ID   HA1B_BOVIN              Reviewed;         364 AA.
AC   P13753;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=BOLA class I histocompatibility antigen, alpha chain BL3-7;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M21043; AAA30641.1; -; mRNA.
DR   PIR; B27638; B27638.
DR   AlphaFoldDB; P13753; -.
DR   SMR; P13753; -.
DR   STRING; 9913.ENSBTAP00000031126; -.
DR   PeptideAtlas; P13753; -.
DR   PRIDE; P13753; -.
DR   eggNOG; ENOG502RQEK; Eukaryota.
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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..364
FT                   /note="BOLA class I histocompatibility antigen, alpha chain
FT                   BL3-7"
FT                   /id="PRO_0000018940"
FT   TOPO_DOM        28..310
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        332..364
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          212..298
FT                   /note="Ig-like C1-type"
FT   REGION          28..117
FT                   /note="Alpha-1"
FT   REGION          118..209
FT                   /note="Alpha-2"
FT   REGION          210..301
FT                   /note="Alpha-3"
FT   REGION          302..310
FT                   /note="Connecting peptide"
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:P01901"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        230..286
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   364 AA;  41513 MW;  622056CF7DCF7873 CRC64;
     MRVMRVMRPR TLLLLLSGVL VLTETLAGSH SLRYFYTGVS RPGLGEPRFI AVGYVDDTQF
     VRFDSDAPNP REEPRVPWME QEGPEYWDRN TRIYKDTAQI FRVDLNTLRG YYNQSETGSH
     NIQAMYGCDV GPDGRLLRGF WQFGYDGRDY IALNEELRSW TAADTAAQIT KRKWEAAGAA
     ETWRNYLEGE CVEWLRRYLE NGKDTLLRAD PPKAHVTHHS ISDREVTLRC WALGFYPEEI
     SLTWQREGED QTQDMELVET RPSGDGTFQK WAALVVPSGE EQRYTCRVQH EGLQEPLTLR
     WEPPQTSFLI MGIIVGLVLL VVALVAGAVI WRKKRSGEKG RIYTQAASSD SAQGSDVSLT
     VPKV