ID 1B07_HUMAN Reviewed; 362 AA. AC P01889; Q29638; Q29681; Q29854; Q29861; Q31613; Q5SRJ2; Q9GIX1; AC Q9TP95; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 3. DT 13-FEB-2019, entry version 194. DE RecName: Full=HLA class I histocompatibility antigen, B-7 alpha chain; DE AltName: Full=MHC class I antigen B*7; DE Flags: Precursor; GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:02). RX PubMed=2320591; DOI=10.1073/pnas.87.7.2833; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:02). RX PubMed=2700944; RA Parham P., Benjamin R.J., Chen B.P., Clayberger C., Ennis P.D., RA Krensky A.M., Lawlor D.A., Littman D.R., Norment A.M., Orr H.T., RA Salter R.D., Zemmour J.; RT "Diversity of class I HLA molecules: functional and evolutionary RT interactions with T cells."; RL Cold Spring Harb. Symp. Quant. Biol. 54:529-543(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:02). RX PubMed=2993161; DOI=10.1007/BF00563508; RA Sood A.K., Pan J., Biro P.A., Pereira D., Srivastava R., Reddy V.B., RA Duceman B.W., Weissman S.M.; RT "Structure and polymorphism of class I MHC antigen mRNA."; RL Immunogenetics 22:101-121(1985). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:02). RA Ellexson M.E., Zhang L., Hildebrand W.H.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:03). RX PubMed=8106270; DOI=10.1016/0198-8859(93)90533-7; RA Bergmans A., Tijssen H., Lardy J., Reekers P.; RT "Complete nucleotide sequence of HLA-B*0703, a B7-variant (BPOT)."; RL Hum. Immunol. 38:159-162(1993). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:04). RX PubMed=7652739; DOI=10.1111/j.1399-0039.1995.tb02461.x; RA Kubens B.S., Arnett K.L., Adams E.J., Parham P., Grosse-Wilde H.; RT "Definition of a new HLA-B7 subtype (B*0704) by isoelectric focusing, RT family studies and DNA sequence analysis."; RL Tissue Antigens 45:322-327(1995). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:05). RX PubMed=7878658; DOI=10.1111/j.1399-0039.1994.tb02402.x; RA Arnett K.L., Adams E.J., Domena J.D., Parham P.; RT "Structure of a novel subtype of B7 (B*0705) isolated from a Chinese RT individual."; RL Tissue Antigens 44:318-321(1994). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*07:03 AND B*07:05). RX PubMed=8537119; RA Smith K.D., Epperson D.F., Lutz C.T.; RT "Alloreactive cytotoxic T-lymphocyte-defined HLA-B7 subtypes differ in RT peptide antigen presentation."; RL Immunogenetics 43:27-37(1996). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:06). RX PubMed=8773323; DOI=10.1111/j.1399-0039.1996.tb02561.x; RA Sanz L., Vilches C., de Pablo R., Bunce M., Moreno M.E., Kreisler M.; RT "Haplotypic association of two new HLA class I alleles: Cw*15052 and RT B*0706: evolutionary relationships of HLA-Cw*15 alleles."; RL Tissue Antigens 47:329-332(1996). RN [10] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:18). RA Bettinotti M.P., Hadzikadic L., Dhillon G., Barracchini K., RA Marincola F.M.; RT "A new HLA-B allele."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:02). RA Marsh S.G.E.; RT "Intron sequences of HLA class I."