ID   HA1A_BOVIN              Reviewed;         360 AA.
AC   P13752;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=BOLA class I histocompatibility antigen, alpha chain BL3-6;
DE   Flags: Precursor;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3133413;
RA   Ennis P.D., Jackson A.P., Parham P.;
RT   "Molecular cloning of bovine class I MHC cDNA.";
RL   J. Immunol. 141:642-651(1988).
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; M21044; AAA30640.1; -; mRNA.
DR   PIR; A27638; A27638.
DR   AlphaFoldDB; P13752; -.
DR   SMR; P13752; -.
DR   PeptideAtlas; P13752; -.
DR   PRIDE; P13752; -.
DR   Proteomes; UP000009136; 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; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..360
FT                   /note="BOLA class I histocompatibility antigen, alpha chain
FT                   BL3-6"
FT                   /id="PRO_0000018939"
FT   TOPO_DOM        22..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..360
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          206..292
FT                   /note="Ig-like C1-type"
FT   REGION          22..111
FT                   /note="Alpha-1"
FT   REGION          112..203
FT                   /note="Alpha-2"
FT   REGION          204..295
FT                   /note="Alpha-3"
FT   REGION          296..308
FT                   /note="Connecting peptide"
FT   REGION          340..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01900"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01900"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        122..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        224..280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   360 AA;  40363 MW;  2399AF055A0485A9 CRC64;
     MGPRALLLLL SGVLILTETR AGSHSLRYFS TAVSRPGLGE PRYLEVGYVD DTQFVQFDSD
     APNPRMEPRA RWVEQEGPEY WDRNTRNAKG NAQSFRVNLN TLRGYYNQSE AGSHTLQWMS
     GCDVGPDGAL RRGFMQYGYD GRDYLALNED LRSWTAGETE AQITKRKWEA AGYAEVQRNY
     LEGECVEWLR RYLENGKDTL LRADPPKAHV THHPISGREV TLRCWALGFY PEEISLTWQH
     DGEDQTQDME LVETRPSGDG TFQKWAALVV PSGDEQRYTC RVQHEGLQEP LTLRWEPPQP
     SFLTMGIIVG LVLLVVTGAV VAGVVICMKK RSGEKGGNYI QASSSDSAQG SDVSLTVPKV