VTCN1_HUMAN
ID VTCN1_HUMAN Reviewed; 282 AA.
AC Q7Z7D3; Q0GN76; Q45VN0; Q5WPZ3; Q6P097; Q9H6B2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 156.
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=B7h.5;
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|EMBL:EAW56672.1};
GN Synonyms=B7H4 {ECO:0000312|EMBL:AAS13400.1}; ORFNames=UNQ659/PRO1291;
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] {ECO:0000305, ECO:0000312|EMBL:AAP37283.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Placenta {ECO:0000269|PubMed:17509674};
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:AAQ24206.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 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 [3] {ECO:0000305, ECO:0000312|EMBL:AAZ17406.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16782226; DOI=10.1016/j.lungcan.2006.05.012;
RA Sun Y., Wang Y., Zhao J., Gu M., Giscombe R., Lefvert A.K., Wang X.;
RT "B7-H3 and B7-H4 expression in non-small-cell lung cancer.";
RL Lung Cancer 53:143-151(2006).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAS13400.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Mao Y., Zhang X.;
RT "A new splice variant of B7-H4.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAQ88718.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] {ECO:0000305, ECO:0000312|EMBL:BAB15349.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Kidney epithelium {ECO:0000269|PubMed:14702039}, and Thymus;
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 [7] {ECO:0000312|EMBL:AL391476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAS13400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000305, ECO:0000312|EMBL:AAH74729.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH74729.1}, and Prostate;
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 [10] {ECO:0000305, ECO:0000312|EMBL:AAS13400.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-167 (ISOFORM 1).
RC TISSUE=Peripheral blood;
RA Huang G., Bai Y., Zhang L., Zhang L., Song M.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [11] {ECO:0000305}
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=14568939; DOI=10.4049/jimmunol.171.9.4650;
RA Choi I.-H., Zhu G., Sica G.L., Strome S.E., Cheville J.C., Lau J.S.,
RA Zhu Y., Flies D.B., Tamada K., Chen L.;
RT "Genomic organization and expression analysis of B7-H4, an immune
RT inhibitory molecule of the B7 family.";
RL J. Immunol. 171:4650-4654(2003).
RN [12] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=15878339; DOI=10.1016/j.yexcr.2005.01.018;
RA Salceda S., Tang T., Kmet M., Munteanu A., Ghosh M., Macina R., Liu W.,
RA Pilkington G., Papkoff J.;
RT "The immunomodulatory protein B7-H4 is overexpressed in breast and ovarian
RT cancers and promotes epithelial cell transformation.";
RL Exp. Cell Res. 306:128-141(2005).
RN [13] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16606666; DOI=10.1084/jem.20050930;
RA Kryczek I., Zou L., Rodriguez P., Zhu G., Wei S., Mottram P., Brumlik M.,
RA Cheng P., Curiel T., Myers L., Lackner A., Alvarez X., Ochoa A., Chen L.,
RA Zou W.;
RT "B7-H4 expression identifies a novel suppressive macrophage population in
RT human ovarian carcinoma.";
RL J. Exp. Med. 203:871-881(2006).
RN [14] {ECO:0000305}
RP INDUCTION.
RX PubMed=16785496; DOI=10.4049/jimmunol.177.1.40;
RA Kryczek I., Wei S., Zou L., Zhu G., Mottram P., Xu H., Chen L., Zou W.;
RT "Induction of B7-H4 on APCs through IL-10: novel suppressive mode for
RT regulatory T cells.";
RL J. Immunol. 177:40-44(2006).
RN [15] {ECO:0000305}
RP TISSUE SPECIFICITY, AND USE AS A MARKER FOR RENAL CELL CANCER.
RX PubMed=16798883; DOI=10.1073/pnas.0600937103;
RA Krambeck A.E., Thompson R.H., Dong H., Lohse C.M., Park E.S., Kuntz S.M.,
RA Leibovich B.C., Blute M.L., Cheville J.C., Kwon E.D.;
RT "B7-H4 expression in renal cell carcinoma and tumor vasculature:
RT associations with cancer progression and survival.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10391-10396(2006).
RN [16] {ECO:0000305}
RP FUNCTION, AND INDUCTION.
RX PubMed=17875732; DOI=10.1158/0008-5472.can-07-1866;
RA Kryczek I., Wei S., Zhu G., Myers L., Mottram P., Cheng P., Chen L.,
RA Coukos G., Zou W.;
RT "Relationship between B7-H4, regulatory T cells, and patient outcome in
RT human ovarian carcinoma.";
RL Cancer Res. 67:8900-8905(2007).
RN [17] {ECO:0000305}
RP FUNCTION.
RX PubMed=17509674; DOI=10.1016/j.ygyno.2007.03.039;
RA Miyatake T., Tringler B., Liu W., Liu S.-H., Papkoff J., Enomoto T.,
RA Torkko K.C., Dehn D.L., Swisher A., Shroyer K.R.;
RT "B7-H4 (DD-O110) is overexpressed in high risk uterine endometrioid
RT adenocarcinomas and inversely correlated with tumor T-cell infiltration.";
RL Gynecol. Oncol. 106:119-127(2007).
