ID HLAC_HUMAN Reviewed; 366 AA. AC P10321; O02863; O02864; O02865; O02866; O02958; O19505; O19652; O19676; AC O62879; O62882; O62883; O62888; O78060; O78061; O78062; O78063; O78067; AC O78068; O78069; O78072; O78083; O78090; O78091; O78149; O78165; O78166; AC O78178; O78202; O78203; O78211; O78214; P04222; P30499; P30500; P30501; AC P30502; P30503; P30504; P30505; P30506; P30507; P30508; P30509; P30510; AC P79498; Q07000; Q29631; Q29641; Q29643; Q29652; Q29743; Q29768; Q29862; AC Q29864; Q29865; Q29867; Q29921; Q29959; Q29960; Q29963; Q29986; Q29989; AC Q29990; Q29991; Q29992; Q29993; Q30192; Q31605; Q31627; Q860R1; Q860R2; AC Q95463; Q95603; Q95604; Q99528; Q9BD28; Q9GIK4; Q9GIK8; Q9GJ33; Q9MY30; AC Q9MY31; Q9MY35; Q9MY49; Q9MY74; Q9MYI3; Q9TNN7; Q9TNZ8; Q9TPS4; Q9TPV8; AC Q9TPX2; Q9TQB4; Q9TQJ5; Q9TQP9; Q9UM32; Q9UM33; Q9UM42; Q9UQS9; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 3. DT 27-MAR-2024, entry version 212. DE RecName: Full=HLA class I histocompatibility antigen, C alpha chain; DE Short=HLA-C; DE AltName: Full=HLA-Cw; DE AltName: Full=Human leukocyte antigen C; DE Flags: Precursor; GN Name=HLA-C {ECO:0000312|HGNC:HGNC:4933}; Synonyms=HLAC; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*16:01), AND ALTERNATIVE SPLICING. RX PubMed=2914713; DOI=10.1007/bf00395855; RA Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., Boccoli G., RA Giannella G., Peschle C., Boncinelli E.; RT "Three new class I HLA alleles: structure of mRNAs and alternative RT mechanisms of processing."; RL Immunogenetics 29:80-91(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-309 (ALLELE C*07:01). RX PubMed=2714852; DOI=10.1007/bf00352839; RA Pohla H., Kuon W., Tabaczewski P., Doerner C., Weiss E.H.; RT "Allelic variation in HLA-B and HLA-C sequences and the evolution of the RT HLA-B alleles."; RL Immunogenetics 29:297-307(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*04:01). RX PubMed=1711567; DOI=10.1084/jem.174.1.53; RA Grassi F., Meneveri R., Gullberg M., Lopalco L., Rossi G.B., Lanza P., RA de Santis C., Brattsand G., Butto S., Ginelli E., Beretta A., RA Siccardi A.G.; RT "Human immunodeficiency virus type 1 gp120 mimics a hidden monomorphic RT epitope borne by class I major histocompatibility complex heavy chains."; RL J. Exp. Med. 174:53-62(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*04:01). RX PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., Williams R.C., RA Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES C*01:02; C*03:02 AND C*08:01). RX PubMed=1384166; DOI=10.1111/j.1399-0039.1992.tb01943.x; RA Zemmour J., Gumperz J.E., Hildebrand W.H., Ward F.E., Marsh S.G.E., RA Williams R.C., Parham P.; RT "The molecular basis for reactivity of anti-Cw1 and anti-Cw3 alloantisera RT with HLA-B46 haplotypes."; RL Tissue Antigens 39:249-257(1992). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES C*12:02 AND C*15:02). RX PubMed=7905471; DOI=10.1016/0198-8859(93)90509-y; RA Vilches C., de Pablo R., Herrero M.J., Moreno M.E., Kreisler M.; RT "Molecular cloning and polymerase chain reaction-sequence-specific RT oligonucleotide detection of the allele encoding the novel allospecificity RT HLA-Cw6.2 (Cw*1502) in Spanish gypsies."; RL Hum. Immunol. 37:259-263(1993). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*07:04). RX PubMed=7482492; DOI=10.1111/j.1399-0039.1995.tb02471.x; RA Vilches C., Bunce M., de Pablo R., Herrero M.J., Kreisler M.; RT "Anchored PCR cloning of the novel HLA-Cw*0704 allele detected by PCR- RT SSP."; RL Tissue Antigens 46:19-23(1995). