ID   A0A140T912_HUMAN        Unreviewed;       372 AA.
AC   A0A140T912;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   16-JAN-2019, entry version 14.
DE   SubName: Full=HLA class I histocompatibility antigen, Cw-6 alpha chain {ECO:0000313|Ensembl:ENSP00000388708};
GN   Name=HLA-C {ECO:0000313|Ensembl:ENSP00000388708};
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:ENSP00000388708};
RN   [1] {ECO:0000313|Ensembl:ENSP00000388708, 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:ENSP00000388708}
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; BX927178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   jPOST; A0A140T912; -.
DR   PeptideAtlas; A0A140T912; -.
DR   PRIDE; A0A140T912; -.
DR   Ensembl; ENST00000453809; ENSP00000388708; ENSG00000237022.
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:A0A140T912,
KW   ECO:0000213|MaxQB:A0A140T912, ECO:0000213|PeptideAtlas:A0A140T912};
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_5007305562.
FT   TRANSMEM    308    332       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      209    297       Ig-like. {ECO:0000259|PROSITE:PS50835}.
SQ   SEQUENCE   372 AA;  41466 MW;  A4E4A1AC1EC0795A CRC64;
     MRVMAPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVRF
     DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ
     WMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARAAEQQ
     RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHLVSD HEATLRCWAL GFYPAEITLT
     WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP
     SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGH FLPTGGKGGS CSQAASSNSA
     QGSDESLIAC KA
//