ID A0A0G2JH50_HUMAN Unreviewed; 372 AA. AC A0A0G2JH50; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 13-FEB-2019, entry version 25. DE SubName: Full=HLA class I histocompatibility antigen, Cw-6 alpha chain {ECO:0000313|Ensembl:ENSP00000372813}; GN Name=HLA-C {ECO:0000313|Ensembl:ENSP00000372813}; 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 {ECO:0000313|Ensembl:ENSP00000372813, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000372813, ECO:0000313|Proteomes:UP000005640} 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., 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 [2] {ECO:0000213|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [3] {ECO:0000213|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; 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). RN [4] {ECO:0000313|Ensembl:ENSP00000372813} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. RN [5] {ECO:0000313|Ensembl:ENSP00000372979} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. {ECO:0000256|SAAS:SAAS00291881}. CC -!- SIMILARITY: Belongs to the MHC class I family. CC {ECO:0000256|RuleBase:RU004439, ECO:0000256|SAAS:SAAS00560993}. 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; BX248310; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX322539; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SwissPalm; A0A0G2JH50; -. DR EPD; A0A0G2JH50; -. DR jPOST; A0A0G2JH50; -. DR PRIDE; A0A0G2JH50; -. DR Ensembl; ENST00000383323; ENSP00000372813; ENSG00000206452. DR Ensembl; ENST00000383487; ENSP00000372979; ENSG00000206435. DR HGNC; HGNC:4933; HLA-C. DR ChiTaRS; HLA-C; human. DR Proteomes; UP000005640; Chromosome 6. 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:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. 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 Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00447792}; KW Immunity {ECO:0000256|SAAS:SAAS00446101}; KW Membrane {ECO:0000256|SAAS:SAAS00447790, ECO:0000256|SAM:Phobius}; KW MHC I {ECO:0000256|SAAS:SAAS00446101}; KW Proteomics identification {ECO:0000213|EPD:A0A0G2JH50, KW ECO:0000213|MaxQB:A0A0G2JH50, ECO:0000213|PeptideAtlas:A0A0G2JH50}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00447790, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00447790, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 372 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014514154. FT TRANSMEM 306 331 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 209 297 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 372 AA; 41565 MW; DF918B04998AD251 CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVQF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DKAAQITQRK WEAAREAEQR RAYLEGTCVE WLRRYLENGK KTLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWGP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGH FLPTGGKGGS CSQAASSNSA QGSDESLIAC KA //