CRTAM_MOUSE
ID CRTAM_MOUSE Reviewed; 393 AA.
AC Q149L7; A0A087WPL6; M0QWH9; Q3TQA9; Q9CVZ9; Q9Z151;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cytotoxic and regulatory T-cell molecule;
DE AltName: Full=Class-I MHC-restricted T-cell-associated molecule;
DE AltName: CD_antigen=CD355;
DE Flags: Precursor;
GN Name=Crtam {ECO:0000312|MGI:MGI:1859822};
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 [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Thymocyte;
RX PubMed=10811014; DOI=10.1002/jlb.67.5.725;
RA Kennedy J., Vicari A.P., Saylor V., Zurawski S.M., Copeland N.G.,
RA Gilbert D.J., Jenkins N.A., Zlotnik A.;
RT "A molecular analysis of NKT cells: identification of a class-I restricted
RT T cell-associated molecule (CRTAM).";
RL J. Leukoc. Biol. 67:725-734(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 80-389 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE37475.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAE37475.1}, and
RC Testis {ECO:0000312|EMBL:BAB24204.2};
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 [5]
RP FUNCTION, INTERACTION WITH CADM1, AND TISSUE SPECIFICITY.
RX PubMed=15811952; DOI=10.1182/blood-2005-02-0817;
RA Boles K.S., Barchet W., Diacovo T., Cella M., Colonna M.;
RT "The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell
RT responses through the cell-surface receptor CRTAM.";
RL Blood 106:779-786(2005).
RN [6]
RP INTERACTION WITH CADM1.
RX PubMed=15781451; DOI=10.1074/jbc.m502095200;
RA Galibert L., Diemer G.S., Liu Z., Johnson R.S., Smith J.L., Walzer T.,
RA Comeau M.R., Rauch C.T., Wolfson M.F., Sorensen R.A.,
RA Van der Vuurst de Vries A.-R., Branstetter D.G., Koelling R.M.,
RA Scholler J., Fanslow W.C., Baum P.R., Derry J.M., Yan W.;
RT "Nectin-like protein 2 defines a subset of T-cell zone dendritic cells and
RT is a ligand for class-I-restricted T-cell-associated molecule.";
RL J. Biol. Chem. 280:21955-21964(2005).
RN [7]
RP FUNCTION, INTERACTION WITH SCRIB, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DOMAIN, MOTIF, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 390-GLU--VAL-393.
RX PubMed=18329370; DOI=10.1016/j.cell.2008.01.013;
RA Yeh J.H., Sidhu S.S., Chan A.C.;
RT "Regulation of a late phase of T cell polarity and effector functions by
RT Crtam.";
RL Cell 132:846-859(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19752223; DOI=10.4049/jimmunol.0901248;
RA Takeuchi A., Itoh Y., Takumi A., Ishihara C., Arase N., Yokosuka T.,
RA Koseki H., Yamasaki S., Takai Y., Miyoshi J., Ogasawara K., Saito T.;
RT "CRTAM confers late-stage activation of CD8+ T cells to regulate retention
RT within lymph node.";
RL J. Immunol. 183:4220-4228(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24687959; DOI=10.1084/jem.20130904;
RA Cortez V.S., Cervantes-Barragan L., Song C., Gilfillan S., McDonald K.G.,
RA Tussiwand R., Edelson B.T., Murakami Y., Murphy K.M., Newberry R.D.,
RA Sibley L.D., Colonna M.;
RT "CRTAM controls residency of gut CD4+CD8+ T cells in the steady state and
RT maintenance of gut CD4+ Th17 during parasitic infection.";
RL J. Exp. Med. 211:623-633(2014).
