HMR1_MOUSE
ID HMR1_MOUSE Reviewed; 341 AA.
AC Q8HWB0; O19478;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Major histocompatibility complex class I-related gene protein;
DE Short=MHC class I-related gene protein;
DE AltName: Full=Class I histocompatibility antigen-like protein;
DE Flags: Precursor;
GN Name=Mr1; Synonyms=Mr1a;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=9325151; DOI=10.1006/bbrc.1997.7379;
RA Yamaguchi H., Hirai M., Kurosawa Y., Hashimoto K.;
RT "A highly conserved major histocompatibility complex class I-related gene
RT in mammals.";
RL Biochem. Biophys. Res. Commun. 238:697-702(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), ALTERNATIVE SPLICING,
RP AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J, and C57BL/6J X 129/SvJ; TISSUE=Spleen;
RX PubMed=9780177;
RA Riegert P., Wanner V., Bahram S.;
RT "Genomics, isoforms, expression, and phylogeny of the MHC class I-related
RT MR1 gene.";
RL J. Immunol. 161:4066-4077(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; 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 [5]
RP INTERACTION WITH B2M.
RX PubMed=11785959; DOI=10.1006/bbrc.2001.6277;
RA Yamaguchi H., Hashimoto K.;
RT "Association of MR1 protein, an MHC class I-related molecule, with beta(2)-
RT microglobulin.";
RL Biochem. Biophys. Res. Commun. 290:722-729(2002).
RN [6]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-279, AND CAUTION.
RX PubMed=12794138; DOI=10.4049/jimmunol.170.12.6090;
RA Miley M.J., Truscott S.M., Yu Y.Y., Gilfillan S., Fremont D.H.,
RA Hansen T.H., Lybarger L.;
RT "Biochemical features of the MHC-related protein 1 consistent with an
RT immunological function.";
RL J. Immunol. 170:6090-6098(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CAUTION.
RX PubMed=12634786; DOI=10.1038/nature01433;
RA Treiner E., Duban L., Bahram S., Radosavljevic M., Wanner V., Tilloy F.,
RA Affaticati P., Gilfillan S., Lantz O.;
RT "Selection of evolutionarily conserved mucosal-associated invariant T cells
RT by MR1.";
RL Nature 422:164-169(2003).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF TYR-25; ARG-27; PHE-40; LEU-83; GLY-86;
RP LYS-92; ALA-93; GLN-99; TYR-110; ARG-112; LEU-128; TYR-170 AND ALA-181.
RX PubMed=15802267; DOI=10.1074/jbc.m501087200;
RA Huang S., Gilfillan S., Cella M., Miley M.J., Lantz O., Lybarger L.,
RA Fremont D.H., Hansen T.H.;
RT "Evidence for MR1 antigen presentation to mucosal-associated invariant T
RT cells.";
RL J. Biol. Chem. 280:21183-21193(2005).
RN [9]
RP FUNCTION, AND CAUTION.
RX PubMed=20581831; DOI=10.1038/ni.1890;
RA Le Bourhis L., Martin E., Peguillet I., Guihot A., Froux N., Core M.,
RA Levy E., Dusseaux M., Meyssonnier V., Premel V., Ngo C., Riteau B.,
RA Duban L., Robert D., Huang S., Rottman M., Soudais C., Lantz O.;
RT "Antimicrobial activity of mucosal-associated invariant T cells.";
RL Nat. Immunol. 11:701-708(2010).
RN [10]
RP FUNCTION.
RX PubMed=31113973; DOI=10.1038/s41467-019-10198-w;
RA Koay H.F., Gherardin N.A., Xu C., Seneviratna R., Zhao Z., Chen Z.,
RA Fairlie D.P., McCluskey J., Pellicci D.G., Uldrich A.P., Godfrey D.I.;
RT "Diverse MR1-restricted T cells in mice and humans.";
RL Nat. Commun. 10:2243-2243(2019).
