HMR1_HUMAN
ID HMR1_HUMAN Reviewed; 341 AA.
AC Q95460; A8K2V9; B4E3B1; O97985; O97986; Q53GM1; Q95HB8; Q9MY23; Q9NPL2;
AC Q9TQB3; Q9TQB9; Q9TQK3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 186.
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;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Thymus;
RX PubMed=7624800; DOI=10.1126/science.7624800;
RA Hashimoto K., Hirai M., Kurosawa Y.;
RT "A gene outside the human MHC related to classical HLA class I genes.";
RL Science 269:693-695(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND POLYMORPHISM.
RC TISSUE=Peripheral blood;
RX PubMed=11019920; DOI=10.1034/j.1399-0039.2000.560211.x;
RA Parra-Cuadrado J.F., Navarro P., Mirones I., Setien F., Oteo M.,
RA Martinez-Naves E.;
RT "A study on the polymorphism of human MHC class I-related MR1 gene and
RT identification of an MR1-like pseudogene.";
RL Tissue Antigens 56:170-172(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Tongue, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney proximal tubule;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11, NUCLEOTIDE SEQUENCE [MRNA] OF
RP 5-341 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 6-229 (ISOFORM 4),
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-341.
RC TISSUE=Placenta;
RX PubMed=9784382; DOI=10.1006/bbrc.1998.9353;
RA Yamaguchi H., Kurosawa Y., Hashimoto K.;
RT "Expanded genomic organization of conserved mammalian MHC class I-related
RT genes, human MR1 and its murine ortholog.";
RL Biochem. Biophys. Res. Commun. 250:558-564(1998).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-109, AND VARIANT ARG-39.
RA Han M., Robinson M.A.;
RT "Unrelated expression patterns of MHC class Ia, Ib and TCRA molecules.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, SIGNAL SEQUENCE CLEAVAGE SITE,
RP GLYCOSYLATION AT ASN-107, INTERACTION WITH B2M, MUTAGENESIS OF CYS-283, AND
RP 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 [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH B2M.
RX PubMed=18068122; DOI=10.1016/j.bbrc.2007.11.156;
RA Aldemir H.;
RT "Novel MHC class I-related molecule MR1 affects MHC class I expression in
RT 293T cells.";
RL Biochem. Biophys. Res. Commun. 366:328-334(2008).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=19760593; DOI=10.14670/hh-24.1439;
RA Gozalbo-Lopez B., Gomez del Moral M., Campos-Martin Y., Setien F.,
RA Martin P., Bellas C., Regueiro J.R., Martinez-Naves E.;
RT "The MHC-related protein 1 (MR1) is expressed by a subpopulation of CD38+,
RT IgA+ cells in the human intestinal mucosa.";
RL Histol. Histopathol. 24:1439-1449(2009).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF GLN-169.
RX PubMed=19416870; DOI=10.1073/pnas.0903196106;
RA Huang S., Martin E., Kim S., Yu L., Soudais C., Fremont D.H., Lantz O.,
RA Hansen T.H.;
RT "MR1 antigen presentation to mucosal-associated invariant T cells was
RT highly conserved in evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8290-8295(2009).
RN [15]
RP FUNCTION.
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 [16]
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), SUBUNIT (ISOFORM 3), AND CAUTION.
RX PubMed=23457030; DOI=10.1002/eji.201242461;
RA Lion J., Debuysscher V., Wlodarczyk A., Hodroge A., Serriari N.E.,
RA Choteau L., Ouled-haddou H., Plistat M., Lassoued K., Lantz O., Treiner E.;
RT "MR1B, a natural spliced isoform of the MHC-related 1 protein, is expressed
RT as homodimers at the cell surface and activates MAIT cells.";
RL Eur. J. Immunol. 43:1363-1373(2013).
RN [17]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22692454; DOI=10.1038/mi.2012.45;
RA Gold M.C., Eid T., Smyk-Pearson S., Eberling Y., Swarbrick G.M.,
RA Langley S.M., Streeter P.R., Lewinsohn D.A., Lewinsohn D.M.;
RT "Human thymic MR1-restricted MAIT cells are innate pathogen-reactive
RT effectors that adapt following thymic egress.";
RL Mucosal Immunol. 6:35-44(2013).
RN [18]
RP FUNCTION.
RX PubMed=27527800; DOI=10.1038/ncomms12506;
RA Meermeier E.W., Laugel B.F., Sewell A.K., Corbett A.J., Rossjohn J.,
RA McCluskey J., Harriff M.J., Franks T., Gold M.C., Lewinsohn D.M.;
RT "Human TRAV1-2-negative MR1-restricted T cells detect S. pyogenes and
RT alternatives to MAIT riboflavin-based antigens.";
RL Nat. Commun. 7:12506-12506(2016).