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:02). RC TISSUE=Blood; RX PubMed=12622774; DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Subthalamic nucleus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*07:24). RC TISSUE=Peripheral blood; RX PubMed=11556973; DOI=10.1034/j.1399-0039.2001.057005471.x; RA Middleton D., Curran M.D., Anholts J.D., Reilly E.R., Schreuder G.M.; RT "Characterisation of a new HLA-B allele, HLA-B*0724."; RL Tissue Antigens 57:471-473(2001). RN [16] RP PROTEIN SEQUENCE OF 25-295 (B*07:02). RX PubMed=518865; DOI=10.1021/bi00592a030; RA Orr H.T., Lopez de Castro J.A., Lancet D., Strominger J.L.; RT "Complete amino acid sequence of a papain-solubilized human RT histocompatibility antigen, HLA-B7. 2. Sequence determination and RT search for homologies."; RL Biochemistry 18:5711-5720(1979). RN [17] RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION). RX PubMed=11390610; DOI=10.1128/JVI.75.13.6086-6094.2001; RA Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L., RA Mulloy J.C., Jacobson S., Franchini G.; RT "Free major histocompatibility complex class I heavy chain is RT preferentially targeted for degradation by human T-cell RT leukemia/lymphotropic virus type 1 p12(I) protein."; RL J. Virol. 75:6086-6094(2001). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [19] RP VARIANT [LARGE SCALE ANALYSIS] THR-65, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP VARIANT [LARGE SCALE ANALYSIS] ASN-138, VARIANT [LARGE SCALE ANALYSIS] RP SER-155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2- CC microglobulin). {ECO:0000250|UniProtKB:P01892}. CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory CC protein p12I. {ECO:0000269|PubMed:11390610}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC {ECO:0000250}. CC -!- POLYMORPHISM: The following alleles of B-7 are known: B*07:02 CC (B7.2), B*07:03 (BPOT), B*07:04, B*07:05, B*07:06 (B7_L79), CC B*07:18 and B*07:24. The sequence shown is B*07:02. 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; M32317; AAA36230.1; -; mRNA. DR EMBL; M16102; AAA59622.1; ALT_SEQ; mRNA. DR EMBL; U29057; AAA91229.1; -; mRNA. DR EMBL; X64454; CAA45785.1; -; mRNA. DR EMBL; U04245; AAA87398.1; -; mRNA. DR EMBL; L33922; AAA65639.1; -; mRNA. DR EMBL; U21052; AAA92563.1; -; mRNA. DR EMBL; U21053; AAA92564.1; -; mRNA. DR EMBL; X91749; CAA62864.1; -; mRNA. DR EMBL; AF189017; AAF01052.1; -; mRNA. DR EMBL; AJ309047; CAC35468.1; -; Genomic_DNA. DR EMBL; AJ292075; CAC33440.1; -; Genomic_DNA. DR EMBL; AL671883; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK313911; BAG36634.1; -; mRNA. DR EMBL; AJ401222; CAC10402.1; -; Genomic_DNA. DR CCDS; CCDS34394.1; -. DR PIR; B35997; HLHUB7. DR PIR; I54418; I54418. DR PIR; I59651; I59651. DR PIR; S60601; S60601. DR RefSeq; NP_005505.2; NM_005514.7. DR UniGene; Hs.654404; -. DR UniGene; Hs.726974; -. DR UniGene; Hs.77961; -. DR PDB; 3VCL; X-ray; 1.70 A; A=25-299. DR PDB; 4U1H; X-ray; 1.59 A; A=25-300. DR PDB; 4U1K; X-ray; 2.09 A; A/D=25-300. DR PDB; 5EO0; X-ray; 1.70 A; A=25-299. DR PDB; 5EO1; X-ray; 1.85 A; A=25-299. DR PDB; 5WMN; X-ray; 1.82 A; A/C=25-300. DR PDB; 5WMO; X-ray; 1.62 A; A=25-300. DR PDB; 5WMP; X-ray; 1.60 A; A=25-300. DR PDB; 6AT5; X-ray; 1.50 A; A=1-362. DR PDB; 6AVF; X-ray; 2.03 A; H=1-362. DR PDB; 6AVG; X-ray; 2.60 A; F/G=1-362. DR PDBsum; 3VCL; -. DR PDBsum; 4U1H; -. DR PDBsum; 4U1K; -. DR PDBsum; 5EO0; -. DR PDBsum; 5EO1; -. DR PDBsum; 5WMN; -. DR PDBsum; 5WMO; -. DR PDBsum; 5WMP; -. DR PDBsum; 6AT5; -. DR PDBsum; 6AVF; -. DR PDBsum; 6AVG; -. DR ProteinModelPortal; P01889; -. DR SMR; P01889; -. DR BioGrid; 109351; 111. DR IntAct; P01889; 18. DR MINT; P01889; -. DR STRING; 9606.ENSP00000399168; -. DR