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*07:02). RC TISSUE=Blood; RX PubMed=8655361; DOI=10.1016/0198-8859(95)00150-6; RA Wang H., Tokunaga K., Ishikawa Y., Asahina A., Kuwata S., Akaza T., RA Tadokoro K., Shibata Y., Takiguchi M., Juji T.; RT "Identification and DNA typing of two Cw7 alleles (Cw*0702 and Cw*0704) in RT Japanese, with the corrected sequence of Cw*0702."; RL Hum. Immunol. 45:52-58(1996). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*18:01). RX PubMed=9008313; DOI=10.1111/j.1399-0039.1996.tb02694.x; RA Vilches C., Bunce M., Sanz L., de Pablo R., Puente S., Kreisler M.; RT "Molecular cloning of two new HLA-C alleles: Cw*1801 and Cw*0706."; RL Tissue Antigens 48:698-702(1996). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*17:01). RX PubMed=9211742; DOI=10.1007/s002510050259; RA Wells R.S., Seielstad M.T., Bunce M., Tyan D.B., Bekele E., Parham P.; RT "Cw*1701 defines a divergent african HLA-C allelic lineage."; RL Immunogenetics 46:173-180(1997). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*17:01). RX PubMed=9098935; DOI=10.1111/j.1399-0039.1997.tb02749.x; RA Herrero M.J., Vilches C., de Pablo R., Puente S., Kreisler M.; RT "The complete primary structure of Cw*1701 reveals a highly divergent HLA RT class I molecule."; RL Tissue Antigens 49:267-270(1997). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*05:01). RX PubMed=10372547; DOI=10.1034/j.1399-0039.1999.530508.x; RA Baurain J.-F., Coulie P.G.; RT "Correction of HLA-Cw*0501 and identification of HLA-Cw*0711."; RL Tissue Antigens 53:510-512(1999). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE C*12:02). RX PubMed=2787363; RA Takiguchi M., Nishimura I., Hayashi H., Karaki S., Kariyone A., Kano K.; RT "The structure and expression of genes encoding serologically undetected RT HLA-C locus antigens."; RL J. Immunol. 143:1372-1378(1989). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE C*02:02). RX PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE C*06:02). RX PubMed=1598685; DOI=10.1111/j.1399-0039.1992.tb01923.x; RA Steinle A., Noessner E., Schendel D.J.; RT "Isolation and characterization of a genomic HLA-Cw6 clone."; RL Tissue Antigens 39:134-137(1992). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-338 (ALLELE C*07:01). RX PubMed=10488744; DOI=10.1034/j.1399-0039.1999.540208.x; RA van der Vlies S.A., Voorter C.E., van den Berg-Loonen E.M.; RT "There is more to HLA -C than exons 2 and 3: sequencing exons 1, 4 and 5."; RL Tissue Antigens 54:169-177(1999). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES C*07:02; C*04:01; C*15:02 AND RP C*18:01). 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 [18] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*03:04). RA Domena J.D.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. RN [19] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*14:02). RA Zhang L., Ellexson M.E., Hildebrand W.H.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE C*05:01). RA Ellexson M.E., Zhang W., Hildebrand W.H.; RT "Cw*0501new."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [21] 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., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., 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., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [22] RP FUNCTION. RX PubMed=8265661; DOI=10.1073/pnas.90.24.12005; RA Falk K., Roetzschke O., Grahovac B., Schendel D., Stevanovic S., Gnau V., RA Jung G., Strominger J.L., Rammensee H.G.; RT "Allele-specific peptide ligand motifs of HLA-C molecules."; RL Proc. Natl. Acad. Sci. U.S.A. 90:12005-12009(1993). RN [23] 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., Mulloy J.C., RA 