RN [19]
RP INTERACTION WITH B2M AND VITAMIN B METABOLITE, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND MUTAGENESIS OF LYS-65.
RX PubMed=27043408; DOI=10.1038/ni.3416;
RA McWilliam H.E., Eckle S.B., Theodossis A., Liu L., Chen Z., Wubben J.M.,
RA Fairlie D.P., Strugnell R.A., Mintern J.D., McCluskey J., Rossjohn J.,
RA Villadangos J.A.;
RT "The intracellular pathway for the presentation of vitamin B-related
RT antigens by the antigen-presenting molecule MR1.";
RL Nat. Immunol. 17:531-537(2016).
RN [20]
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).
RN [21]
RP FUNCTION, AND MUTAGENESIS OF LYS-65.
RX PubMed=31959982; DOI=10.1038/s41590-019-0578-8;
RA Crowther M.D., Dolton G., Legut M., Caillaud M.E., Lloyd A., Attaf M.,
RA Galloway S.A.E., Rius C., Farrell C.P., Szomolay B., Ager A., Parker A.L.,
RA Fuller A., Donia M., McCluskey J., Rossjohn J., Svane I.M., Phillips J.D.,
RA Sewell A.K.;
RT "Genome-wide CRISPR-Cas9 screening reveals ubiquitous T cell cancer
RT targeting via the monomorphic MHC class I-related protein MR1.";
RL Nat. Immunol. 21:178-185(2020).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 23-292 IN COMPLEX WITH B2M AND
RP METABOLITE ANTIGEN, ANTIGEN-BINDING SITE, DISULFIDE BONDS, FUNCTION, AND
RP MUTAGENESIS OF LYS-65.
RX PubMed=23051753; DOI=10.1038/nature11605;
RA Kjer-Nielsen L., Patel O., Corbett A.J., Le Nours J., Meehan B., Liu L.,
RA Bhati M., Chen Z., Kostenko L., Reantragoon R., Williamson N.A.,
RA Purcell A.W., Dudek N.L., McConville M.J., O'Hair R.A., Khairallah G.N.,
RA Godfrey D.I., Fairlie D.P., Rossjohn J., McCluskey J.;
RT "MR1 presents microbial vitamin B metabolites to MAIT cells.";
RL Nature 491:717-723(2012).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 23-292 IN COMPLEX WITH B2M AND
RP METABOLITE ANTIGEN, ANTIGEN-BINDING SITES, DOMAIN, INTERACTION WITH TCR,
RP AND FUNCTION.
RX PubMed=23846752; DOI=10.1038/ncomms3142;
RA Patel O., Kjer-Nielsen L., Le Nours J., Eckle S.B., Birkinshaw R.,
RA Beddoe T., Corbett A.J., Liu L., Miles J.J., Meehan B., Reantragoon R.,
RA Sandoval-Romero M.L., Sullivan L.C., Brooks A.G., Chen Z., Fairlie D.P.,
RA McCluskey J., Rossjohn J.;
RT "Recognition of vitamin B metabolites by mucosal-associated invariant T
RT cells.";
RL Nat. Commun. 4:2142-2142(2013).
RN [24] {ECO:0007744|PDB:4NQC, ECO:0007744|PDB:4NQD, ECO:0007744|PDB:4NQE}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 23-292 IN COMPLEXES WITH B2M AND
RP METABOLITE ANTIGENS, DISULFIDE BOND, ANTIGEN-BINDING SITES, DOMAIN,
RP FUNCTION, AND INTERACTION WITH TCR.
RX PubMed=24695216; DOI=10.1038/nature13160;
RA Corbett A.J., Eckle S.B., Birkinshaw R.W., Liu L., Patel O., Mahony J.,
RA Chen Z., Reantragoon R., Meehan B., Cao H., Williamson N.A.,
RA Strugnell R.A., Van Sinderen D., Mak J.Y., Fairlie D.P., Kjer-Nielsen L.,
RA Rossjohn J., McCluskey J.;
RT "T-cell activation by transitory neo-antigens derived from distinct
RT microbial pathways.";
RL Nature 509:361-365(2014).
RN [25] {ECO:0007744|PDB:5D5M, ECO:0007744|PDB:5D7I, ECO:0007744|PDB:5D7J, ECO:0007744|PDB:5D7L}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 23-292 IN COMPLEX WITH B2M AND
RP METABOLITE ANTIGEN, DISULFIDE BOND, ANTIGEN-BINDING SITES, DOMAIN,
RP FUNCTION, AND INTERACTION WITH TCR.
