1A02_PANTR
ID 1A02_PANTR Reviewed; 362 AA.
AC P16210;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Patr class I histocompatibility antigen, A-5 alpha chain;
DE AltName: Full=ChLa class I histocompatibility antigen, A-5 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=1690682; DOI=10.1111/j.1600-065x.1990.tb00040.x;
RA Lawlor D.A., Warren E., Ward F.E., Parham P.;
RT "Comparison of class I MHC alleles in humans and apes.";
RL Immunol. Rev. 113:147-185(1990).
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; M30679; AAA87971.1; -; mRNA.
DR PIR; I36962; I36962.
DR AlphaFoldDB; P16210; -.
DR SMR; P16210; -.
DR STRING; 9598.ENSPTRP00000061016; -.
DR PaxDb; P16210; -.
DR Ensembl; ENSPTRT00000072427; ENSPTRP00000061016; ENSPTRG00000041261.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT00980000198488; -.
DR HOGENOM; CLU_047501_1_1_1; -.
DR InParanoid; P16210; -.
DR OMA; ETERWIT; -.
DR TreeFam; TF336617; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000041261; Expressed in cortex of kidney and 21 other tissues.
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..362
FT /note="Patr class I histocompatibility antigen, A-5 alpha
FT chain"
FT /id="PRO_0000018911"
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 MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18462"
FT MOD_RES 344
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18462"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18462"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18462"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04439"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04439"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04439"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04439"
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; 40487 MW; 9B5A674445037056 CRC64;
MQVTAPRTVL LLLSAALALT ETWAGSHSMK YFYTAVSRPG RGEPRFISVG YVDDTQFVWF
DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNAQTYRE SLRNLRGYYN QSEAGSHIIQ
RMYGCDMGPD GRLLRGYEQY AYDGKDYIAL NQDLSSWTAA DTAAQITQRK WEAARWAEQL
RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT
WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP
SSQSTIPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL
TA
