HMR1_PONAB
ID HMR1_PONAB Reviewed; 340 AA.
AC Q5RD09;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Major histocompatibility complex class I-related gene protein;
DE AltName: Full=MHC class I-related gene protein;
DE Flags: Precursor;
GN Name=MR1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Antigen-presenting molecule specialized in presenting
CC microbial vitamin B metabolites. Involved in the development and
CC expansion of a small population of T-cells expressing an invariant T-
CC cell receptor alpha chain called mucosal-associated invariant T-cells
CC (MAIT). MAIT lymphocytes are preferentially located in the gut lamina
CC propria and therefore may be involved in monitoring commensal flora or
CC serve as a distress signal. Expression and MAIT cell recognition seem
CC to be ligand-dependent (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimerizes with B2M, this interaction is required for
CC surface expression. Associated with the peptide-loading complex, TAPBP,
CC CALR and PDIA3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}; Extracellular side {ECO:0000250}. Endoplasmic
CC reticulum {ECO:0000250}.
CC -!- DOMAIN: The alpha-3 region and to a lesser extent the transmembrane and
CC cytosolic domains regulate surface expression. The alpha-3 region
CC mediates interaction with B2M (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The ligand-binding groove is ideally suited to present small
CC organic compounds that can originate from vitamins rather than
CC antigenic peptides. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: MR1 is detected in an open versus folded conformation.
CC Only the folded MR1 conformer activates MAIT cells (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR EMBL; CR858109; CAH90348.1; -; mRNA.
DR RefSeq; NP_001125167.1; NM_001131695.1.
DR AlphaFoldDB; Q5RD09; -.
DR SMR; Q5RD09; -.
DR STRING; 9601.ENSPPYP00000000505; -.
DR Ensembl; ENSPPYT00000040292; ENSPPYP00000026393; ENSPPYG00000000445.
DR GeneID; 100172054; -.
DR KEGG; pon:100172054; -.
DR CTD; 3140; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT01040000240396; -.
DR HOGENOM; CLU_047501_0_1_1; -.
DR InParanoid; Q5RD09; -.
DR OrthoDB; 912212at2759; -.
DR TreeFam; TF336617; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR GO; GO:0030881; F:beta-2-microglobulin binding; IEA:Ensembl.
DR GO; GO:0042608; F:T cell receptor binding; IEA:Ensembl.
DR GO; GO:0019884; P:antigen processing and presentation of exogenous antigen; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Immunity; Immunoglobulin domain; Innate immunity; Membrane; MHC I;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..340
FT /note="Major histocompatibility complex class I-related
FT gene protein"
FT /id="PRO_0000344444"
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..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 203..294
FT /note="Ig-like C1-type"
FT REGION 23..109
FT /note="Alpha-1"
FT /evidence="ECO:0000250"
FT REGION 110..201
FT /note="Alpha-2"
FT /evidence="ECO:0000250"
FT REGION 202..293
FT /note="Alpha-3"
FT /evidence="ECO:0000250"
FT REGION 294..302
FT /note="Connecting peptide"
FT /evidence="ECO:0000250"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
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:0000250|UniProtKB:Q95460"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 222..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 340 AA; 39216 MW; 81FB787F03F06E9F CRC64;
MGELTAFLLP LIIVLMVKHS NSRTHSLRYF RLGVSDPIHG VPEFISVGYV DSHPITTYDS
VTQQKEPRAP WMAENLAPDH WERYTQLLRG WQQMFKVELK RLQRHYNHSG SHTYQRMIGC
ELLEDGSTTG FLQYAYDGQD FLIFNKDTLS WLAVDNVAHT IKRAWEANQH ELQYQKNWLE
EECIAWLKRF LEYGKDTLQR TEPPLVRVNR KETFPGVTTL FCKAHGFYPP EIYMTWMKNG
EEIVQEMDYG DILPSGDGTY QTWASVELDP QSSNLYSCHV EHCGVHVVLQ VPQESEAIPL
VMKAVSGSIV FVIVLAGVGV LVWRRRPREQ NGAVYLPTPD