RX PubMed=26795251; DOI=10.1016/j.immuni.2015.12.005;
RA Gherardin N.A., Keller A.N., Woolley R.E., Le Nours J., Ritchie D.S.,
RA Neeson P.J., Birkinshaw R.W., Eckle S.B.G., Waddington J.N., Liu L.,
RA Fairlie D.P., Uldrich A.P., Pellicci D.G., McCluskey J., Godfrey D.I.,
RA Rossjohn J.;
RT "Diversity of T Cells Restricted by the MHC Class I-Related Molecule MR1
RT Facilitates Differential Antigen Recognition.";
RL Immunity 44:32-45(2016).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 23-292 IN COMPLEX WITH B2M AND
RP DRUG, AND ACTIVITY REGULATION.
RX PubMed=28166217; DOI=10.1038/ni.3679;
RA Keller A.N., Eckle S.B., Xu W., Liu L., Hughes V.A., Mak J.Y., Meehan B.S.,
RA Pediongco T., Birkinshaw R.W., Chen Z., Wang H., D'Souza C.,
RA Kjer-Nielsen L., Gherardin N.A., Godfrey D.I., Kostenko L., Corbett A.J.,
RA Purcell A.W., Fairlie D.P., McCluskey J., Rossjohn J.;
RT "Drugs and drug-like molecules can modulate the function of mucosal-
RT associated invariant T cells.";
RL Nat. Immunol. 18:402-411(2017).
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
CC (PubMed:23051753, PubMed:26795251, PubMed:12794138, PubMed:19416870,
CC PubMed:22692454, PubMed:23846752). In complex with B2M preferentially
CC presents riboflavin-derived metabolites to semi-invariant TRAV1-2 TCRs
CC on MAIT cells, guiding immune surveillance of the microbial metabolome
CC at mucosal epithelial barriers (PubMed:26795251, PubMed:24695216,
CC PubMed:20581831). Signature pyrimidine-based microbial antigens are
CC generated via non-enzymatic condensation of metabolite intermediates of
CC the riboflavin pathway with by-products arising from other metabolic
CC pathways such as glycolysis. Typical potent antigenic metabolites are
CC 5-(2-oxoethylideneamino)-6-D-ribitylaminouracil (5-OE-RU) and 5-(2-
CC oxopropylideneamino)-6-D-ribitylaminouracil (5-OP-RU), products of
CC condensation of 5-amino-6-D-ribityaminouracil (5-A-RU) with glyoxal or
CC methylglyoxal by-products, respectively (PubMed:24695216). May present
CC microbial antigens to various TRAV1-2-negative MAIT cell subsets,
CC providing for unique recognition of diverse microbes, including
CC pathogens that do not synthesize riboflavin (PubMed:27527800,
CC PubMed:31113973). Upon antigen recognition, elicits rapid innate-type
CC MAIT cell activation to eliminate pathogenic microbes by directly
CC killing infected cells (PubMed:24695216, PubMed:27527800,
CC PubMed:23846752). During T cell development, drives thymic selection
CC and post-thymic terminal differentiation of MAIT cells in a process
CC dependent on commensal microflora (By similarity). Acts as an immune
CC sensor of cancer cell metabolome (PubMed:31959982). May present a
CC tumor-specific or -associated metabolite essential for cancer cell
CC survival to a pan-cancer TCR consisting of TRAV38.2-DV8*TRAJ31 alpha
CC chain paired with a TRBV25.1*TRBJ2.3 beta chain on a non-MAIT CD8-
CC positive T cell clone (MC.7.G5), triggering T cell-mediated killing of
CC a wide range of cancer cell types (PubMed:31959982).
CC {ECO:0000250|UniProtKB:Q8HWB0, ECO:0000269|PubMed:12794138,
CC ECO:0000269|PubMed:19416870, ECO:0000269|PubMed:20581831,
CC ECO:0000269|PubMed:22692454, ECO:0000269|PubMed:23051753,
CC ECO:0000269|PubMed:23846752, ECO:0000269|PubMed:24695216,
CC ECO:0000269|PubMed:26795251, ECO:0000269|PubMed:27527800,
CC ECO:0000269|PubMed:31113973, ECO:0000269|PubMed:31959982}.
CC -!- ACTIVITY REGULATION: Usually inhibited by pterin-based metabolites such
CC as 6-formylpterin (6-FP, a product of folic acid photodegradation). 6-
CC FP competitively inhibits MAIT cell activation by 5-OP-RU
CC (PubMed:28166217). Modulated by commonly prescribed anti-inflammatory
CC drug metabolites. Inhibited by salicilates such as 3-formylsalicylic
CC and 5-formylsalicylic acids. Activated by diclofenac and/or its hydroxy
CC metabolites (PubMed:28166217). {ECO:0000269|PubMed:28166217}.
CC -!- SUBUNIT: Heterotrimer that consists of MR1, B2M and a metabolite
CC antigen (PubMed:27043408, PubMed:23051753, PubMed:23846752,
CC PubMed:24695216). Forms reversible covalent Schiff base complexes with
CC the microbial metabolite, which serves 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
CC (PubMed:27043408, PubMed:23051753, PubMed:23846752, PubMed:24695216).
