ID   HA19_CANLF              Reviewed;         362 AA.
AC   P18466;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=DLA class I histocompatibility antigen, A9/A9 alpha chain;
DE   Flags: Precursor;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2370086; DOI=10.1007/bf02115019;
RA   Sarmiento U.M., Storb R.;
RT   "Nucleotide sequence of a dog class I cDNA clone.";
RL   Immunogenetics 31:400-404(1990).
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; M32283; AAA30865.1; -; mRNA.
DR   PIR; A45845; A45845.
DR   AlphaFoldDB; P18466; -.
DR   SMR; P18466; -.
DR   STRING; 9612.ENSCAFP00000000718; -.
DR   PRIDE; P18466; -.
DR   eggNOG; ENOG502RQEK; Eukaryota.
DR   Proteomes; UP000002254; 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: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: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   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;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..362
FT                   /note="DLA class I histocompatibility antigen, A9/A9 alpha
FT                   chain"
FT                   /id="PRO_0000018945"
FT   TOPO_DOM        25..306
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        307..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..362
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          210..296
FT                   /note="Ig-like C1-type"
FT   REGION          25..114
FT                   /note="Alpha-1"
FT   REGION          115..207
FT                   /note="Alpha-2"
FT   REGION          208..299
FT                   /note="Alpha-3"
FT   REGION          300..306
FT                   /note="Connecting peptide"
FT   REGION          333..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        125..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        228..284
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   362 AA;  40462 MW;  AC893ABD4F4941AA CRC64;
     MEVVMPRALL VLLSAALALT PTRAGSHSLR YFYTSVSRPG AGDPRFIAVG YVDDTQFVRF
     DSDAATGRME PRAPWVEQEG PEYWDRQTRT IKETARTFRV DLDTLRGYYN QSEAGSHTRQ
     TMYGCDLGPD GRLLRGYSQD AYDGADYIAL NEDLRSWTAA DTAAQITQRK WEAAGVAELQ
     WRNYLETTCV EWLRRYLEMG KETLLRADPP STRVTHHPVS DHEVTLRCWA LGFYPAEITL
     TWQRDGEDQT QDTEVVDTRP AGDGTFQKWA AVVVPSGQEQ RYTCHVQHEG LPEPITRRWE
     PSPLSTIVIV SIAALVLLVV AGVIGAVIWR KQRSGGKGPG YSHAARDDSA QGSDVSLTAP
     RV