ID   1C01_PANTR              Reviewed;         366 AA.
AC   P30686;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Patr class I histocompatibility antigen, C alpha chain;
DE   AltName: Full=ChLa class I histocompatibility antigen, C alpha chain;
DE   Flags: Precursor;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1381540; DOI=10.1016/0042-6822(92)90925-f;
RA   Kato T., Esumi M., Yamashita S., Abe K., Shikata T.;
RT   "Interferon-inducible gene expression in chimpanzee liver infected with
RT   hepatitis C virus.";
RL   Virology 190:856-860(1992).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA01979.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D11383; BAA01979.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; P30686; -.
DR   SMR; P30686; -.
DR   eggNOG; ENOG502RQEK; Eukaryota.
DR   Proteomes; UP000002277; 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; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..366
FT                   /note="Patr class I histocompatibility antigen, C alpha
FT                   chain"
FT                   /id="PRO_0000018914"
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..366
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          209..297
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   MOD_RES         357
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01900"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01900"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        125..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        227..283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   366 AA;  40843 MW;  58B25703B3D82C4D CRC64;
     MRVTAPRTLL LLLSGGLALT ETWAGSHSLR YFDTAVSRPG RREPRFISVG YVDDTQFVRF
     DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV SLRNLRGYYN QSEDGSHTLQ
     WMYGCDLGPD GRLLRGYGQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQL
     RAYLEGKRVE SCRRYLENGK ETLQRTECPK THMTHHPVSD HEATLRCWAL AFYPAEITLT
     WQRDGEDQIQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PEPLTLRWKP
     TSQPTIPIVG IVAGLAVLAV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES
     LIACKA