ID   HLAE_PONPY              Reviewed;         359 AA.
AC   P16212;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Popy class I histocompatibility antigen, alpha chain E;
DE   AltName: Full=MHC class I antigen E;
DE   Flags: Precursor; Fragment;
GN   Name=Popy-E;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
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; M30681; AAA88836.1; -; mRNA.
DR   PIR; I61867; I61867.
DR   AlphaFoldDB; P16212; -.
DR   SMR; P16212; -.
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   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          <1..18
FT   CHAIN           19..359
FT                   /note="Popy class I histocompatibility antigen, alpha chain
FT                   E"
FT                   /id="PRO_0000018919"
FT   TOPO_DOM        19..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..359
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          203..291
FT                   /note="Ig-like C1-type"
FT   REGION          19..108
FT                   /note="Alpha-1"
FT   REGION          109..200
FT                   /note="Alpha-2"
FT   REGION          201..292
FT                   /note="Alpha-3"
FT   REGION          293..302
FT                   /note="Connecting peptide"
FT   REGION          330..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         351
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01900"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        119..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        221..277
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   NON_TER         1
SQ   SEQUENCE   359 AA;  40409 MW;  4B2BE601B91D9966 CRC64;
     GTLLLLLSEA LALTETWAGS HSLKYFHTSV SRPGRGEPRF ISVGYVDDTQ FVRFDNDAAS
     PRMVPRAQWM EQEGPEYWDR ETRSARDTAQ TFRVNLRTLR GYYNQTEAGS HTLQWMHGCD
     LGPDGRFLRG YEQFAYDGKD YLTLNEDLRS WTAVDTAAQI SERKSNDACE AEHQRAYLED
     TCVEWLRKYL EKGKETLLHL DPPKTHVTHH RISDHEATLR CWALGFYPAE ITLTWQRDGE
     DQNQYTELVE TRPAGDGTFQ KWAAVVVPSG EEQRYTCHVQ HEGLPEPLTL RWEPASQTTI
     PIVGIFAGLV LLGAVVTGAT VVAAVMWRKK SSGGKGGSYS KAEWSDSAQG SESLTACKA