ID 1C02_GORGO Reviewed; 366 AA.
AC P30385;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 28-JUN-2023, entry version 107.
DE RecName: Full=Class I histocompatibility antigen, Gogo-C*0201 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; X60251; CAA42803.1; -; mRNA.
DR PIR; JH0545; JH0545.
DR AlphaFoldDB; P30385; -.
DR SMR; P30385; -.
DR InParanoid; P30385; -.
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: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:0055038; C:recycling endosome 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 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; 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:SF252; HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, C ALPHA CHAIN; 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.
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..366
FT /note="Class I histocompatibility antigen, Gogo-C*0201
FT alpha chain"
FT /id="PRO_0000018906"
FT TOPO_DOM 25..308
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..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 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 366 AA; 40954 MW; 05E159364C769FC5 CRC64;
MRVMAPRTLI LPLSGALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF
DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEDGSHTLQ
SMYGCDLGPD GRLLRGYSQF AYDGKDYIAL NEDLRSWTAA DTAAQVTQRK WEAARVAEQE
RAYLEGLCVE WLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT
WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL PEPLTLRWEP
SSQPTIPIVG IVVGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES
LITCKA
//