CC On antigen-presenting cells, the ternary complex interacts with TCR on
CC CD8-positive T cells (PubMed:23846752, PubMed:24695216,
CC PubMed:26795251). The molecular machinery involved in antigen
CC processing remains unknown, but appears to be TAP1-TAP2 and proteasome-
CC independent. Structurally, MR1-B2M heterodimer adopts a topology
CC similar to classical MHC class I molecules, with alpha-1 and alpha-2
CC domains of MR1 forming the antigen-binding cleft composed of two alpha-
CC helices resting on a floor of 7-stranded anti-parallel beta-pleated
CC sheet (PubMed:23846752, PubMed:24695216, PubMed:26795251). The ribityl
CC moiety of pyrimidine-based antigens is recognized by Tyr-95 residue in
CC the CDR3 alpha loop of the invariant TRAV1-2 TCR (PubMed:23846752,
CC PubMed:24695216, PubMed:26795251). {ECO:0000269|PubMed:23051753,
CC ECO:0000269|PubMed:23846752, ECO:0000269|PubMed:24695216,
CC ECO:0000269|PubMed:26795251, ECO:0000269|PubMed:27043408}.
CC -!- SUBUNIT: [Isoform 3]: Homodimerizes and does not associate with B2M.
CC {ECO:0000269|PubMed:23457030, ECO:0000305|PubMed:20581831}.
CC -!- INTERACTION:
CC Q95460; Q969F0: FATE1; NbExp=3; IntAct=EBI-10280401, EBI-743099;
CC Q95460-1; P61769: B2M; NbExp=3; IntAct=EBI-16016814, EBI-714718;
CC Q95460-2; O95674: CDS2; NbExp=3; IntAct=EBI-12201447, EBI-3913685;
CC Q95460-2; Q07325: CXCL9; NbExp=3; IntAct=EBI-12201447, EBI-3911467;
CC Q95460-2; P54852: EMP3; NbExp=3; IntAct=EBI-12201447, EBI-3907816;
CC Q95460-2; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-12201447, EBI-10976398;
CC Q95460-2; Q969F0: FATE1; NbExp=3; IntAct=EBI-12201447, EBI-743099;
CC Q95460-2; Q8N3T1: GALNT15; NbExp=3; IntAct=EBI-12201447, EBI-3925203;
CC Q95460-2; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-12201447, EBI-10317425;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12794138,
CC ECO:0000269|PubMed:18068122, ECO:0000269|PubMed:27043408}; Single-pass
CC type I membrane protein. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18068122, ECO:0000269|PubMed:27043408}; Single-pass
CC type I membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:18068122}; Single-pass type I membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:27043408};
CC Single-pass type I membrane protein {ECO:0000255}. Late endosome
CC membrane {ECO:0000269|PubMed:18068122, ECO:0000269|PubMed:27043408};
CC Single-pass type I membrane protein {ECO:0000255}. Note=In the absence
CC of antigen remains within the endoplasmic reticulum where it acts as a
CC metabolite sensor. Antigen binding triggers trafficking of the ternary
CC complex to the plasma membrane. After presentation, most of these
CC complexes are rapidly internalized and degraded via endocytosis. A
CC small subset recycles via endosomes back to the plasma membrane and may
CC thus acquire and present new antigens that do not efficiently reach the
CC endoplasmic reticulum. {ECO:0000269|PubMed:27043408}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:23457030}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23457030}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane
CC {ECO:0000269|PubMed:23457030}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23457030}; Single-pass membrane protein
CC {ECO:0000255}. Note=The larger proportion remains in the ER in an
CC immature state. The subset that reach cell surface does it through a
CC B2M-independent pathway. {ECO:0000269|PubMed:23457030}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted
CC {ECO:0000303|PubMed:9780177}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=MR1A;
CC IsoId=Q95460-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95460-2; Sequence=VSP_034755;
CC Name=3; Synonyms=MR1B, MR1D;
CC IsoId=Q95460-3; Sequence=VSP_034757;
CC Name=4; Synonyms=MR1C;
CC IsoId=Q95460-4; Sequence=VSP_034756, VSP_034758;
CC Name=5;
CC IsoId=Q95460-5; Sequence=VSP_043479;
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:7624800, PubMed:9780177). Low
CC expression is detected in peripheral blood B cells, T cells, monocytes
CC and in bronchial epithelial cells (at protein level) (PubMed:27043408).
CC Expressed in plasmablasts or plasma B cells in the lamina propria of
CC ileum, appendix and colon (at protein level) (PubMed:19760593). Highly
CC expressed on a subset of CD45-positive CD3-positive thymocytes (at
CC protein level) (PubMed:22692454). {ECO:0000269|PubMed:19760593,
CC ECO:0000269|PubMed:22692454, ECO:0000269|PubMed:27043408,
CC ECO:0000269|PubMed:7624800, ECO:0000269|PubMed:9780177}.