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:Q7TSP5, ECO:0000269|PubMed:15878339,
CC ECO:0000269|PubMed:16606666, ECO:0000269|PubMed:17509674,
CC ECO:0000269|PubMed:17875732}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=Expressed at the cell surface. A
CC soluble form has also been detected. {ECO:0000255,
CC ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:15878339,
CC ECO:0000269|PubMed:16782226}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:12920180,
CC ECO:0000269|PubMed:12975309, ECO:0000269|PubMed:14702039,
CC ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16710414,
CC ECO:0000269|PubMed:16782226};
CC IsoId=Q7Z7D3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16782226};
CC IsoId=Q7Z7D3-2; Sequence=VSP_052841;
CC Name=3 {ECO:0000269|Ref.4};
CC IsoId=Q7Z7D3-3; Sequence=VSP_052842, VSP_052843;
CC Name=4;
CC IsoId=Q7Z7D3-4; Sequence=VSP_045423;
CC -!- TISSUE SPECIFICITY: Overexpressed in breast, ovarian, endometrial,
CC renal cell (RCC) and non-small-cell lung cancers (NSCLC). Expressed on
CC activated T- and B-cells, monocytes and dendritic cells, but not
CC expressed in most normal tissues (at protein level). Widely expressed,
CC including in kidney, liver, lung, ovary, placenta, spleen and testis.
CC {ECO:0000269|PubMed:12818165, ECO:0000269|PubMed:14568939,
CC ECO:0000269|PubMed:15878339, ECO:0000269|PubMed:16606666,
CC ECO:0000269|PubMed:16782226, ECO:0000269|PubMed:16798883,
CC ECO:0000269|PubMed:17509674}.
CC -!- INDUCTION: Up-regulated by IL6/interleukin-6 and IL10/interleukin-10
CC and inhibited by CSF2/GM-CSF and IL4/interleukin-4 on antigen-
CC presenting cells (APCs). {ECO:0000269|PubMed:16606666,
CC ECO:0000269|PubMed:16785496, ECO:0000269|PubMed:17875732}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15878339}.
CC -!- MISCELLANEOUS: May serve as a predictive marker for renal cell
CC carcinoma. {ECO:0000269|PubMed:16798883}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000250|UniProtKB:Q5ZPR3}.
CC -!- CAUTION: The mouse ortholog has been shown to be a GPI-anchored protein
CC but the Gly residue which is predicted to be the modified site in mouse
CC and rat is not conserved in human. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/VTCN1ID44144ch1p13.html";
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DR EMBL; AY280972; AAP37283.1; -; mRNA.
DR EMBL; AY346100; AAQ24206.1; -; mRNA.
DR EMBL; DQ103757; AAZ17406.1; -; mRNA.
DR EMBL; AY442303; AAS13400.1; -; mRNA.
DR EMBL; AY358352; AAQ88718.1; -; mRNA.
DR EMBL; AK026071; BAB15349.1; -; mRNA.
DR EMBL; AK303466; BAH13967.1; -; mRNA.
DR EMBL; AL391476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56672.1; -; Genomic_DNA.
DR EMBL; CH471122; EAW56673.1; -; Genomic_DNA.
DR EMBL; BC065717; AAH65717.1; -; mRNA.
DR EMBL; BC074729; AAH74729.1; -; mRNA.
DR EMBL; DQ836392; ABI16083.1; -; mRNA.
DR CCDS; CCDS58019.1; -. [Q7Z7D3-4]
DR CCDS; CCDS58020.1; -. [Q7Z7D3-2]
DR CCDS; CCDS894.1; -. [Q7Z7D3-1]
DR RefSeq; NP_001240778.1; NM_001253849.1. [Q7Z7D3-4]
DR RefSeq; NP_001240779.1; NM_001253850.1. [Q7Z7D3-2]
DR RefSeq; NP_078902.2; NM_024626.3. [Q7Z7D3-1]
DR PDB; 4GOS; X-ray; 1.59 A; A=30-148.
DR PDBsum; 4GOS; -.
DR AlphaFoldDB; Q7Z7D3; -.
DR SMR; Q7Z7D3; -.
DR BioGRID; 122803; 18.
DR IntAct; Q7Z7D3; 2.
DR STRING; 9606.ENSP00000358470; -.
DR GlyConnect; 1897; 5 N-Linked glycans (1 site).
DR GlyGen; Q7Z7D3; 2 sites, 5 N-linked glycans (1 site).
DR iPTMnet; Q7Z7D3; -.
DR PhosphoSitePlus; Q7Z7D3; -.
DR BioMuta; VTCN1; -.
DR DMDM; 74759262; -.
DR jPOST; Q7Z7D3; -.
DR MassIVE; Q7Z7D3; -.
DR PaxDb; Q7Z7D3; -.
