ID Q6ICR9_HUMAN Unreviewed; 261 AA.
AC Q6ICR9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 151.
DE SubName: Full=HLA-DMA protein {ECO:0000313|EMBL:CAG29320.1};
DE Flags: Fragment;
GN Name=HLA-DMA {ECO:0000313|EMBL:CAG29320.1};
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 {ECO:0000313|EMBL:CAG29320.1};
RN [1] {ECO:0000313|EMBL:CAG29320.1}
RP NUCLEOTIDE SEQUENCE.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:4I0P}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 39-226, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-41.
RX PubMed=23222639; DOI=10.1038/nsmb.2460;
RA Guce A.I., Mortimer S.E., Yoon T., Painter C.A., Jiang W., Mellins E.D.,
RA Stern L.J.;
RT "HLA-DO acts as a substrate mimic to inhibit HLA-DM by a competitive
RT mechanism.";
RL Nat. Struct. Mol. Biol. 20:90-98(2013).
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004530}. Lysosome membrane
CC {ECO:0000256|ARBA:ARBA00004352}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004352}.
CC -!- SIMILARITY: Belongs to the MHC class II family.
CC {ECO:0000256|RuleBase:RU004238}.
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DR EMBL; CR450324; CAG29320.1; -; mRNA.
DR RefSeq; NP_006111.2; NM_006120.3.
DR PDB; 4I0P; X-ray; 3.20 A; A/E=39-226.
DR PDBsum; 4I0P; -.
DR AlphaFoldDB; Q6ICR9; -.
DR SMR; Q6ICR9; -.
DR DIP; DIP-60118N; -.
DR GlyCosmos; Q6ICR9; 1 site, No reported glycans.
DR Antibodypedia; 2402; 395 antibodies from 33 providers.
DR DNASU; 3108; -.
DR GeneID; 3108; -.
DR KEGG; hsa:3108; -.
DR UCSC; uc003ocm.3; human.
DR CTD; 3108; -.
DR PharmGKB; PA35058; -.
DR VEuPathDB; HostDB:ENSG00000204257; -.
DR HOGENOM; CLU_069380_1_0_1; -.
DR OMA; ADWAHQH; -.
DR OrthoDB; 5256716at2759; -.
DR BioGRID-ORCS; 3108; 20 hits in 1148 CRISPR screens.
DR ChiTaRS; HLA-DMA; human.
DR GenomeRNAi; 3108; -.
DR ExpressionAtlas; Q6ICR9; baseline and differential.
DR Genevisible; Q6ICR9; HS.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW.
DR CDD; cd21009; IgC1_MHC_II_alpha_HLA-DM; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR014745; MHC_II_a/b_N.
DR InterPro; IPR001003; MHC_II_a_N.
DR PANTHER; PTHR19944:SF50; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM ALPHA CHAIN; 1.
DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00993; MHC_II_alpha; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00920; MHC_II_alpha; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4I0P};
KW Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW MHC II {ECO:0000256|ARBA:ARBA00023182};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..261
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004274595"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..215
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT CARBOHYD 41
FT /note="N-acetyl-D-glucosamine"
FT /evidence="ECO:0007829|PDB:4I0P"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007829|PDB:4I0P"
FT DISULFID 50..105
FT /evidence="ECO:0007829|PDB:4I0P"
FT DISULFID 147..202
FT /evidence="ECO:0007829|PDB:4I0P"
FT NON_TER 261
FT /evidence="ECO:0000313|EMBL:CAG29320.1"
SQ SEQUENCE 261 AA; 29207 MW; BAAB2528874DFFC6 CRC64;
MGHEQNQGAA LLQMLPLLWL LPHSWAVPEA PTPMWPDDLQ NHTFLHTVYC QDGSPSVGLS
EAYDEDQLFF FDFSQNTRVP RLPEFADWAQ EQGDAPAILF DKEFCEWMIQ QIGPKLDGKI
PVSRGFPIAE VFTLKPLEFG KPNTLVCFVS NLFPPMLTVN WQHHSVPVEG FGPTFVSAVD
GLSFQAFSYL NFTPEPSDIF SCIVTHEIDR YTAIAYWVPR NALPSDLLEN VLCGVAFGLG
VLGIIVGIVL IIYFRKPCSG D
//
