ID   HA11_RAT                Reviewed;         319 AA.
AC   P15978;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Class I histocompatibility antigen, Non-RT1.A alpha-1 chain;
DE   Flags: Precursor;
GN   Name=RT1-Aw2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2315309; DOI=10.1073/pnas.87.6.2167;
RA   Rada C., Lorenzi R., Powis S.J., van den Bogaerde J., Parham P.,
RA   Howard J.C.;
RT   "Concerted evolution of class I genes in the major histocompatibility
RT   complex of murine rodents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:2167-2171(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-49.
RX   PubMed=3585249; DOI=10.1084/jem.165.6.1595;
RA   Spencer S.C., Fabre J.W.;
RT   "Identification in rat liver and serum of water-soluble class I MHC
RT   molecules possibly homologous to the murine Q10 gene product.";
RL   J. Exp. Med. 165:1595-1608(1987).
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; M31038; AAA41608.1; -; mRNA.
DR   PIR; B35090; B35090.
DR   RefSeq; NP_036777.1; NM_012645.1.
DR   AlphaFoldDB; P15978; -.
DR   SMR; P15978; -.
DR   GlyGen; P15978; 2 sites.
DR   jPOST; P15978; -.
DR   PRIDE; P15978; -.
DR   GeneID; 24737; -.
DR   CTD; 24737; -.
DR   RGD; 3512; RT1-Aw2.
DR   InParanoid; P15978; -.
DR   PhylomeDB; P15978; -.
DR   PRO; PR:P15978; -.
DR   Proteomes; UP000002494; Unplaced.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR   GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
DR   GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
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   Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW   Membrane; MHC I; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..319
FT                   /note="Class I histocompatibility antigen, Non-RT1.A alpha-
FT                   1 chain"
FT                   /id="PRO_0000018943"
FT   TOPO_DOM        25..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          209..295
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..307
FT                   /note="Connecting peptide"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        227..283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   319 AA;  36570 MW;  E87C15B2409E1FC0 CRC64;
     MGAMAPRTLL LLLAAVLAPT QTWAGSHSLR YFHTAVSRPG LGEPRFISVG YVDDTQFVRY
     DSDAENPRYE PRARWMEREG PEYWEEQTLV AKGQELDYRV SLRNLLSYYN QSEGGSHTIQ
     RMYGCDVGSD GSLLRGYEQH AYDGRDYIAL NEDLKTWAVA DFAAWITRSK WQRNGAAERS
     RAYLEGTCVE WLLRYLERGK ETLLRSDPPE AHVTLHPRPE GDVTLRCWAL GFYPADITLT
     WQLNGEDLTQ DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCRVEHEGL PEPLSQRWEP
     SPSTDSNLLL LFLELWQFL