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 [24] RP FUNCTION (ALLELE C*05:01). RX PubMed=11172028; DOI=10.1073/pnas.98.4.1781; RG HIV Controller Study Collaboration; RA Addo M.M., Altfeld M., Rosenberg E.S., Eldridge R.L., Philips M.N., RA Habeeb K., Khatri A., Brander C., Robbins G.K., Mazzara G.P., Goulder P.J., RA Walker B.D.; RT "The HIV-1 regulatory proteins Tat and Rev are frequently targeted by RT cytotoxic T lymphocytes derived from HIV-1-infected individuals."; RL Proc. Natl. Acad. Sci. U.S.A. 98:1781-1786(2001). RN [25] RP FUNCTION (ALLELES C*01:02; C*04:01; C*08:01; C*12:02 AND C*15:02). RX PubMed=12947002; DOI=10.1182/blood-2003-03-0824; RA Kondo E., Akatsuka Y., Kuzushima K., Tsujimura K., Asakura S., Tajima K., RA Kagami Y., Kodera Y., Tanimoto M., Morishima Y., Takahashi T.; RT "Identification of novel CTL epitopes of CMV-pp65 presented by a variety of RT HLA alleles."; RL Blood 103:630-638(2004). RN [26] RP FUNCTION, AND INTERACTION WITH KIR2DL1; KIR2DL2; KIR2DL3 AND KIR2DS1. RX PubMed=16141329; DOI=10.1073/pnas.0503594102; RA Stewart C.A., Laugier-Anfossi F., Vely F., Saulquin X., Riedmuller J., RA Tisserant A., Gauthier L., Romagne F., Ferracci G., Arosa F.A., Moretta A., RA Sun P.D., Ugolini S., Vivier E.; RT "Recognition of peptide-MHC class I complexes by activating killer RT immunoglobulin-like receptors."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13224-13229(2005). RN [27] RP INTERACTION WITH THE PEPTIDE LOADING COMPLEX, MUTAGENESIS OF SER-112, RP GLYCOSYLATION AT ASN-110, AND SUBCELLULAR LOCATION. RX PubMed=18420581; DOI=10.1074/jbc.m709175200; RA Martayan A., Sibilio L., Setini A., Lo Monaco E., Tremante E., Fruci D., RA Colonna M., Giacomini P.; RT "N-linked glycosylation selectively regulates the generic folding of HLA- RT Cw1."; RL J. Biol. Chem. 283:16469-16476(2008). RN [28] 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 multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [29] RP FUNCTION (ALLELE C*04:01). RX PubMed=20104487; DOI=10.1002/eji.200939634; RA Makadzange A.T., Gillespie G., Dong T., Kiama P., Bwayo J., Kimani J., RA Plummer F., Easterbrook P., Rowland-Jones S.L.; RT "Characterization of an HLA-C-restricted CTL response in chronic HIV RT infection."; RL Eur. J. Immunol. 40:1036-1041(2010). RN [30] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH RP KIR2DL1 AND KIR2DS1. RX PubMed=20972337; DOI=10.1172/jci43998; RA Hiby S.E., Apps R., Sharkey A.M., Farrell L.E., Gardner L., Mulder A., RA Claas F.H., Walker J.J., Redman C.W., Redman C.C., Morgan L., Tower C., RA Regan L., Moore G.E., Carrington M., Moffett A.; RT "Maternal activating KIRs protect against human reproductive failure RT mediated by fetal HLA-C2."; RL J. Clin. Invest. 120:4102-4110(2010). RN [31] RP FUNCTION (C*01:02), AND INTERACTION WITH KIR2DL2 AND KIR2DL3. RX PubMed=20439706; DOI=10.1073/pnas.0913745107; RA Fadda L., Borhis G., Ahmed P., Cheent K., Pageon S.V., Cazaly A., RA Stathopoulos S., Middleton D., Mulder A., Claas F.H., Elliott T., RA Davis D.M., Purbhoo M.A., Khakoo S.I.; RT "Peptide antagonism as a mechanism for NK cell activation."; RL Proc. Natl. Acad. Sci. U.S.A. 107:10160-10165(2010). RN [32] RP NOMENCLATURE. RX PubMed=20356336; DOI=10.1111/j.1399-0039.2010.01466.x; RA Marsh S.G., Albert E.D., Bodmer W.F., Bontrop R.E., Dupont B., Erlich H.A., RA Fernandez-Vina M., Geraghty D.E., Holdsworth R., Hurley C.K., Lau M., RA Lee K.W., Mach B., Maiers M., Mayr W.R., Mueller C.R., Parham P., RA Petersdorf E.W., Sasazuki T., Strominger J.L., Svejgaard A., Terasaki P.I., RA Tiercy J.M., Trowsdale J.; RT "Nomenclature for factors of the HLA system, 2010."; RL Tissue Antigens 75:291-455(2010). RN [33] RP FUNCTION (ALLELE C*06:02). RX PubMed=24091323; DOI=10.1172/jci68991; RA Xiong S., Sharkey A.M., Kennedy P.R., Gardner L., Farrell L.E., Chazara O., RA Bauer J., Hiby S.E., Colucci F., Moffett A.; RT "Maternal uterine NK cell-activating receptor KIR2DS1 enhances RT placentation."; RL J. Clin. Invest. 