DR PeptideAtlas; Q7Z7D3; -.
DR PRIDE; Q7Z7D3; -.
DR ProteomicsDB; 66811; -.
DR ProteomicsDB; 69518; -. [Q7Z7D3-1]
DR ProteomicsDB; 69519; -. [Q7Z7D3-2]
DR ABCD; Q7Z7D3; 36 sequenced antibodies.
DR Antibodypedia; 33888; 751 antibodies from 44 providers.
DR CPTC; Q7Z7D3; 2 antibodies.
DR DNASU; 79679; -.
DR Ensembl; ENST00000328189.7; ENSP00000328168.3; ENSG00000134258.18. [Q7Z7D3-2]
DR Ensembl; ENST00000369458.8; ENSP00000358470.3; ENSG00000134258.18. [Q7Z7D3-1]
DR Ensembl; ENST00000539893.5; ENSP00000444724.1; ENSG00000134258.18. [Q7Z7D3-4]
DR GeneID; 79679; -.
DR KEGG; hsa:79679; -.
DR MANE-Select; ENST00000369458.8; ENSP00000358470.3; NM_024626.4; NP_078902.2.
DR UCSC; uc001ehb.4; human. [Q7Z7D3-1]
DR CTD; 79679; -.
DR DisGeNET; 79679; -.
DR GeneCards; VTCN1; -.
DR HGNC; HGNC:28873; VTCN1.
DR HPA; ENSG00000134258; Tissue enhanced (breast, fallopian tube, pancreas).
DR MIM; 608162; gene.
DR neXtProt; NX_Q7Z7D3; -.
DR OpenTargets; ENSG00000134258; -.
DR PharmGKB; PA142670611; -.
DR VEuPathDB; HostDB:ENSG00000134258; -.
DR eggNOG; ENOG502S286; Eukaryota.
DR GeneTree; ENSGT00940000157300; -.
DR HOGENOM; CLU_013137_8_6_1; -.
DR InParanoid; Q7Z7D3; -.
DR OMA; DQNEMFR; -.
DR OrthoDB; 1040668at2759; -.
DR PhylomeDB; Q7Z7D3; -.
DR TreeFam; TF331083; -.
DR PathwayCommons; Q7Z7D3; -.
DR SignaLink; Q7Z7D3; -.
DR BioGRID-ORCS; 79679; 10 hits in 1057 CRISPR screens.
DR ChiTaRS; VTCN1; human.
DR GeneWiki; VTCN1; -.
DR GenomeRNAi; 79679; -.
DR Pharos; Q7Z7D3; Tbio.
DR PRO; PR:Q7Z7D3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z7D3; protein.
DR Bgee; ENSG00000134258; Expressed in palpebral conjunctiva and 89 other tissues.
DR ExpressionAtlas; Q7Z7D3; baseline and differential.
DR Genevisible; Q7Z7D3; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0050868; P:negative regulation of T cell activation; IMP:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0001562; P:response to protozoan; IEA:Ensembl.
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; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Lipoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..282
FT /note="V-set domain-containing T-cell activation inhibitor
FT 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000339237"
FT TOPO_DOM 25..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..146
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 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 VAR_SEQ 1..95
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_045423"
FT VAR_SEQ 33..148
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16782226"
FT /id="VSP_052841"
FT VAR_SEQ 33..87
FT /note="GRHSITVTTVASAGNIGEDGILSCTFEPDIKLSDIVIQWLKEGVLGLVHEFK
FT EGK -> EVSVWLSAMKGWCRSSKASLSIDLCFLNFRETLHHSHYCRLSWEHWGGWNPE
FT LHF (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_052842"
FT VAR_SEQ 88..282
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_052843"
FT CONFLICT 29
FT /note="F -> L (in Ref. 10; ABI16083)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="L -> Q (in Ref. 6; BAB15349)"
FT /evidence="ECO:0000305"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:4GOS"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4GOS"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4GOS"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4GOS"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4GOS"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:4GOS"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4GOS"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:4GOS"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:4GOS"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4GOS"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:4GOS"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4GOS"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:4GOS"
FT STRAND 137..148
FT /evidence="ECO:0007829|PDB:4GOS"
SQ SEQUENCE 282 AA; 30878 MW; 1C9C565A9242E78C CRC64;
MASLGQILFW SIISIIIILA GAIALIIGFG ISGRHSITVT TVASAGNIGE DGILSCTFEP
DIKLSDIVIQ WLKEGVLGLV HEFKEGKDEL SEQDEMFRGR TAVFADQVIV GNASLRLKNV
QLTDAGTYKC YIITSKGKGN ANLEYKTGAF SMPEVNVDYN ASSETLRCEA PRWFPQPTVV
WASQVDQGAN FSEVSNTSFE LNSENVTMKV VSVLYNVTIN NTYSCMIEND IAKATGDIKV
TESEIKRRSH LQLLNSKASL CVSSFFAISW ALLPLSPYLM LK