CC -!- DOMAIN: The alpha-1 domain is a structural part of antigen-binding
CC cleft. {ECO:0000269|PubMed:23846752, ECO:0000269|PubMed:24695216,
CC ECO:0000269|PubMed:26795251}.
CC -!- DOMAIN: The alpha-2 domain is a structural part of antigen-binding
CC cleft. {ECO:0000269|PubMed:24695216, ECO:0000269|PubMed:26795251}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12794138,
CC ECO:0000269|PubMed:27043408}.
CC -!- POLYMORPHISM: Several individuals from different ethnic background were
CC analyzed for polymorphism. MR1 was identical in all individuals
CC analyzed, except one. MR1 is not polymorphic.
CC {ECO:0000269|PubMed:11019920}.
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:23457030,
CC PubMed:12794138). This association in primary cells and its functional
CC relevance is disputable, given that antigen presentation and MAIT cell
CC activation is shown to be TAP1-TAP2 and proteasome-independent.
CC {ECO:0000269|PubMed:12794138, ECO:0000269|PubMed:23457030,
CC ECO:0000305|PubMed:20581831}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD01443.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; U22963; AAC50174.1; -; mRNA.
DR EMBL; AJ249778; CAB77667.1; -; mRNA.
DR EMBL; AK290374; BAF83063.1; -; mRNA.
DR EMBL; AK304645; BAG65423.1; -; mRNA.
DR EMBL; AK222910; BAD96630.1; -; mRNA.
DR EMBL; AL356267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91097.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91098.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91095.1; -; Genomic_DNA.
DR EMBL; BC012485; AAH12485.1; -; mRNA.
DR EMBL; AF010446; AAD01442.1; -; mRNA.
DR EMBL; AF010447; AAD01443.1; ALT_INIT; mRNA.
DR EMBL; AF031469; AAD01933.1; -; mRNA.
DR EMBL; AF039526; AAD02172.1; -; Genomic_DNA.
DR EMBL; AH006983; AAC72900.1; -; Genomic_DNA.
DR EMBL; AF223407; AAF40170.1; -; Genomic_DNA.
DR CCDS; CCDS1342.1; -. [Q95460-1]
DR CCDS; CCDS53440.1; -. [Q95460-3]
DR CCDS; CCDS53441.1; -. [Q95460-5]
DR CCDS; CCDS53442.1; -. [Q95460-2]
DR PIR; A57136; A57136.
DR RefSeq; NP_001181928.1; NM_001194999.1. [Q95460-2]
DR RefSeq; NP_001181929.1; NM_001195000.1. [Q95460-3]
DR RefSeq; NP_001181964.1; NM_001195035.1. [Q95460-5]
DR RefSeq; NP_001522.1; NM_001531.2. [Q95460-1]
DR PDB; 4GUP; X-ray; 3.20 A; A/C=23-292.
DR PDB; 4L4T; X-ray; 2.00 A; A/C=23-292.
DR PDB; 4L4V; X-ray; 1.90 A; A/C=23-292.
DR PDB; 4LCW; X-ray; 2.40 A; A/C=23-292.
DR PDB; 4NQC; X-ray; 2.50 A; A/C=23-292.
DR PDB; 4NQD; X-ray; 2.20 A; A/C=23-292.
DR PDB; 4NQE; X-ray; 2.10 A; A/C=23-292.
DR PDB; 4PJ5; X-ray; 2.00 A; A/C=23-292.
DR PDB; 4PJ7; X-ray; 2.50 A; A/C=23-292.
DR PDB; 4PJ8; X-ray; 3.30 A; A=23-292.
DR PDB; 4PJ9; X-ray; 2.00 A; A=23-292.
DR PDB; 4PJA; X-ray; 2.68 A; A/C=23-292.
DR PDB; 4PJB; X-ray; 2.85 A; A/C=23-292.
DR PDB; 4PJC; X-ray; 2.50 A; A/C=23-292.
DR PDB; 4PJD; X-ray; 2.78 A; A/C=23-292.
DR PDB; 4PJE; X-ray; 1.95 A; A/C=23-292.
DR PDB; 4PJF; X-ray; 2.45 A; A/C=23-292.
DR PDB; 4PJG; X-ray; 2.40 A; A/C=23-292.
DR PDB; 4PJH; X-ray; 2.00 A; A/C=23-292.
DR PDB; 4PJI; X-ray; 2.50 A; A/C=23-292.
DR PDB; 4PJX; X-ray; 2.25 A; A/C=23-292.
DR PDB; 5D5M; X-ray; 2.20 A; A/C=23-292.
DR PDB; 5D7I; X-ray; 2.00 A; A/C=23-292.
DR PDB; 5D7J; X-ray; 1.97 A; C/E=23-292.