CC -!- FUNCTION: Antigen-presenting molecule specialized in displaying
CC microbial pyrimidine-based metabolites to alpha-beta T cell receptors
CC (TCR) on innate-type mucosal-associated invariant T (MAIT) cells. In
CC complex with B2M preferentially presents riboflavin-derived metabolites
CC to semi-invariant TRAV1 TCRs on MAIT cells, guiding immune surveillance
CC of the microbial metabolome at mucosal epithelial barriers
CC (PubMed:20581831, PubMed:15802267). Signature pyrimidine-based
CC microbial antigens are generated via non-enzymatic condensation of
CC metabolite intermediates of the riboflavin pathway with by-products
CC arising from other metabolic pathways such as glycolysis. Typical
CC potent antigenic metabolites are 5-(2-oxoethylideneamino)-6-D-
CC ribitylaminouracil (5-OE-RU) and 5-(2-oxopropylideneamino)-6-D-
CC ribitylaminouracil (5-OP-RU), products of condensation of 5-amino-6-D-
CC ribityaminouracil (5-A-RU) with glyoxal or methylglyoxal by-products,
CC respectively. May present microbial antigens to various TRAV1-negative
CC MAIT cell subsets, providing for unique recognition of diverse
CC microbes, including pathogens that do not synthesize riboflavin. Upon
CC antigen recognition, elicits rapid innate-type MAIT cell activation to
CC eliminate pathogenic microbes by directly killing infected cells (By
CC similarity). During T cell development, drives thymic selection and
CC post-thymic terminal differentiation of MAIT cells in a process
CC dependent on commensal microflora (PubMed:12634786, PubMed:31113973).
CC Acts as an immune sensor of cancer cell metabolome. May present a
CC tumor-specific or -associated metabolite essential for cancer cell
CC survival to a pan-cancer TCR on a non-MAIT CD8-positive T cell clone,
CC triggering T cell-mediated killing of a wide range of cancer cell types
CC (By similarity). {ECO:0000250|UniProtKB:Q95460,
CC ECO:0000269|PubMed:12634786, ECO:0000269|PubMed:15802267,
CC ECO:0000269|PubMed:20581831, ECO:0000269|PubMed:31113973}.
CC -!- SUBUNIT: Heterotrimer that consists of MR1, B2M and metabolite antigen
CC (By similarity). Forms reversible covalent Schiff base complexes with
CC the microbial metabolite, which serve as a molecular switch triggering
CC complete folding, stable association with B2M and translocation of the
CC ternary complex from endoplasmic reticulum to the plasma membrane (By
CC similarity). On antigen-presenting cells, the ternary complex interacts
CC with TCR on CD8-positive T cells (By similarity). The molecular
CC machinery involved in antigen processing remains unknown, but appears
CC to be TAP1-TAP2 and proteasome-independent. Structurally, MR1-B2M
CC heterodimer adopts a topology similar to classical MHC class I
CC molecules, with alpha-1 and alpha-2 domains of MR1 forming the antigen-
CC binding cleft composed of two alpha-helices resting on a floor of 7-
CC stranded anti-parallel beta-pleated sheet (By similarity).
CC {ECO:0000250|UniProtKB:Q95460}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12794138};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q95460}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95460}; Single-
CC pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q95460};
CC Single-pass type I membrane protein {ECO:0000255}. Late endosome
CC membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane
CC protein {ECO:0000255}. Note=In the absence of antigen remains within
CC the endoplasmic reticulum where it acts as a metabolite sensor. Antigen
CC binding triggers trafficking of the ternary complex to the plasma
CC membrane. After presentation, most of these complexes are rapidly
CC internalized and degraded via endocytosis. A small subset recycles via
CC endosomes back to the plasma membrane and may thus acquire and present
CC new antigens that do not efficiently reach the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q95460}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Mr1a;
CC IsoId=Q8HWB0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8HWB0-2; Sequence=VSP_034759;
CC -!- TISSUE SPECIFICITY: Highly expressed thymus. Expressed in liver,
CC kidney, spleen, heart, brain, lung, skeletal muscle and testis.