123:4264-4272(2013). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [35] RP FUNCTION. RX PubMed=25311805; DOI=10.4049/jimmunol.1401689; RA Rasmussen M., Harndahl M., Stryhn A., Boucherma R., Nielsen L.L., RA Lemonnier F.A., Nielsen M., Buus S.; RT "Uncovering the peptide-binding specificities of HLA-C: a general strategy RT to determine the specificity of any MHC class I molecule."; RL J. Immunol. 193:4790-4802(2014). RN [36] RP VARIANT [LARGE SCALE ANALYSIS] MET-272, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA 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 [37] RP FUNCTION (ALLELE C*07:02). RX PubMed=29312307; DOI=10.3389/fimmu.2017.01776; RA Hosie L., Pachnio A., Zuo J., Pearce H., Riddell S., Moss P.; RT "Cytomegalovirus-Specific T Cells Restricted by HLA-Cw*0702 Increase RT Markedly with Age and Dominate the CD8+ T-Cell Repertoire in Older RT People."; RL Front. Immunol. 8:1776-1776(2017). RN [38] RP DOMAIN, AND POLYMORPHISM. RX PubMed=37264229; DOI=10.1038/s41590-023-01523-z; RA Lin Z., Bashirova A.A., Viard M., Garner L., Quastel M., Beiersdorfer M., RA Kasprzak W.K., Akdag M., Yuki Y., Ojeda P., Das S., Andresson T., RA Naranbhai V., Horowitz A., McMichael A.J., Hoelzemer A., Gillespie G.M., RA Garcia-Beltran W.F., Carrington M.; RT "HLA class I signal peptide polymorphism determines the level of CD94/NKG2- RT HLA-E-mediated regulation of effector cell responses."; RL Nat. Immunol. 24:1087-1097(2023). RN [39] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 25-302 (ALLELE C*03:04) IN COMPLEX RP WITH B2M PEPTIDE AND KIR2DL2, DISULFIDE BONDS, AND DOMAIN. RX PubMed=10850706; DOI=10.1038/35014520; RA Boyington J.C., Motyka S.A., Schuck P., Brooks A.G., Sun P.D.; RT "Crystal structure of an NK cell immunoglobulin-like receptor in complex RT with its class I MHC ligand."; RL Nature 405:537-543(2000). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 25-299 (ALLELE C*04:01) IN RP COMPLEX WITH B2M PEPTIDE AND KIR2DL1. RX PubMed=11323700; DOI=10.1038/87766; RA Fan Q.R., Long E.O., Wiley D.C.; RT "Crystal structure of the human natural killer cell inhibitory receptor RT KIR2DL1-HLA-Cw4 complex."; RL Nat. Immunol. 2:452-460(2001). RN [41] RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 26-298 (ALLELE C*08:01) IN RP COMPLEX WITH B2M AND PEPTIDE, FUNCTION (ALLELE C*08:01), DOMAIN, AND RP DISULFIDE BOND. RX PubMed=24990997; DOI=10.1128/jvi.00855-14; RA Choo J.A., Liu J., Toh X., Grotenbreg G.M., Ren E.C.; RT "The immunodominant influenza A virus M158-66 cytotoxic T lymphocyte RT epitope exhibits degenerate class I major histocompatibility complex RT restriction in humans."; RL J. Virol. 88:10613-10623(2014). RN [42] RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 26-298 (ALLELE C*05:01) IN RP COMPLEX WITH B2M AND PEPTIDE, X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF RP 26-300 (ALLELE C*07:02) IN COMPLEX WITH B2M AND PEPTIDE, SUBCELLULAR RP LOCATION, FUNCTION, AND DOMAIN. RX PubMed=28649982; DOI=10.1038/ncomms15924; RA Kaur G., Gras S., Mobbs J.I., Vivian J.P., Cortes A., Barber T., RA Kuttikkatte S.B., Jensen L.T., Attfield K.E., Dendrou C.A., Carrington M., RA McVean G., Purcell A.W., Rossjohn J., Fugger L.; RT "Structural and regulatory diversity shape HLA-C protein expression RT levels."; RL Nat. Commun. 