ID   1B02_GORGO              Reviewed;         362 AA.
AC   P30380;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Class I histocompatibility antigen, Gogo-B*0102 alpha chain;
DE   Flags: Precursor;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1744581; DOI=10.1084/jem.174.6.1491;
RA   Lawlor D.A., Warren E., Taylor P., Parham P.;
RT   "Gorilla class I major histocompatibility complex alleles: comparison to
RT   human and chimpanzee class I.";
RL   J. Exp. Med. 174:1491-1509(1991).
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; X60693; CAA43101.1; -; mRNA.
DR   PIR; JH0540; JH0540.
DR   AlphaFoldDB; P30380; -.
DR   SMR; P30380; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProt.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProt.
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:0055038; C:recycling endosome 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:0000250"
FT   CHAIN           25..362
FT                   /note="Class I histocompatibility antigen, Gogo-B*0102
FT                   alpha chain"
FT                   /id="PRO_0000018902"
FT   TOPO_DOM        25..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..362
FT                   /note="Cytoplasmic"
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..308
FT                   /note="Connecting peptide"
FT   REGION          335..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        125..188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        227..283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   362 AA;  40205 MW;  E19EEE2B7CC7BECD CRC64;
     MRVTAPRTLL LLLSAALALT ETWAGSHSMR YFDTAVSRPG RGEPRFITVG YVDDTQFVRF
     DSDAASPRME PRAPWIEQEG PEYWDRETQT SKAQAQTDRE NLRIALRYYN QSEAGSHTFQ
     RMFGCDVGPD GRLLRGYSQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL
     RAYLEGTCVE WLRRYLENGR ETLQRADTPK THVTHHPISD HEATLRCWAL GFYPAEITLT
     WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEER YTCHVQHEGL PKPLTLRWEP
     SSQSTIPIVG IVAGLAVLAV VVIGAVVTAV ICRRKSSGGK GGSYSQAASS DSAQGSDVSL
     TA