DR PDB; 5D7L; X-ray; 3.40 A; A/C=23-292.
DR PDB; 5U16; X-ray; 2.00 A; A/C=23-292.
DR PDB; 5U17; X-ray; 2.15 A; A/C=23-292.
DR PDB; 5U1R; X-ray; 2.70 A; A/C=23-292.
DR PDB; 5U2V; X-ray; 2.20 A; A/C=23-292.
DR PDB; 5U6Q; X-ray; 1.90 A; A/C=23-292.
DR PDB; 5U72; X-ray; 2.50 A; A/C=23-292.
DR PDB; 6MWR; X-ray; 3.30 A; A=23-292.
DR PDB; 6PUC; X-ray; 1.85 A; A/C=23-292.
DR PDB; 6PUD; X-ray; 1.80 A; A/C=23-292.
DR PDB; 6PUE; X-ray; 1.90 A; A/C=23-292.
DR PDB; 6PUF; X-ray; 1.92 A; A/C=23-292.
DR PDB; 6PUG; X-ray; 1.80 A; A/C=23-292.
DR PDB; 6PUH; X-ray; 1.88 A; A/C=23-292.
DR PDB; 6PUI; X-ray; 1.96 A; A/C=23-292.
DR PDB; 6PUJ; X-ray; 1.92 A; A/C=23-292.
DR PDB; 6PUK; X-ray; 2.08 A; A/C=23-292.
DR PDB; 6PUL; X-ray; 1.84 A; A/C=23-292.
DR PDB; 6PUM; X-ray; 1.96 A; A/C=23-292.
DR PDB; 6PVC; X-ray; 1.96 A; A/C=23-292.
DR PDB; 6PVD; X-ray; 2.14 A; A/C=23-292.
DR PDB; 6W9U; X-ray; 1.89 A; A/C=23-292.
DR PDB; 6W9V; X-ray; 1.95 A; A/C=23-292.
DR PDB; 6XQP; X-ray; 2.90 A; A/C=23-292.
DR PDB; 7LLI; X-ray; 3.20 A; A/C=23-292.
DR PDB; 7LLJ; X-ray; 3.15 A; C/E=23-292.
DR PDBsum; 4GUP; -.
DR PDBsum; 4L4T; -.
DR PDBsum; 4L4V; -.
DR PDBsum; 4LCW; -.
DR PDBsum; 4NQC; -.
DR PDBsum; 4NQD; -.
DR PDBsum; 4NQE; -.
DR PDBsum; 4PJ5; -.
DR PDBsum; 4PJ7; -.
DR PDBsum; 4PJ8; -.
DR PDBsum; 4PJ9; -.
DR PDBsum; 4PJA; -.
DR PDBsum; 4PJB; -.
DR PDBsum; 4PJC; -.
DR PDBsum; 4PJD; -.
DR PDBsum; 4PJE; -.
DR PDBsum; 4PJF; -.
DR PDBsum; 4PJG; -.
DR PDBsum; 4PJH; -.
DR PDBsum; 4PJI; -.
DR PDBsum; 4PJX; -.
DR PDBsum; 5D5M; -.
DR PDBsum; 5D7I; -.
DR PDBsum; 5D7J; -.
DR PDBsum; 5D7L; -.
DR PDBsum; 5U16; -.
DR PDBsum; 5U17; -.
DR PDBsum; 5U1R; -.
DR PDBsum; 5U2V; -.
DR PDBsum; 5U6Q; -.
DR PDBsum; 5U72; -.
DR PDBsum; 6MWR; -.
DR PDBsum; 6PUC; -.
DR PDBsum; 6PUD; -.
DR PDBsum; 6PUE; -.
DR PDBsum; 6PUF; -.
DR PDBsum; 6PUG; -.
DR PDBsum; 6PUH; -.
DR PDBsum; 6PUI; -.
DR PDBsum; 6PUJ; -.
DR PDBsum; 6PUK; -.
DR PDBsum; 6PUL; -.
DR PDBsum; 6PUM; -.
DR PDBsum; 6PVC; -.
DR PDBsum; 6PVD; -.
DR PDBsum; 6W9U; -.
DR PDBsum; 6W9V; -.
DR PDBsum; 6XQP; -.
DR PDBsum; 7LLI; -.
DR PDBsum; 7LLJ; -.
DR AlphaFoldDB; Q95460; -.
DR SMR; Q95460; -.
DR BioGRID; 109385; 135.
DR DIP; DIP-59986N; -.
DR IntAct; Q95460; 16.
DR STRING; 9606.ENSP00000477563; -.
DR DrugBank; DB00098; Antithymocyte immunoglobulin (rabbit).
DR GlyGen; Q95460; 1 site.
DR iPTMnet; Q95460; -.
DR PhosphoSitePlus; Q95460; -.
DR BioMuta; MR1; -.
