1B02_PANTR
ID 1B02_PANTR Reviewed; 362 AA.
AC P13751; Q9MXK0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Patr class I histocompatibility antigen, B-2 alpha chain;
DE AltName: Full=ChLa class I histocompatibility antigen, B-2 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=2460344; DOI=10.1002/j.1460-2075.1988.tb03131.x;
RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., Klein J.;
RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for
RT trans-species mode of evolution.";
RL EMBO J. 7:2765-2774(1988).
RN [2]
RP SEQUENCE REVISION.
RA Mayer W.;
RL Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=10866106; DOI=10.1007/s002510050638;
RA de Groot N.G., Otting N., Arguello R., Watkins D.I., Doxiadis G.G.,
RA Madrigal J.A., Bontrop R.E.;
RT "Major histocompatibility complex class I diversity in a West African
RT chimpanzee population: implications for HIV research.";
RL Immunogenetics 51:398-409(2000).
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; X13116; CAA31508.1; -; mRNA.
DR EMBL; AF168411; AAF72792.2; -; mRNA.
DR PIR; S03538; S03538.
DR RefSeq; NP_001009081.1; NM_001009081.1.
DR AlphaFoldDB; P13751; -.
DR SMR; P13751; -.
DR GeneID; 450202; -.
DR KEGG; ptr:450202; -.
DR CTD; 450202; -.
DR OrthoDB; 1390181at2759; -.
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;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..362
FT /note="Patr class I histocompatibility antigen, B-2 alpha
FT chain"
FT /id="PRO_0000018917"
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 336..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; 40488 MW; FFDB2991044DAA83 CRC64;
MQVTAPRTVL LLLSAALALT ETWAGSHSMK YFYTAVSRPG RGEPRFISVG YVDDTQFVWF
DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNAQTYRE SLRNLRGYYN QSEAGSHIIQ
RMYGCDMGPD GRLLRGYEQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARWAEQL
RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT
WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP
SSQSTIPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL
TA