CC {ECO:0000269|PubMed:9325151, ECO:0000269|PubMed:9780177}.
CC -!- DOMAIN: The alpha-1 domain is a structural part of antigen-binding
CC cleft. {ECO:0000250|UniProtKB:Q95460}.
CC -!- DOMAIN: The alpha-2 domain is a structural part of antigen-binding
CC cleft. {ECO:0000250|UniProtKB:Q95460}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q95460}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice lack invariant MAIT cells due to
CC impaired thymic selection. They show normal development of T, B and NK
CC cells. {ECO:0000269|PubMed:12634786}.
CC -!- MISCELLANEOUS: MR1 is detected in an open versus folded conformation.
CC Only the folded MR1 conformer activates MAIT cells.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
CC -!- CAUTION: Reported to be associated with components of the peptide-
CC loading complex, TAPBP, CALR, CANX and PDIA3 (PubMed:12794138). This
CC association in primary cells and its functional relevance is
CC disputable, given that antigen presentation and MAIT cell activation is
CC shown to be TAP1-TAP2 and proteasome-independent.
CC {ECO:0000269|PubMed:12794138, ECO:0000305|PubMed:12634786,
CC ECO:0000305|PubMed:20581831}.
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DR EMBL; U94989; AAB81345.1; -; mRNA.
DR EMBL; AF068692; AAD17568.1; -; Genomic_DNA.
DR EMBL; AF068691; AAD17568.1; JOINED; Genomic_DNA.
DR EMBL; AF010448; AAD01444.1; -; mRNA.
DR EMBL; AF035672; AAD02040.1; -; Genomic_DNA.
DR EMBL; AK042119; BAC31174.1; -; mRNA.
DR EMBL; BC026137; AAH26137.1; -; mRNA.
DR CCDS; CCDS15383.1; -. [Q8HWB0-1]
DR PIR; JC5663; JC5663.
DR RefSeq; NP_032235.1; NM_008209.4. [Q8HWB0-1]
DR RefSeq; XP_006529207.1; XM_006529144.2.
DR AlphaFoldDB; Q8HWB0; -.
DR SMR; Q8HWB0; -.
DR STRING; 10090.ENSMUSP00000027744; -.
DR GlyGen; Q8HWB0; 1 site.
DR PhosphoSitePlus; Q8HWB0; -.
DR MaxQB; Q8HWB0; -.
DR PaxDb; Q8HWB0; -.
DR PeptideAtlas; Q8HWB0; -.
DR PRIDE; Q8HWB0; -.
DR ProteomicsDB; 273369; -. [Q8HWB0-1]
DR ProteomicsDB; 273370; -. [Q8HWB0-2]
DR Antibodypedia; 34431; 184 antibodies from 26 providers.
DR DNASU; 15064; -.
DR Ensembl; ENSMUST00000027744; ENSMUSP00000027744; ENSMUSG00000026471. [Q8HWB0-1]
DR GeneID; 15064; -.
DR KEGG; mmu:15064; -.
DR UCSC; uc007day.1; mouse. [Q8HWB0-1]
DR CTD; 3140; -.
DR MGI; MGI:1195463; Mr1.
DR VEuPathDB; HostDB:ENSMUSG00000026471; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_0_1_1; -.
DR InParanoid; Q8HWB0; -.
DR OMA; HVEHCGL; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; Q8HWB0; -.
DR TreeFam; TF336617; -.
DR BioGRID-ORCS; 15064; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Mr1; mouse.
DR PRO; PR:Q8HWB0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8HWB0; protein.
DR Bgee; ENSMUSG00000026471; Expressed in thymus and 181 other tissues.
DR ExpressionAtlas; Q8HWB0; baseline and differential.
DR Genevisible; Q8HWB0; MM.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030881; F:beta-2-microglobulin binding; ISS:UniProtKB.
DR GO; GO:0042608; F:T cell receptor binding; ISS:UniProtKB.