DR DMDM; 74751679; -.
DR EPD; Q95460; -.
DR jPOST; Q95460; -.
DR MassIVE; Q95460; -.
DR PaxDb; Q95460; -.
DR PeptideAtlas; Q95460; -.
DR PRIDE; Q95460; -.
DR ProteomicsDB; 75731; -. [Q95460-1]
DR ProteomicsDB; 75732; -. [Q95460-2]
DR ProteomicsDB; 75733; -. [Q95460-3]
DR ProteomicsDB; 75734; -. [Q95460-4]
DR ProteomicsDB; 75735; -. [Q95460-5]
DR Antibodypedia; 34431; 184 antibodies from 26 providers.
DR DNASU; 3140; -.
DR Ensembl; ENST00000282990.10; ENSP00000282990.6; ENSG00000153029.16. [Q95460-3]
DR Ensembl; ENST00000367579.7; ENSP00000356551.3; ENSG00000153029.16. [Q95460-2]
DR Ensembl; ENST00000367580.6; ENSP00000356552.5; ENSG00000153029.16. [Q95460-1]
DR Ensembl; ENST00000434571.7; ENSP00000388504.2; ENSG00000153029.16. [Q95460-5]
DR Ensembl; ENST00000614012.5; ENSP00000477563.1; ENSG00000153029.16. [Q95460-1]
DR GeneID; 3140; -.
DR KEGG; hsa:3140; -.
DR MANE-Select; ENST00000367580.6; ENSP00000356552.5; NM_001385161.1; NP_001372090.1.
DR UCSC; uc001goq.2; human. [Q95460-1]
DR CTD; 3140; -.
DR DisGeNET; 3140; -.
DR GeneCards; MR1; -.
DR HGNC; HGNC:4975; MR1.
DR HPA; ENSG00000153029; Low tissue specificity.
DR MalaCards; MR1; -.
DR MIM; 600764; gene.
DR neXtProt; NX_Q95460; -.
DR OpenTargets; ENSG00000153029; -.
DR PharmGKB; PA29309; -.
DR VEuPathDB; HostDB:ENSG00000153029; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_0_1_1; -.
DR InParanoid; Q95460; -.
DR OMA; HVEHCGL; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; Q95460; -.
DR TreeFam; TF336617; -.
DR PathwayCommons; Q95460; -.
DR SignaLink; Q95460; -.
DR BioGRID-ORCS; 3140; 7 hits in 1072 CRISPR screens.
DR ChiTaRS; MR1; human.
DR GeneWiki; Major_histocompatibility_complex,_class_I-related; -.
DR GenomeRNAi; 3140; -.
DR Pharos; Q95460; Tbio.
DR PRO; PR:Q95460; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q95460; protein.
DR Bgee; ENSG00000153029; Expressed in type B pancreatic cell and 181 other tissues.
DR Genevisible; Q95460; HS.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA: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; IDA:UniProtKB.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030881; F:beta-2-microglobulin binding; IDA:UniProtKB.
DR GO; GO:0032393; F:MHC class I receptor activity; TAS:UniProtKB.
DR GO; GO:0042608; F:T cell receptor binding; IDA:UniProtKB.
DR GO; GO:0019884; P:antigen processing and presentation of exogenous antigen; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
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; IDA:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISS: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 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Immunity;
KW Immunoglobulin domain; Innate immunity; Membrane; MHC I;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:12794138"
FT CHAIN 23..341
FT /note="Major histocompatibility complex class I-related
FT gene protein"
FT /id="PRO_0000344441"
FT TOPO_DOM 23..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 203..299
FT /note="Ig-like C1-type"
FT REGION 23..201
FT /note="Antigen-binding cleft"
FT /evidence="ECO:0000269|PubMed:24695216"
FT REGION 23..109
FT /note="Alpha-1"
FT /evidence="ECO:0000255"
FT REGION 110..201
FT /note="Alpha-2"
FT /evidence="ECO:0000255"
FT REGION 202..293
FT /note="Alpha-3"
FT /evidence="ECO:0000255"
FT REGION 294..302
FT /note="Connecting peptide"
FT BINDING 31
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:0000269|PubMed:24695216,
FT ECO:0007744|PDB:4NQE"
FT BINDING 31
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:0000269|PubMed:24695216,
FT ECO:0000269|PubMed:26795251, ECO:0007744|PDB:4NQC,
FT ECO:0007744|PDB:5D5M"
FT BINDING 46
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:0000269|PubMed:24695216,
FT ECO:0007744|PDB:4NQE"
FT BINDING 46
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:0000269|PubMed:24695216,
FT ECO:0000269|PubMed:26795251, ECO:0007744|PDB:4NQC,
FT ECO:0007744|PDB:5D5M"
FT BINDING 65
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:0000269|PubMed:24695216,
FT ECO:0007744|PDB:4NQE"
FT BINDING 65
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:0000269|PubMed:24695216,
FT ECO:0000269|PubMed:26795251, ECO:0007744|PDB:4NQC,
FT ECO:0007744|PDB:5D5M"
FT BINDING 116
