ID   HA1A_RABIT              Reviewed;         361 AA.
AC   P01894;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=RLA class I histocompatibility antigen, alpha chain 11/11;
DE   Flags: Precursor;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6432910;
RA   Tykocinski M.L., Marche P.N., Max E.E., Kindt T.J.;
RT   "Rabbit class I MHC genes: cDNA clones define full-length transcripts of an
RT   expressed gene and a putative pseudogene.";
RL   J. Immunol. 133:2261-2269(1984).
CC   -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC       immune system.
CC   -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
CC       microglobulin).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR   EMBL; K02441; AAA98729.1; -; mRNA.
DR   PIR; A02193; HLRB.
DR   RefSeq; NP_001164741.1; NM_001171270.1.
DR   AlphaFoldDB; P01894; -.
DR   SMR; P01894; -.
DR   GeneID; 100328967; -.
DR   KEGG; ocu:100328967; -.
DR   OrthoDB; 1390181at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; IEA:UniProt.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProt.
DR   GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
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   InterPro; IPR010579; MHC_I_a_C.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00129; MHC_I; 1.
DR   Pfam; PF06623; MHC_I_C; 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   Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..361
FT                   /note="RLA class I histocompatibility antigen, alpha chain
FT                   11/11"
FT                   /id="PRO_0000018941"
FT   TOPO_DOM        25..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          209..297
FT                   /note="Ig-like C1-type"
FT   REGION          25..114
FT                   /note="Alpha-1"
FT   REGION          115..206
FT                   /note="Alpha-2"
FT   REGION          207..298
FT                   /note="Alpha-3"
FT   REGION          299..308
FT                   /note="Connecting peptide"
FT   REGION          335..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01900"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01900"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        125..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        227..283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   361 AA;  40447 MW;  580B673323C1AE35 CRC64;
     MGSMAPRTLL LLLAGALTLK DTQAGSHSMR YFYTSVSRPG LGEPRFIIVG YVDDTQFVRF
     DSDAASPRME QRAPWMGQVE PEYWDQQTQI AKDTAQTFRV NLNTALRYYN QSAAGSHTFQ
     TMFGCEVWAD GRFFHGYRQY AYDGADYIAL NEDLRSWTAA DTAAQNTQRK WEAAGEAERH
     RAYLERECVE WLRRYLEMGK ETLQRADPPK AHVTHHPASD REATLRCWAL GFYPAEISLT
     WQRDGEDQTQ DTELVETRPG GDGTFQKWAA VVVPSGEEQR YTCRVQHEGL PEPLTLTWEP
     PAQPTALIVG IVAGVLGVLL ILGAVVAVVR RKKHSSDGKG GRYTPAAGGH RDQGSDDSLM
     P