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1A03_PANTR
ID   1A03_PANTR              Reviewed;         365 AA.
AC   P13748; Q547D5;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Patr class I histocompatibility antigen, A-108 alpha chain;
DE   AltName: Full=ChLa class I histocompatibility antigen, A-108 alpha chain;
DE   AltName: Full=MHC class I antigen Patr-A*0301;
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=12021342; DOI=10.1128/jvi.76.12.6093-6103.2002;
RA   Mizukoshi E., Nascimbeni M., Blaustein J.B., Mihalik K., Rice C.M.,
RA   Liang T.J., Feinstone S.M., Rehermann B.;
RT   "Molecular and immunological significance of chimpanzee major
RT   histocompatibility complex haplotypes for hepatitis C virus immune response
RT   and vaccination studies.";
RL   J. Virol. 76:6093-6103(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-365.
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).
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; AF500288; AAM49754.1; -; mRNA.
DR   EMBL; X13113; CAA31505.1; -; mRNA.
DR   PIR; S03535; S03535.
DR   RefSeq; NP_001009058.3; NM_001009058.3.
DR   AlphaFoldDB; P13748; -.
DR   SMR; P13748; -.
DR   PaxDb; P13748; -.
DR   GeneID; 750725; -.
DR   CTD; 750725; -.
DR   InParanoid; P13748; -.
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; 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-108 alpha
FT                   chain"
FT                   /id="PRO_0000018912"
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          339..360
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:P18462"
FT   MOD_RES         344
FT                   /note="Phosphotyrosine"
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   365 AA;  40823 MW;  48CC757055221FC3 CRC64;
     MAVMPPRTLL LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF
     DSDAASQRME PRAPWIEQEG PEYWDQETRN MKASAQTDRV DLGTLRGYYN QSEDGSHTIQ
     IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA AMAAQITKRK WEAAHAAEQL
     RAYLEGRCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAVITLT
     WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP
     SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL
     TACKV
 
 
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