GlyConnect; 1348; -. DR iPTMnet; P01889; -. DR SwissPalm; P01889; -. DR BioMuta; HLA-B; -. DR DMDM; 122162; -. DR EPD; P01889; -. DR jPOST; P01889; -. DR MaxQB; P01889; -. DR PaxDb; P01889; -. DR PeptideAtlas; P01889; -. DR PRIDE; P01889; -. DR Ensembl; ENST00000412585; ENSP00000399168; ENSG00000234745. DR GeneID; 3106; -. DR KEGG; hsa:3106; -. DR CTD; 3106; -. DR DisGeNET; 3106; -. DR EuPathDB; HostDB:ENSG00000234745.9; -. DR GeneCards; HLA-B; -. DR HGNC; HGNC:4932; HLA-B. DR HPA; CAB015418; -. DR MalaCards; HLA-B; -. DR MIM; 142830; gene. DR neXtProt; NX_P01889; -. DR OpenTargets; ENSG00000234745; -. DR PharmGKB; PA35056; -. DR eggNOG; ENOG410II5V; Eukaryota. DR eggNOG; ENOG4111K8F; LUCA. DR GeneTree; ENSGT00940000153872; -. DR HOVERGEN; HBG016709; -. DR KO; K06751; -. DR OMA; VPGYYNQ; -. DR OrthoDB; 1390181at2759; -. DR PhylomeDB; P01889; -. DR Reactome; R-HSA-1236974; ER-Phagosome pathway. DR Reactome; R-HSA-1236977; Endosomal/Vacuolar pathway. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SIGNOR; P01889; -. DR ChiTaRS; HLA-B; human. DR GeneWiki; HLA-B; -. DR GenomeRNAi; 3106; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000234745; Expressed in 92 organ(s), highest expression level in blood. DR ExpressionAtlas; P01889; baseline and differential. DR Genevisible; P01889; HS. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProtKB. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0055038; C:recycling endosome membrane; TAS:Reactome. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; IDA:UniProtKB. DR GO; GO:2001198; P:regulation of dendritic cell differentiation; IMP:BHF-UCL. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0032655; P:regulation of interleukin-12 production; IMP:BHF-UCL. DR GO; GO:0032675; P:regulation of interleukin-6 production; IMP:BHF-UCL. DR GO; GO:0002667; P:regulation of T cell anergy; IMP:BHF-UCL. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; 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 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 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Host-virus interaction; Immunity; KW Membrane; MHC I; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 {ECO:0000269|PubMed:518865}. FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-7 alpha chain. FT /FTId=PRO_0000018833. FT TOPO_DOM 25 309 Extracellular. {ECO:0000255}. FT TRANSMEM 310 333 Helical. {ECO:0000255}. FT TOPO_DOM 334 362 Cytoplasmic. {ECO:0000255}. FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 4 4 M -> T (in dbSNP:rs1050458). FT /FTId=VAR_050332. FT VARIANT 9 9 V -> L (in dbSNP:rs1050462). FT /FTId=VAR_050333. FT VARIANT 17 17 L -> V (in dbSNP:rs1131165). FT /FTId=VAR_050334. FT VARIANT 35 35 S -> A (in dbSNP:rs1131170). FT /FTId=VAR_050335. FT VARIANT 36 36 V -> M (in dbSNP:rs1050486). FT /FTId=VAR_050336. FT VARIANT 48 48 S -> A (in dbSNP:rs713031). FT /FTId=VAR_061386. FT VARIANT 48 48 S -> P (in dbSNP:rs713031). FT /FTId=VAR_061387. FT VARIANT 48 48 S -> T (in dbSNP:rs713031). FT /FTId=VAR_061388. FT VARIANT 65 65 A -> T (in dbSNP:rs1050529). FT {ECO:0000244|PubMed:21269460}. FT /FTId=VAR_050337. FT VARIANT 87 87 N -> D (in dbSNP:rs1050570). FT /FTId=VAR_050338. FT VARIANT 87 87 N -> K (in dbSNP:rs1065386). FT /FTId=VAR_059467. FT VARIANT 93 95 AQA -> TNT (in allele B*07:03). FT /FTId=VAR_016351. FT VARIANT 97 97 T -> A (in