ID   1B01_PANTR              Reviewed;         359 AA.
AC   P13750;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Patr class I histocompatibility antigen, B-1 alpha chain;
DE   AltName: Full=ChLa class I histocompatibility antigen, B-1 alpha chain;
DE   Flags: Precursor; Fragment;
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.
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; X13115; CAA31507.1; -; mRNA.
DR   AlphaFoldDB; P13750; -.
DR   SMR; P13750; -.
DR   PRIDE; P13750; -.
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..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..359
FT                   /note="Patr class I histocompatibility antigen, B-1 alpha
FT                   chain"
FT                   /id="PRO_0000018916"
FT   TOPO_DOM        21..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..359
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          205..291
FT                   /note="Ig-like C1-type"
FT   REGION          21..110
FT                   /note="Alpha-1"
FT   REGION          111..202
FT                   /note="Alpha-2"
FT   REGION          203..294
FT                   /note="Alpha-3"
FT   REGION          295..305
FT                   /note="Connecting peptide"
FT   REGION          332..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01900"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01900"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        223..279
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   NON_TER         1
SQ   SEQUENCE   359 AA;  40174 MW;  858ACBAF74D6829D CRC64;
     APRTVLLLLS AALALTETWA GSHSMRYFYT SVSRPGRGEP RFITVGYVDD TQFVRFDSDA
     ASPRMEPRAP WIEQEGPEYW DRETRNMKAS AQTDRENLRI ALRYYNQSEA GSHTWQTMYG
     CDMGPDGRLL RGYGQYAYDG KDYIALNEDL SSWTAADTAA QITQRKWEAA REAEQRRAYL
     EGTCVEWLRR YLENGKETLQ RADPPKTHVT HHPISDHEAT LRCWALGFYP AEITLTWQRD
     GEDQTQDTEL VETRPEGDRT FQKWAAVVVP SGEEQRYTCH VQHEGLPKPL TLRWEPSSQS
     TIPIVGIVAG LAVLVVTVAV VAVVAAVMCR RKSSGGKGGS YSQAASSDSA QGSDVSLTA