HLAE_PANTR
ID HLAE_PANTR Reviewed; 350 AA.
AC Q95IT3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Patr class I histocompatibility antigen, alpha chain E;
DE AltName: Full=MHC class I antigen E;
DE Flags: Precursor;
GN Name=Patr-E;
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 [GENOMIC DNA].
RX PubMed=11398964; DOI=10.1007/s002510100318;
RA Adams E.J., Parham P.;
RT "Genomic analysis of common chimpanzee major histocompatibility complex
RT class I genes.";
RL Immunogenetics 53:200-208(2001).
RN [2]
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: Preferably binds to a peptide derived from the signal
CC sequence of most HLA-A, -B, -C and -G molecules. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
CC microglobulin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR EMBL; AF338354; AAK77478.1; -; Genomic_DNA.
DR EMBL; BA000041; BAC78182.1; -; Genomic_DNA.
DR RefSeq; NP_001038963.1; NM_001045498.1.
DR AlphaFoldDB; Q95IT3; -.
DR SMR; Q95IT3; -.
DR STRING; 9598.ENSPTRP00000054601; -.
DR PaxDb; Q95IT3; -.
DR GeneID; 462540; -.
DR KEGG; ptr:462540; -.
DR CTD; 462540; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR HOGENOM; CLU_047501_1_1_1; -.
DR InParanoid; Q95IT3; -.
DR OrthoDB; 912212at2759; -.
DR TreeFam; TF336617; -.
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 3: Inferred from homology;
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..350
FT /note="Patr class I histocompatibility antigen, alpha chain
FT E"
FT /id="PRO_0000018883"
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..350
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:0000255"
FT DISULFID 122..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 224..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 350 AA; 39379 MW; CD3364274632D95E CRC64;
MVDGTLLLLL SEALALTQTW AGSHSLKYFH TSVSRPGRGE PRFISVGYVD DTQFVRFDND
AASPRMVPRA PWMEQEGSEY WDRETRSARD TAQIFRVNLR TLRGYYNQSE AGSHTLQWMH
GCDLGPDGRF LRGYEQFAYD GKDYLTLNED LRSWTAVDTA AQISERKSND ACEAEHQRAY
LEDTCVEWLH KYLEKGKETL LHLEPPKTHV THHPISDHEA TLRCWALGFY PAEITLTWQQ
DGEGHTQDTE LVDTRPAGDG TFQKWAAVVV PSGEEQRYTC HVQHEGLPEP LTLRWKPASQ
PTIPIVGIIA GLVLLGSVVS GAVVAAVMWR KKSSGGKGRS YSKAEWSDSA