dbSNP:rs1050393). FT /FTId=VAR_050339. FT VARIANT 98 98 D -> Y (in dbSNP:rs1131215). FT /FTId=VAR_059468. FT VARIANT 101 101 S -> N (in dbSNP:rs1050388). FT /FTId=VAR_050340. FT VARIANT 118 119 TL -> II (in allele B*07:18; FT dbSNP:rs796332753). FT /FTId=VAR_016352. FT VARIANT 121 121 S -> R (in allele B*07:18; FT dbSNP:rs1140412). FT /FTId=VAR_016353. FT VARIANT 137 137 H -> Y (in dbSNP:rs1050379). FT /FTId=VAR_050341. FT VARIANT 138 138 D -> H (in dbSNP:rs709055). FT /FTId=VAR_061389. FT VARIANT 138 138 D -> N (in allele B*07:05 and allele FT B*07:06; dbSNP:rs709055). FT {ECO:0000244|PubMed:25944712}. FT /FTId=VAR_016354. FT VARIANT 155 155 R -> S (in dbSNP:rs1050654). FT {ECO:0000244|PubMed:25944712}. FT /FTId=VAR_050342. FT VARIANT 180 180 R -> D (in allele B*07:04; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016355. FT VARIANT 187 187 E -> A (in dbSNP:rs2308466). FT /FTId=VAR_059469. FT VARIANT 187 187 E -> G (in dbSNP:rs2308466). FT /FTId=VAR_059470. FT VARIANT 187 187 E -> K (in dbSNP:rs2523600). FT /FTId=VAR_059471. FT VARIANT 187 187 E -> L (in allele B*07:24; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016616. FT VARIANT 187 187 E -> Q (in dbSNP:rs2523600). FT /FTId=VAR_059472. FT VARIANT 187 187 E -> V (in dbSNP:rs2308466). FT /FTId=VAR_059473. FT VARIANT 195 195 Y -> H (in dbSNP:rs1050696). FT /FTId=VAR_050343. FT VARIANT 306 306 V -> I (in allele B*07:05; FT dbSNP:rs1131500). FT /FTId=VAR_016356. FT VARIANT 329 329 A -> T (in dbSNP:rs1051488). FT /FTId=VAR_050344. FT VARIANT 349 349 C -> S (in dbSNP:rs2308655). FT /FTId=VAR_061390. FT VARIANT 349 349 C -> Y (in dbSNP:rs2308655). FT /FTId=VAR_061391. FT CONFLICT 15 18 AALA -> GPW (in Ref. 3; AAA59622). FT {ECO:0000305}. FT CONFLICT 266 266 Q -> E (in Ref. 16; AA sequence). FT {ECO:0000305}. FT CONFLICT 268 268 W -> S (in Ref. 3; AAA59622). FT {ECO:0000305}. FT CONFLICT 297 297 R -> G (in Ref. 3; AAA59622). FT {ECO:0000305}. FT CONFLICT 314 315 GL -> RP (in Ref. 3; AAA59622). FT {ECO:0000305}. FT STRAND 27 36 {ECO:0000244|PDB:6AT5}. FT STRAND 41 43 {ECO:0000244|PDB:5WMN}. FT STRAND 45 52 {ECO:0000244|PDB:6AT5}. FT STRAND 55 61 {ECO:0000244|PDB:6AT5}. FT STRAND 64 66 {ECO:0000244|PDB:6AT5}. FT STRAND 70 73 {ECO:0000244|PDB:4U1K}. FT HELIX 74 76 {ECO:0000244|PDB:6AT5}. FT HELIX 81 108 {ECO:0000244|PDB:6AT5}. FT STRAND 113 115 {ECO:0000244|PDB:6AT5}. FT STRAND 118 127 {ECO:0000244|PDB:6AT5}. FT STRAND 133 142 {ECO:0000244|PDB:6AT5}. FT STRAND 145 150 {ECO:0000244|PDB:6AT5}. FT STRAND 157 161 {ECO:0000244|PDB:6AT5}. FT HELIX 162 173 {ECO:0000244|PDB:6AT5}. FT HELIX 176 185 {ECO:0000244|PDB:6AT5}. FT HELIX 187 198 {ECO:0000244|PDB:6AT5}. FT HELIX 200 203 {ECO:0000244|PDB:6AT5}. FT STRAND 210 219 {ECO:0000244|PDB:6AT5}. FT STRAND 222 235 {ECO:0000244|PDB:6AT5}. FT STRAND 238 243 {ECO:0000244|PDB:6AT5}. FT TURN 249 251 {ECO:0000244|PDB:6AT5}. FT STRAND 252 254 {ECO:0000244|PDB:6AT5}. FT STRAND 261 263 {ECO:0000244|PDB:6AT5}. FT STRAND 265 274 {ECO:0000244|PDB:6AT5}. FT HELIX 278 280 {ECO:0000244|PDB:6AT5}. FT STRAND 281 286 {ECO:0000244|PDB:6AT5}. FT STRAND 290 292 {ECO:0000244|PDB:3VCL}. FT STRAND 294 296 {ECO:0000244|PDB:6AT5}. SQ SEQUENCE 362 AA; 40460 MW; 5E5A7BDE031403D6 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHDQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGECVE WLRRYLENGK DKLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA //