ID I3ZN84_HUMAN Unreviewed; 362 AA. AC I3ZN84; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 24-JUL-2024, entry version 74. DE SubName: Full=HLA-B alpha chain (B*5703GB) {ECO:0000313|EMBL:CAA70355.1}; DE SubName: Full=MHC class I antigen {ECO:0000313|EMBL:AFL91488.1}; GN Name=HLA-B {ECO:0000313|EMBL:AFL91488.1}; GN Synonyms=HLA-B*5703GB {ECO:0000313|EMBL:CAA70355.1}; 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:AFL91488.1}; RN [1] {ECO:0000313|EMBL:CAA70355.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=9234488; DOI=10.1111/j.1399-0039.1997.tb02814.x; RA Vilches C., Bunce M., de Pablo R., Moreno M.E., Puente S., Sanz L., RA Kreisler M.; RT "The novel HLA-Cw*1802 allele is associated with B*5703 in the Bubi RT population from Equatorial Guinea."; RL Tissue Antigens 49:644-648(1997). RN [2] {ECO:0000313|EMBL:AFL91488.1} RP NUCLEOTIDE SEQUENCE. RA Lind C., Ferriola D., Mackiewicz K., Sasson A., Monos D.; RT "Full genomic sequencing of 15 common and well-documented HLA class I RT alleles using next generation sequencing technology."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ALZ40818.1} RP NUCLEOTIDE SEQUENCE. RA Bravo-Egana V., Clark P., Monos D.; RT "Generation of high confidence HLA genotyping and consensus sequences for RT Class I HLA loci using the NGS-based Omixon Holotype HLA typing system and RT the Illumina MiSeq platform."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ANG08746.1} RP NUCLEOTIDE SEQUENCE. RA Barsakis K., Babrzadeh F., Chi A., Mindrinos M.N., Fernandez Vina M.A.; RT "HLA variation in coding and non-coding gene segments."; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:ASA39912.1} RP NUCLEOTIDE SEQUENCE. RA Varghese N.; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:SBW38437.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28547825; DOI=10.1111/tan.13057; RA Albrecht V., Zweiniger C., Surendranath V., Lang K., Schofl G., Dahl A., RA Winkler S., Lange V., Bohme I., Schmidt A.H.; RT "Dual redundant sequencing strategy: Full-length gene characterisation of RT 1056 novel and confirmatory HLA alleles."; RL HLA 90:79-87(2017). RN [7] {ECO:0007829|PDB:5VVP} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 25-300, AND DISULFIDE BONDS. RX PubMed=30410026; DOI=10.1038/s41467-018-07109-w; RA Illing P.T., Pymm P., Croft N.P., Hilton H.G., Jojic V., Han A.S., RA Mendoza J.L., Mifsud N.A., Dudek N.L., McCluskey J., Parham P., RA Rossjohn J., Vivian J.P., Purcell A.W.; RT "HLA-B57 micropolymorphism defines the sequence and conformational breadth RT of the immunopeptidome."; RL Nat. Commun. 9:4693-4693(2018). RN [8] {ECO:0000313|EMBL:SPS03132.1} RP NUCLEOTIDE SEQUENCE. RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M., RA Wayne K.J., Tettelin H., Glass J.I., Rusch D., Podicherti R., Tsui H.-C.T., RA Winkler M.E.; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:QDK62508.1} RP NUCLEOTIDE SEQUENCE. RA Cereb N., Yang S.Y.; RT "HLA new alleles found by Histogenetics."; RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0007829|PDB:6V2P, ECO:0007829|PDB:6V2Q} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 25-300, AND DISULFIDE BONDS. RX PubMed=32404419; DOI=10.1073/pnas.1920570117; RA Saunders P.M., MacLachlan B.J., Pymm P., Illing P.T., Deng Y., Wong S.C., RA Oates C.V.L., Purcell A.W., Rossjohn J., Vivian J.P., Brooks A.G.; RT "The molecular basis of how buried human leukocyte antigen polymorphism RT modulates natural killer cell function."; RL Proc. Natl. Acad. Sci. U.S.A. 117:11636-11647(2020). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. {ECO:0000256|ARBA:ARBA00002297}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the MHC class I family. CC {ECO:0000256|ARBA:ARBA00006909, 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; JQ771786; AFL91488.1; -; Genomic_DNA. DR EMBL; KU528603; ALZ40818.1; -; Genomic_DNA. DR EMBL; KU319331; ANG08746.1; -; Genomic_DNA. DR EMBL; KU319332; ANG08747.1; -; Genomic_DNA. DR EMBL; KY000094; ASA39912.1; -; Genomic_DNA. DR EMBL; MH173405; AWM62451.1; -; Genomic_DNA. DR EMBL; Y09157; CAA70355.1; -; mRNA. DR EMBL; MK938025; QDK62508.1; -; Genomic_DNA. DR EMBL; MK938045; QDK62528.1; -; Genomic_DNA. DR EMBL; MN016199; QDK62895.1; -; Genomic_DNA. DR EMBL; MN016311; QDK63006.1; -; Genomic_DNA. DR EMBL; MN016449; QDK63144.1; -; Genomic_DNA. DR EMBL; MN053492; QDK63236.1; -; Genomic_DNA. DR EMBL; MN136795; QDK63298.1; -; Genomic_DNA. DR EMBL; MT681781; QMI58748.1; -; Genomic_DNA. DR EMBL; MT681785; QMI58752.1; -; Genomic_DNA. DR EMBL; MT681786; QMI58753.1; -; Genomic_DNA. DR EMBL; LT599216; SBW38437.1; -; Genomic_DNA. DR EMBL; LS423034; SPS03132.1; -; Genomic_DNA. DR PDB; 5VVP; X-ray; 2.00 A; A=25-300. DR PDB; 6V2P; X-ray; 1.30 A; A=25-300. DR PDB; 6V2Q; X-ray; 1.60 A; A=25-300. DR PDB; 6V3J; X-ray; 1.98 A; A=25-299. DR PDBsum; 5VVP; -. DR AlphaFoldDB; I3ZN84; -. DR SMR; I3ZN84; -. DR PeptideAtlas; I3ZN84; -. DR ChiTaRS; HLA-B; human. 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; IEA:TreeGrafter. DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter. DR GO; GO:0098553; C: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:0042605; F:peptide antigen binding; IEA:TreeGrafter. DR GO; GO:0005102; F:signaling receptor binding; IEA:TreeGrafter. DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IEA:TreeGrafter. DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IEA:TreeGrafter. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:TreeGrafter. DR CDD; cd21026; IgC1_MHC_Ia_HLA-B; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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; IPR050208; MHC_class-I_related. 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 PANTHER; PTHR16675:SF242; CLASS IB MHC ANTIGEN QA-2-RELATED; 1. DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. 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; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:5VVP, ECO:0007829|PDB:6V2P}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Immunity {ECO:0000256|ARBA:ARBA00022451}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW MHC I {ECO:0000256|ARBA:ARBA00022451}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 25..362 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014305270" FT TRANSMEM 308..330 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 209..295 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT REGION 337..362 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 339..362 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 125..188 FT /evidence="ECO:0007829|PDB:5VVP, ECO:0007829|PDB:6V2P" FT DISULFID 227..283 FT /evidence="ECO:0007829|PDB:5VVP, ECO:0007829|PDB:6V2P" SQ SEQUENCE 362 AA; 40299 MW; 45C98B4CD2F28B31 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDGETRN MKASAQTYRE NLRIALRYYN QSEAGSHIIQ VMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA //