576.1}, and
RC Oviduct {ECO:0000312|EMBL:BAE25330.1};
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 [5] {ECO:0000312|EMBL:AAH32925.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus {ECO:0000312|EMBL:AAH32925.1};
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 [6] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=16914726; DOI=10.1128/mcb.00755-06;
RA Suh W.-K., Wang S., Duncan G.S., Miyazaki Y., Cates E., Walker T.,
RA Gajewska B.U., Deenick E., Dawicki W., Okada H., Wakeham A., Itie A.,
RA Watts T.H., Ohashi P.S., Jordana M., Yoshida H., Mak T.W.;
RT "Generation and characterization of B7-H4/B7S1/B7x-deficient mice.";
RL Mol. Cell. Biol. 26:6403-6411(2006).
CC -!- FUNCTION: Negatively regulates T-cell-mediated immune response by
CC inhibiting T-cell activation, proliferation, cytokine production and
CC development of cytotoxicity. When expressed on the cell surface of
CC tumor macrophages, plays an important role, together with regulatory T-
CC cells (Treg), in the suppression of tumor-associated antigen-specific
CC T-cell immunity. Involved in promoting epithelial cell transformation.
CC {ECO:0000250|UniProtKB:Q7Z7D3, ECO:0000269|PubMed:12818165,
CC ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12818165,
CC ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}; Lipid-
CC anchor, GPI-anchor {ECO:0000269|PubMed:12818165,
CC ECO:0000269|PubMed:12818166, ECO:0000269|PubMed:12920180}.
CC Note=Expressed at the cell surface. A soluble form has also been
CC detected. {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166,
CC ECO:0000269|PubMed:12920180}.
CC -!- TISSUE SPECIFICITY: Expressed on the surface of professional antigen-
CC presenting cells (at protein level). Widely expressed, including in
CC kidney, liver, lung, pancreas, placenta, prostate, spleen, testis and
CC thymus. {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12818166,
CC ECO:0000269|PubMed:12920180}.
CC -!- INDUCTION: Down-regulated upon activation of B-cells.
CC {ECO:0000269|PubMed:12818166}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q7Z7D3}.
CC -!- DISRUPTION PHENOTYPE: Mice mount mildy augmented T-helper 1 responses
CC and display slightly lowered parasitic burdens upon Leishmania major
CC infection. {ECO:0000269|PubMed:16914726}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000250|UniProtKB:Q5ZPR3}.
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DR EMBL; AY280973; AAP37284.1; -; mRNA.
DR EMBL; AY322147; AAP88965.1; -; mRNA.
DR EMBL; AY346099; AAQ24205.1; -; mRNA.
DR EMBL; AK143276; BAE25330.1; -; mRNA.
DR EMBL; AK145664; BAE26576.1; -; mRNA.
DR EMBL; BC032925; AAH32925.1; -; mRNA.
DR CCDS; CCDS17677.1; -.
DR RefSeq; NP_848709.2; NM_178594.3.
DR AlphaFoldDB; Q7TSP5; -.
DR SMR; Q7TSP5; -.
DR STRING; 10090.ENSMUSP00000057721; -.
DR GlyGen; Q7TSP5; 1 site.
DR PhosphoSitePlus; Q7TSP5; -.
DR EPD; Q7TSP5; -.
DR PaxDb; Q7TSP5; -.
DR PRIDE; Q7TSP5; -.
DR ProteomicsDB; 297933; -.
DR Antibodypedia; 33888; 751 antibodies from 44 providers.
DR Ensembl; ENSMUST00000054791; ENSMUSP00000057721; ENSMUSG00000051076.
DR GeneID; 242122; -.
DR KEGG; mmu:242122; -.
DR UCSC; uc008qqx.2; mouse.
DR CTD; 79679; -.
DR MGI; MGI:3039619; Vtcn1.
DR VEuPathDB; HostDB:ENSMUSG00000051076; -.
DR eggNOG; ENOG502S286; Eukaryota.
DR GeneTree; ENSGT00940000157300; -.
DR HOGENOM; CLU_013137_8_6_1; -.
DR InParanoid; Q7TSP5; -.
DR OMA; DQNEMFR; -.
DR OrthoDB; 1040668at2759; -.
DR PhylomeDB; Q7TSP5; -.
DR TreeFam; TF331083; -.
DR BioGRID-ORCS; 242122; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q7TSP5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q7TSP5; protein.
DR Bgee; ENSMUSG00000051076; Expressed in placenta labyrinth and 28 other tissues.
DR Genevisible; Q7TSP5; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0050868; P:negative regulation of T cell activation; IDA:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0001562; P:response to protozoan; IMP:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
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; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunity; Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..257
FT /note="V-set domain containing T-cell activation inhibitor
FT 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000339238"
FT PROPEP 258..283
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000339239"
FT DOMAIN 35..144
FT /note="Ig-like V-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 153..241
FT /note="Ig-like V-type 2"
FT /evidence="ECO:0000255"
FT LIPID 257
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 168..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 134
FT /note="T -> S (in Ref. 5; AAH32925)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="F -> S (in Ref. 5; AAH32925)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="V -> A (in Ref. 2; AAP88965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 283 AA; 30875 MW; 7E2F174618578519 CRC64;
MASLGQIIFW SIINIIIILA GAIALIIGFG ISGKHFITVT TFTSAGNIGE DGTLSCTFEP
DIKLNGIVIQ WLKEGIKGLV HEFKEGKDDL SQQHEMFRGR TAVFADQVVV GNASLRLKNV
QLTDAGTYTC YIRTSKGKGN ANLEYKTGAF SMPEINVDYN ASSESLRCEA PRWFPQPTVA
WASQVDQGAN FSEVSNTSFE LNSENVTMKV VSVLYNVTIN NTYSCMIEND IAKATGDIKV
TDSEVKRRSQ LQLLNSGPSP CVFSSAFVAG WALLSLSCCL MLR
