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 27-MAR-2024, entry version 128.
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; 9615.ENSCAFP00000000716; -.
DR PaxDb; 9612-ENSCAFP00000000718; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR InParanoid; P18466; -.
DR Proteomes; UP000002254; Unplaced.
DR Proteomes; UP000694429; Unplaced.
DR Proteomes; UP000694542; Unplaced.
DR Proteomes; UP000805418; 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:0098553; C: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:0042605; F:peptide antigen binding; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IBA:GO_Central.
DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central.
DR CDD; cd07698; IgC1_MHC_I_alpha3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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 PANTHER; PTHR16675:SF242; CLASS IB MHC ANTIGEN QA-2-RELATED; 1.
DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1.
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; Immunoglobulin; 1.
DR SUPFAM; SSF54452; MHC antigen-recognition domain; 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
//