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:0000269|PubMed:24695216,
FT ECO:0007744|PDB:4NQE"
FT BINDING 116
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:0000269|PubMed:24695216,
FT ECO:0000269|PubMed:26795251, ECO:0007744|PDB:4NQC,
FT ECO:0007744|PDB:5D5M"
FT BINDING 174
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:0000269|PubMed:24695216,
FT ECO:0007744|PDB:4NQE"
FT BINDING 174
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:0000269|PubMed:24695216,
FT ECO:0000269|PubMed:26795251, ECO:0007744|PDB:4NQC,
FT ECO:0007744|PDB:5D5M"
FT BINDING 175
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:0000269|PubMed:24695216,
FT ECO:0007744|PDB:4NQE"
FT BINDING 175
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:0000269|PubMed:24695216,
FT ECO:0000269|PubMed:26795251, ECO:0007744|PDB:4NQC,
FT ECO:0007744|PDB:5D5M"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12794138"
FT DISULFID 120..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23051753, ECO:0000269|PubMed:24695216,
FT ECO:0000269|PubMed:26795251"
FT DISULFID 222..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23051753, ECO:0000269|PubMed:24695216,
FT ECO:0000269|PubMed:26795251"
FT VAR_SEQ 110..154
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034755"
FT VAR_SEQ 202..328
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043479"
FT VAR_SEQ 202..220
FT /note="EPPLVRVNRKETFPGVTAL -> GKEKEKASFPHCLNNCFYT (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:9780177"
FT /id="VSP_034756"
FT VAR_SEQ 203..294
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9780177"
FT /id="VSP_034757"
FT VAR_SEQ 221..341
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9780177"
FT /id="VSP_034758"
FT VARIANT 39
FT /note="H -> R (in dbSNP:rs2236410)"
FT /evidence="ECO:0000269|Ref.10"
FT /id="VAR_045608"
FT VARIANT 63
FT /note="R -> Q (in dbSNP:rs3897433)"
FT /id="VAR_045609"
FT VARIANT 77
FT /note="A -> V (in dbSNP:rs3897434)"
FT /id="VAR_045610"
FT MUTAGEN 65
FT /note="K->A: Associates with B2M and translocates to plasma
FT membrane in the absence of 6-FP. Impairs recognition by
FT pan-cancer TCR, MC.7.G5."
FT /evidence="ECO:0000269|PubMed:27043408,
FT ECO:0000269|PubMed:31959982"
FT MUTAGEN 65
FT /note="K->R: Fails to refold in the presence of 6-FP.
FT Impairs the association with B2M and translocation to the
FT plasma membrane."
FT /evidence="ECO:0000269|PubMed:23051753,
FT ECO:0000269|PubMed:27043408"
FT MUTAGEN 169
FT /note="Q->L: Able to activate mouse MAIT cells (xeno-
FT reactivity)."
FT /evidence="ECO:0000269|PubMed:19416870"
FT MUTAGEN 283
FT /note="C->G: No effect on cell surface expression."
FT /evidence="ECO:0000269|PubMed:12794138"
FT CONFLICT 117
FT /note="M -> V (in Ref. 3; BAF83063)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="R -> G (in Ref. 4; BAD96630)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="L -> P (in Ref. 4; BAD96630)"
FT /evidence="ECO:0000305"
FT STRAND 25..36
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:5D7J"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6PUD"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6PUD"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6MWR"
FT HELIX 78..106
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:6PUD"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:6PUD"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:6PUD"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:6PUD"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:6PUD"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5U1R"
FT STRAND 219..230
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:6PUD"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:4PJ9"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6PUG"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:6PUD"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:6PUD"
SQ SEQUENCE 341 AA; 39366 MW; 2990C1F3F0A1CAD9 CRC64;
MGELMAFLLP LIIVLMVKHS DSRTHSLRYF RLGVSDPIHG VPEFISVGYV DSHPITTYDS
VTRQKEPRAP WMAENLAPDH WERYTQLLRG WQQMFKVELK RLQRHYNHSG SHTYQRMIGC
ELLEDGSTTG FLQYAYDGQD FLIFNKDTLS WLAVDNVAHT IKQAWEANQH ELLYQKNWLE
EECIAWLKRF LEYGKDTLQR TEPPLVRVNR KETFPGVTAL FCKAHGFYPP EIYMTWMKNG
EEIVQEIDYG DILPSGDGTY QAWASIELDP QSSNLYSCHV EHCGVHMVLQ VPQESETIPL
VMKAVSGSIV LVIVLAGVGV LVWRRRPREQ NGAIYLPTPD R