DR GO; GO:0019884; P:antigen processing and presentation of exogenous antigen; ISO:MGI.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002854; P:positive regulation of T cell mediated cytotoxicity directed against tumor cell target; ISS:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR001039; MHC_I_a_a1/a2.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR PRINTS; PR01638; MHCCLASSI.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Endosome; Glycoprotein; Golgi apparatus; Immunity; Immunoglobulin domain;
KW Innate immunity; Membrane; MHC I; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..341
FT /note="Major histocompatibility complex class I-related
FT gene protein"
FT /id="PRO_0000344442"
FT TOPO_DOM 19..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 204..278
FT /note="Ig-like C1-type"
FT REGION 19..105
FT /note="Alpha-1"
FT REGION 106..197
FT /note="Alpha-2"
FT REGION 198..289
FT /note="Alpha-3"
FT REGION 290..296
FT /note="Connecting peptide"
FT BINDING 27
FT /ligand="5-(2-oxoethylideneamino)-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78397"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 27
FT /ligand="5-(2-oxopropylideneamino)-6-(D-
FT ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78398"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 42
FT /ligand="5-(2-oxoethylideneamino)-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78397"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 42
FT /ligand="5-(2-oxopropylideneamino)-6-(D-
FT ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78398"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 61
FT /ligand="5-(2-oxoethylideneamino)-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78397"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 61
FT /ligand="5-(2-oxopropylideneamino)-6-(D-
FT ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78398"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 112
FT /ligand="5-(2-oxoethylideneamino)-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78397"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 112
FT /ligand="5-(2-oxopropylideneamino)-6-(D-
FT ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78398"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 170
FT /ligand="5-(2-oxoethylideneamino)-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78397"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 170
FT /ligand="5-(2-oxopropylideneamino)-6-(D-
FT ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78398"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 171
FT /ligand="5-(2-oxoethylideneamino)-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78397"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT BINDING 171
FT /ligand="5-(2-oxopropylideneamino)-6-(D-
FT ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:78398"
FT /ligand_note="pathogen-derived metabolite antigen"
FT /evidence="ECO:0000250|UniProtKB:Q95460"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 218..274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034759"
FT MUTAGEN 25
FT /note="Y->L: Loss of MAIT cell activation."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 27
FT /note="R->V: Loss of MAIT cell activation."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 40
FT /note="F->Y: Impair expression of folded protein."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 83
FT /note="L->K: Loss of MAIT cell activation."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 86
FT /note="G->R: Loss of MAIT cell activation."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 92
FT /note="K->R: Reduced MAIT cell activation."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 93
FT /note="A->V: Activated."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 99
FT /note="Q->R: Activated."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 110
FT /note="Y->I: Impair expression of folded protein."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 112
FT /note="R->E: Loss of MAIT cell activation."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 128
FT /note="L->Q: Impair expression of folded protein."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 170
FT /note="Y->R: Loss of MAIT cell activation."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 181
FT /note="A->E: Reduced MAIT cell activation."
FT /evidence="ECO:0000269|PubMed:15802267"
FT MUTAGEN 279
FT /note="C->G: No effect on cell surface expression."
FT /evidence="ECO:0000269|PubMed:12794138"
SQ SEQUENCE 341 AA; 39391 MW; B21D27227EEFC623 CRC64;
MMLLLPLLAV FLVKRSHTRT HSLRYFRLAV SDPGPVVPEF ISVGYVDSHP ITTYDSVTRQ
KEPKAPWMAE NLAPDHWERY TQLLRGWQQT FKAELRHLQR HYNHSGLHTY QRMIGCELLE
DGSTTGFLQY AYDGQDFIIF NKDTLSWLAM DYVAHITKQA WEANLHELQY QKNWLEEECI
AWLKRFLEYG RDTLERTEHP VVRTTRKETF PGITTFFCRA HGFYPPEISM TWMKNGEEIA
QEVDYGGVLP SGDGTYQTWL SVNLDPQSND VYSCHVEHCG RQMVLEAPRE SGDILRVSTI
SGTTILIIAL AGVGVLIWRR SQELKEVMYQ PTQVNEGSSP S