CC -!- FUNCTION: Mediates heterophilic cell-cell adhesion which regulates the
CC activation, differentiation and tissue retention of various T-cell
CC subsets (PubMed:15811952, PubMed:18329370, PubMed:19752223,
CC PubMed:24687959). Interaction with CADM1 promotes natural killer (NK)
CC cell cytotoxicity and IFNG/interferon-gamma secretion by CD8+ T-cells
CC in vitro as well as NK cell-mediated rejection of tumors expressing
CC CADM1 in vivo (PubMed:15811952). Regulates CD8+ T-cell proliferation in
CC response to T-cell receptor (TCR) activation (PubMed:18329370). Appears
CC to be dispensable for CD8+ T-cell-mediated cytotoxicity
CC (PubMed:19752223). Interaction with SCRIB promotes the late phase of
CC cellular polarization of a subset of CD4+ T-cells, which in turn
CC regulates TCR-mediated proliferation and IFNG, IL17 and IL22 production
CC (PubMed:18329370). By interacting with CADM1 on CD8+ dendritic cells,
CC regulates the retention of activated CD8+ T-cells within the draining
CC lymph node (PubMed:19752223). Required for the intestinal retention of
CC intraepithelial CD4+ CD8+ T-cells and, to a lesser extent,
CC intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells
CC (PubMed:24687959). Interaction with CADM1 promotes the adhesion to gut-
CC associated CD103+ dendritic cells, which may facilitate the expression
CC of gut-homing and adhesion molecules on T-cells and the conversion of
CC CD4+ T-cells into CD4+ CD8+ T-cells (PubMed:24687959).
CC {ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:18329370,
CC ECO:0000269|PubMed:19752223, ECO:0000269|PubMed:24687959}.
CC -!- SUBUNIT: Monomer (By similarity). May form homodimer (via Ig-like V-
CC type domain) (By similarity). Interacts (via Ig-like V-type domain)
CC with CADM1 (via Ig-like V-type domain); the interaction competes with
CC CRTAM homodimerization and CADM1 homodimerization (PubMed:15781451,
CC PubMed:15811952). Interacts (via PDZ-binding motif) with SCRIB (via PDZ
CC domain 3); the interaction promotes CRTAM and SCRIB polarization in a
CC subset of CD4+ T-cells (PubMed:18329370).
CC {ECO:0000250|UniProtKB:O95727, ECO:0000269|PubMed:15781451,
CC ECO:0000269|PubMed:15811952, ECO:0000269|PubMed:18329370}.
CC -!- INTERACTION:
CC Q149L7; Q80U72: Scrib; NbExp=4; IntAct=EBI-1766072, EBI-1766028;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18329370,
CC ECO:0000269|PubMed:19752223, ECO:0000269|PubMed:24687959}; Single-pass
CC type I membrane protein {ECO:0000255}. Note=In a subset of CD4+ T-
CC cells, colocalizes with SCRIB at the immunological synapse during the
CC late phase of T-cell activation. {ECO:0000269|PubMed:18329370}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q149L7-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:16141072};
CC IsoId=Q149L7-2; Sequence=VSP_052473, VSP_052474;
CC Name=3 {ECO:0000303|PubMed:10811014};
CC IsoId=Q149L7-3; Sequence=VSP_059946;
CC -!- TISSUE SPECIFICITY: In the immune system, expression is restricted to
CC activated class-I MHC-restricted cells, including NKT, NK and CD8+ T-
CC cells (at protein level) (PubMed:10811014, PubMed:15811952,
CC PubMed:18329370, PubMed:19752223). Transiently expressed in activated
CC CD8+ T-cells and a subset of activated CD4+ T-cells (at protein level)
CC (PubMed:18329370). Expressed in activated intestinal T-cells,
CC specifically intraepithelial CD4+ CD8+ T-cells, intraepithelial CD4+ T-
CC cells and, CD8+ T-cells in the intestine epithelium, lamina propria,
CC Peyer's Patches and mesenteric lymph nodes (PubMed:24687959). Also
CC expressed in spleen, brain and testis (PubMed:10811014).
CC {ECO:0000269|PubMed:10811014, ECO:0000269|PubMed:15811952,
CC ECO:0000269|PubMed:18329370, ECO:0000269|PubMed:19752223,
CC ECO:0000269|PubMed:24687959}.
