ID   VTCN1_RAT               Reviewed;         282 AA.
AC   Q501W4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=V-set domain-containing T-cell activation inhibitor 1;
DE   Flags: Precursor;
GN   Name=Vtcn1 {ECO:0000312|EMBL:AAH95842.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000312|EMBL:AAH95842.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus {ECO:0000312|EMBL:AAH95842.1};
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).
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       (By similarity). {ECO:0000250|UniProtKB:Q7TSP5,
CC       ECO:0000250|UniProtKB:Q7Z7D3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7TSP5};
CC       Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q7TSP5}. Note=Expressed
CC       at the cell surface. A soluble form has also been detected (By
CC       similarity). {ECO:0000250|UniProtKB:Q7TSP5}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q7Z7D3}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC       {ECO:0000250|UniProtKB:Q5ZPR3}.
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DR   EMBL; BC095842; AAH95842.1; -; mRNA.
DR   RefSeq; NP_001019415.1; NM_001024244.1.
DR   AlphaFoldDB; Q501W4; -.
DR   SMR; Q501W4; -.
DR   STRING; 10116.ENSRNOP00000020566; -.
DR   GlyGen; Q501W4; 1 site.
DR   PaxDb; Q501W4; -.
DR   Ensembl; ENSRNOT00000020566; ENSRNOP00000020566; ENSRNOG00000015279.
DR   GeneID; 295322; -.
DR   KEGG; rno:295322; -.
DR   UCSC; RGD:1311204; rat.
DR   CTD; 79679; -.
DR   RGD; 1311204; Vtcn1.
DR   eggNOG; ENOG502S286; Eukaryota.
DR   GeneTree; ENSGT00940000157300; -.
DR   HOGENOM; CLU_013137_8_6_1; -.
DR   InParanoid; Q501W4; -.
DR   OMA; DQNEMFR; -.
DR   OrthoDB; 1040668at2759; -.
DR   PhylomeDB; Q501W4; -.
DR   TreeFam; TF331083; -.
DR   PRO; PR:Q501W4; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000015279; Expressed in ovary and 9 other tissues.
DR   Genevisible; Q501W4; RN.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0050868; P:negative regulation of T cell activation; ISO:RGD.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:RGD.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR   GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0001562; P:response to protozoan; ISO:RGD.
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   2: Evidence at transcript 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_0000339240"
FT   PROPEP          258..282
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000339241"
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"
SQ   SEQUENCE   282 AA;  30664 MW;  A487A8DABF27E41C CRC64;
     MASLGQIIFW SIINVIIILA GAIVLIIGFG ISGKHFITVT TFTSAGNIGE DGTLSCTFEP
     DIKLNGIVIQ WLKEGIKGLV HEFKEGKDDL SQQHEMFRGR TAVFADQVVV GNASLRLKNV
     QLTDAGTYTC YIHTSKGKGN ANLEYKTGAF SMPEINVDYN ASSESLRCEA PRWFPQPTVA
     WASQVDQGAN FSEVSNTSFE LNSENVTMKV VSVLYNVTIN NTYSCMIEND IAKATGDIKV
     TDSEVKRRSQ LELLNSGPSP CVSSVSAAGW ALLSLSCCLM LR