ID   DRA_MACMU               Reviewed;         254 AA.
AC   Q30631;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Mamu class II histocompatibility antigen, DR alpha chain;
DE   AltName: Full=MHC class II antigen DRA;
DE   Flags: Precursor;
GN   Name=Mamu-DRA;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7558932; DOI=10.1016/0198-8859(94)00155-j;
RA   Lekutis C., Letvin N.L.;
RT   "Biochemical and molecular characterization of rhesus monkey major
RT   histocompatibility complex class II DR.";
RL   Hum. Immunol. 43:72-80(1995).
CC   -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR   EMBL; L27739; AAB63305.1; -; mRNA.
DR   AlphaFoldDB; Q30631; -.
DR   SMR; Q30631; -.
DR   STRING; 9544.ENSMMUP00000025306; -.
DR   eggNOG; ENOG502RXYJ; Eukaryota.
DR   InParanoid; Q30631; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProt.
DR   GO; GO:0042613; C:MHC class II protein complex; IBA:GO_Central.
DR   GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IBA:GO_Central.
DR   GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR   GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.10.320.10; -; 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; IPR011162; MHC_I/II-like_Ag-recog.
DR   InterPro; IPR014745; MHC_II_a/b_N.
DR   InterPro; IPR001003; MHC_II_a_N.
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; 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   Adaptive immunity; Disulfide bond; Glycoprotein; Immunity; Isopeptide bond;
KW   Membrane; MHC II; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..254
FT                   /note="Mamu class II histocompatibility antigen, DR alpha
FT                   chain"
FT                   /id="PRO_0000018948"
FT   TOPO_DOM        26..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..254
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          112..204
FT                   /note="Ig-like C1-type"
FT   REGION          26..109
FT                   /note="Alpha-1"
FT   REGION          110..203
FT                   /note="Alpha-2"
FT   REGION          204..216
FT                   /note="Connecting peptide"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        132..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CROSSLNK        244
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P01903"
SQ   SEQUENCE   254 AA;  28405 MW;  8587C99E22944443 CRC64;
     MAESGVPVLG FFIIAVLMSA QESWAIKEEH VIIQAEFYLN PDQSGEFMFD FDGDEIFHVD
     MAKKETVWRL EEFGRFASFE AQGALANIAV DKANLEIMTK RSNNTPITNV PPEVTVLTNS
     PVELGEPNVL ICFIDKFSPP VVKVTWLKNG KPVTTGVSET VFLPREDHLF RKFHYLPFLP
     STEDIYDCKV EHWCLDAPLL KHWEFDAPSP LPETTENVVC ALGLIVGLVG IIVGTVFIIK
     GVRKSNAAER RGPL