CC -!- DOMAIN: The extracellular domain is required for the regulation of IFNG
CC and IL22 production, but is dispensable for late T-cell polarization.
CC {ECO:0000269|PubMed:18329370}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:18329370,
CC PubMed:19752223). In the small intestine mucosa and under steady-state
CC conditions, severe reduction in the number of intraepithelial CD4+ CD8+
CC T-cells and, partial reduction in the number of lamina propria and
CC intraepithelial CD8+ and CD4+ T-cells (PubMed:24687959). In intestinal
CC CD4+ T-cells, expression of gut-retention molecules Itgae/CD103 and
CC Cd69, and gut-homing molecule Ccr9 is reduced (PubMed:24687959).
CC Development of lymphocytes and myeloid cells is normal
CC (PubMed:18329370, PubMed:19752223). However, in older mice, the number
CC of CD4+ and CD8+ T-cells is increased in lymph nodes and blood
CC (PubMed:18329370). Susceptible to oral infection with bacterium
CC C.rodentium resulting in higher bacteria load in the colon and spleen
CC (PubMed:18329370). However, in another study, the mice were not
CC susceptible to oral infection with bacterium C.rodentium
CC (PubMed:24687959). Impaired immune response following intranasal
CC infection with influenza virus caused by a decrease in the number of
CC antigen-specific CD8+ T-cells in the infected lung (PubMed:19752223).
CC However, the capacity of CD8+ T-cells to kill infected cells is not
CC affected (PubMed:19752223). Increased resistance to oral infection with
CC intracellular parasite T.gondii caused by a reduced number of IL17-
CC producing CD4+ T-cells resulting in enhanced clearance of the parasite
CC (PubMed:24687959). {ECO:0000269|PubMed:18329370,
CC ECO:0000269|PubMed:19752223, ECO:0000269|PubMed:24687959}.
CC -!- SIMILARITY: Belongs to the nectin family.
CC {ECO:0000250|UniProtKB:O95727}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24204.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB24204.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF001104; AAC80266.1; -; mRNA.
DR EMBL; AK005719; BAB24204.2; ALT_SEQ; mRNA.
DR EMBL; AK163744; BAE37475.1; -; mRNA.
DR EMBL; AC159820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117716; AAI17717.1; -; mRNA.
DR CCDS; CCDS40593.2; -. [Q149L7-3]
DR CCDS; CCDS72216.1; -. [Q149L7-1]
DR RefSeq; NP_001268883.1; NM_001281954.1. [Q149L7-1]
DR RefSeq; NP_062338.3; NM_019465.4. [Q149L7-3]
DR AlphaFoldDB; Q149L7; -.
DR SMR; Q149L7; -.
DR IntAct; Q149L7; 1.
DR STRING; 10090.ENSMUSP00000137837; -.
DR GlyGen; Q149L7; 2 sites.
DR PhosphoSitePlus; Q149L7; -.
DR PaxDb; Q149L7; -.
DR PRIDE; Q149L7; -.
DR ProteomicsDB; 284024; -. [Q149L7-1]
DR ProteomicsDB; 316411; -.
DR ProteomicsDB; 318036; -.
DR Antibodypedia; 32807; 264 antibodies from 25 providers.
DR DNASU; 54698; -.
DR Ensembl; ENSMUST00000180384; ENSMUSP00000137837; ENSMUSG00000032021. [Q149L7-1]
DR Ensembl; ENSMUST00000180872; ENSMUSP00000137749; ENSMUSG00000032021. [Q149L7-2]
DR Ensembl; ENSMUST00000188848; ENSMUSP00000139826; ENSMUSG00000032021. [Q149L7-3]
DR GeneID; 54698; -.
DR KEGG; mmu:54698; -.
DR UCSC; uc009pad.1; mouse. [Q149L7-2]
DR CTD; 56253; -.
DR MGI; MGI:1859822; Crtam.
DR VEuPathDB; HostDB:ENSMUSG00000032021; -.
