1A04_PANTR
ID 1A04_PANTR Reviewed; 365 AA.
AC P13749; Q7JJU4;
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, A-126 alpha chain;
DE AltName: Full=ChLa class I histocompatibility antigen, A-126 alpha chain;
DE AltName: Full=MHC class I antigen Patr-A*0401;
DE Flags: Precursor;
GN Name=Patr-A;
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 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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X13114; CAA31506.1; -; mRNA.
DR EMBL; AF168401; AAF72782.1; -; mRNA.
DR EMBL; BA000041; BAC78189.1; -; Genomic_DNA.
DR PIR; S01171; S01171.
DR AlphaFoldDB; P13749; -.
DR SMR; P13749; -.
DR PaxDb; P13749; -.
DR PRIDE; P13749; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:UniProt.
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: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: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..365
FT /note="Patr class I histocompatibility antigen, A-126 alpha
FT chain"
FT /id="PRO_0000018913"
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..365
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 338..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10314"
FT MOD_RES 344
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10314"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10314"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10314"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10314"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10314"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10314"
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 365 AA; 40656 MW; D3C9A810B22A768F CRC64;
MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF
DSDAASQRME PRAPWIEQEG PEYWDEETRS VKASAQTDRV DLGTLRGYYN QSEDGSHTIQ
LMFGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAAHAAEQL
RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD REATLRCWAL GFYPAEITLT
WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP
SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL
TACKV
