ID   1C28_PANTR              Reviewed;         346 AA.
AC   P16215;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Patr class I histocompatibility antigen, CH28 alpha chain;
DE   AltName: Full=ChLa class I histocompatibility antigen, CH28 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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3412487; DOI=10.1038/335268a0;
RA   Lawlor D.A., Ward F.E., Ennis P.D., Jackson A.P., Parham P.;
RT   "HLA-A and B polymorphisms predate the divergence of humans and
RT   chimpanzees.";
RL   Nature 335:268-271(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}.
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; M30685; AAA87973.1; -; mRNA.
DR   PIR; S07114; S07114.
DR   RefSeq; NP_001122670.1; NM_001129198.1.
DR   AlphaFoldDB; P16215; -.
DR   SMR; P16215; -.
DR   GeneID; 100169977; -.
DR   KEGG; ptr:100169977; -.
DR   CTD; 100169977; -.
DR   eggNOG; ENOG502RQEK; Eukaryota.
DR   OrthoDB; 1390181at2759; -.
DR   Proteomes; UP000002277; Unplaced.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
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   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   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00129; MHC_I; 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;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..346
FT                   /note="Patr class I histocompatibility antigen, CH28 alpha
FT                   chain"
FT                   /id="PRO_0000018915"
FT   TOPO_DOM        22..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          206..294
FT                   /note="Ig-like C1-type"
FT   REGION          22..111
FT                   /note="Alpha-1"
FT   REGION          112..203
FT                   /note="Alpha-2"
FT   REGION          204..295
FT                   /note="Alpha-3"
FT   REGION          296..305
FT                   /note="Connecting peptide"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        122..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        224..280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   346 AA;  39085 MW;  F83E882D5C2E0971 CRC64;
     MAPRSLLLLF SGALALTETW AGSHSLRYFS TAVSRPGRGE PRYIAVEYVD DTQFLRFDSD
     AAIPRMEPRE PWVEQEGPQY WERTTGYAKA NAQTDRVALR NLLRRYNQSE AGSHTLQGMN
     GCDMGPDGRL LRGYHQHAYD GKDYISLNED LRSWTAADTV AQITQRFYEA EEYAEEFRTY
     LEGECLELLR RYLENGKETL QRADPPKAHI AHHPISDHEA TLRCWALGFY PAEITLTWQR
     DGEEQTQDTE LVETRPAGDG NFQKWAAVVV PSGEEQRYTC HVQHEGLPQP LTLRWEQSPQ
     PTIPIVGIVA GLVVLGAVVT GAVVAAVMWR KKSSDRNRGS YSQAAV