ID A0A060VCZ1_HUMAN Unreviewed; 339 AA. AC A0A060VCZ1; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 19-JAN-2022, entry version 34. DE SubName: Full=MHC class I antigen {ECO:0000313|EMBL:CDQ51666.1}; DE Flags: Fragment; GN Name=HLA-A {ECO:0000313|EMBL:CDQ51666.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CDQ51666.1}; RN [1] {ECO:0000313|EMBL:CDQ51666.1} RP NUCLEOTIDE SEQUENCE. RA Albrecht V., Boehme I., Schmidt A.H.; RT "Characterisation and Confirmation of new HLA-Alleles found by DKMS Life RT Science Lab."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class I family. CC {ECO:0000256|RuleBase:RU004439}. 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; LK021985; CDQ51666.1; -; Genomic_DNA. DR ChiTaRS; HLA-A; human. 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:0030670; C:phagocytic vesicle membrane; IEA:UniProt. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProt. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; IEA:UniProt. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IEA:UniProt. DR GO; GO:0045321; P:leukocyte activation; IEA:UniProt. 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 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 283..307 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 184..270 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT REGION 314..339 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 316..339 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CDQ51666.1" FT NON_TER 339 FT /evidence="ECO:0000313|EMBL:CDQ51666.1" SQ SEQUENCE 339 AA; 38166 MW; AB02D42AE276F555 CRC64; SHSMRYFFTS VSRPGRGEPR FIAVGYVDDT QFVRFDSDAA SQKMEPRAPW IEQEGPEYWD QETRNMKAHS QTDRANLGTL RGYYNQSEDG SHTIQIMYGC DVGPDGRFLR GYRQDAYDGK DYIALNEDLR SWTAADMAAQ ITKRKWEAVH AAEQRRVYLE GRCVDGLRRY LENGKETLQR TDPPKTHMTH HPISDHEATL RCWALGFYPA EITLTWQRDG EDQTQDTELV ETRPAGDGTF QKWAAVVVPS GEEQRYTCHV QHEGLPKPLT LRWELSSQPT IPIVGIIAGL VLLGAVITGA VVAAVMWRRK SSDRKGGSYT QAASSDSAQG SDVSLTACK //