DR eggNOG; ENOG502RYH2; Eukaryota.
DR GeneTree; ENSGT00940000159804; -.
DR InParanoid; Q149L7; -.
DR OMA; AFLTNHT; -.
DR OrthoDB; 753787at2759; -.
DR PhylomeDB; Q149L7; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 54698; 3 hits in 68 CRISPR screens.
DR PRO; PR:Q149L7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q149L7; protein.
DR Bgee; ENSMUSG00000032021; Expressed in cerebellar cortex and 43 other tissues.
DR ExpressionAtlas; Q149L7; baseline and differential.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0008037; P:cell recognition; IDA:UniProtKB.
DR GO; GO:0051606; P:detection of stimulus; IDA:UniProtKB.
DR GO; GO:0002355; P:detection of tumor cell; IDA:UniProtKB.
DR GO; GO:0001768; P:establishment of T cell polarity; IDA:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:UniProtKB.
DR GO; GO:0097021; P:lymphocyte migration into lymphoid organs; IMP:UniProtKB.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:0002860; P:positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IDA:UniProtKB.
DR GO; GO:2001185; P:regulation of CD8-positive, alpha-beta T cell activation; IMP:UniProtKB.
DR GO; GO:0050863; P:regulation of T cell activation; IMP:UniProtKB.
DR GO; GO:0045580; P:regulation of T cell differentiation; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013162; CD80_C2-set.
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; PF08205; C2-set_2; 1.
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 Adaptive immunity; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..393
FT /note="Cytotoxic and regulatory T-cell molecule"
FT /id="PRO_0000292603"
FT TOPO_DOM 17..289
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 17..111
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255"
FT DOMAIN 119..208
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT REGION 218..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 390..393
FT /note="PDZ-binding"
FT /evidence="ECO:0000305|PubMed:18329370"
FT COMPBIAS 226..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 139..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..197
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052473"
FT VAR_SEQ 198..214
FT /note="HEGLHGRKLVAPFQFED -> MWLKLISVVAEFCFSPF (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052474"
FT VAR_SEQ 275
FT /note="Missing (in isoform 3)"
FT /id="VSP_059946"
FT MUTAGEN 390..393
FT /note="Missing: In response to TCR stimulation, increases
FT CD4+ T-cell proliferation and impairs IFNG and IL22
FT production."
FT /evidence="ECO:0000269|PubMed:18329370"
FT CONFLICT 5
FT /note="A -> V (in Ref. 1; AAC80266 and 4; AAI17717)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="N -> H (in Ref. 1; AAC80266 and 4; AAI17717)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="M -> T (in Ref. 1; AAC80266 and 4; AAI17717)"
FT /evidence="ECO:0000305"
FT CONFLICT 222..225
FT /note="Missing (in Ref. 1; AAC80266 and 4; AAI17717)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="S -> L (in Ref. 2; BAB24204)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="R -> Q (in Ref. 1; AAC80266 and 4; AAI17717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 43907 MW; 74666FFB7844D2B3 CRC64;
MWWGALSLLF WVPVQAAFLK METVTVEEGQ TLTLTCVTSQ TKNVSLQWLA PSGFTIFLNQ
HPALKSSKYQ LLHHSATQLS ISVSNVTLRE EGVYTCLHYG SSVKTKQVRV TVLVTPFQPT
VEALVLRRQN GEKSVVLKCS TERSKPPPQI TWLLGEGLEI YGELNHEFEA DGKICNTSSM
LIARAYGKNS TVHCIIQHEG LHGRKLVAPF QFEDLVADQE TSDQETSDAP EQSSLSSQAL
QQPTSTVSMM ENSSIPETDK EEKEHATQDP GLSTEASAQH TGLARRKSGI LLLTLVSFLI
FILFIIVQLF IMKLRKAHVV WKKESEISEQ ALESYRSRSN NEETSSQENS SQAPQSKRCM
NYITRLYSGA KTKKSAQHWK LGGKHSRVPE SIV