8:15924-15924(2017). RN [43] RP ASSOCIATION OF ALLELE C*06:02 WITH PSORIASIS. RX PubMed=11122018; DOI=10.1046/j.1365-2133.2000.03885.x; RA Mallon E., Bunce M., Savoie H., Rowe A., Newson R., Gotch F., Bunker C.B.; RT "HLA-C and guttate psoriasis."; RL Br. J. Dermatol. 143:1177-1182(2000). RN [44] RP ASSOCIATION OF ALLELE C*06:02 WITH PSORIASIS. RX PubMed=16235096; DOI=10.1007/s00439-005-0048-2; RA Helms C., Saccone N.L., Cao L., Daw J.A.W., Cao K., Hsu T.M., RA Taillon-Miller P., Duan S., Gordon D., Pierce B., Ott J., Rice J., RA Fernandez-Vina M.A., Kwok P.-Y., Menter A., Bowcock A.M.; RT "Localization of PSORS1 to a haplotype block harboring HLA-C and distinct RT from corneodesmosin and HCR."; RL Hum. Genet. 118:466-476(2005). RN [45] RP INVOLVEMENT IN PSORS1 (ALLELE C*06:02). RX PubMed=16642438; DOI=10.1086/503821; RA Nair R.P., Stuart P.E., Nistor I., Hiremagalore R., Chia N.V.C., RA Jenisch S., Weichenthal M., Abecasis G.R., Lim H.W., Christophers E., RA Voorhees J.J., Elder J.T.; RT "Sequence and haplotype analysis supports HLA-C as the psoriasis RT susceptibility 1 gene."; RL Am. J. Hum. Genet. 78:827-851(2006). RN [46] RP INVOLVEMENT IN PSORS1 (ALLELE C*06:02). RX PubMed=26621454; DOI=10.1084/jem.20151093; RA Arakawa A., Siewert K., Stoehr J., Besgen P., Kim S.M., Ruehl G., RA Nickel J., Vollmer S., Thomas P., Krebs S., Pinkert S., Spannagl M., RA Held K., Kammerbauer C., Besch R., Dornmair K., Prinz J.C.; RT "Melanocyte antigen triggers autoimmunity in human psoriasis."; RL J. Exp. Med. 212:2203-2212(2015). RN [47] RP POLYMORPHISM. RX PubMed=28650991; DOI=10.1371/journal.pgen.1006862; RA Robinson J., Guethlein L.A., Cereb N., Yang S.Y., Norman P.J., RA Marsh S.G.E., Parham P.; RT "Distinguishing functional polymorphism from random variation in the RT sequences of >10,000 HLA-A, -B and -C alleles."; RL PLoS Genet. 13:E1006862-E1006862(2017). CC -!- FUNCTION: Antigen-presenting major histocompatibility complex class I CC (MHCI) molecule with an important role in reproduction and antiviral CC immunity (PubMed:20972337, PubMed:24091323, PubMed:20439706, CC PubMed:11172028, PubMed:20104487, PubMed:28649982, PubMed:29312307). In CC complex with B2M/beta 2 microglobulin displays a restricted repertoire CC of self and viral peptides and acts as a dominant ligand for inhibitory CC and activating killer immunoglobulin receptors (KIRs) expressed on NK CC cells (PubMed:16141329). In an allogeneic setting, such as during CC pregnancy, mediates interaction of extravillous trophoblasts with KIR CC on uterine NK cells and regulate trophoblast invasion necessary for CC placentation and overall fetal growth (PubMed:20972337, CC PubMed:24091323). During viral infection, may present viral peptides CC with low affinity for KIRs, impeding KIR-mediated inhibition through CC peptide antagonism and favoring lysis of infected cells CC (PubMed:20439706). Presents a restricted repertoire of viral peptides CC on antigen-presenting cells for recognition by alpha-beta T cell CC receptor (TCR) on HLA-C-restricted CD8-positive T cells, guiding CC antigen-specific T cell immune response to eliminate infected cells, CC particularly in chronic viral infection settings such as HIV-1 or CMV CC infection (PubMed:11172028, PubMed:20104487, PubMed:28649982). Both the CC peptide and the MHC molecule are recognized by TCR, the peptide is CC responsible for the fine specificity of antigen recognition and MHC CC residues account for the MHC restriction of T cells (By similarity). CC Typically presents intracellular peptide antigens of 9 amino acids that CC arise from cytosolic proteolysis via proteasome. Can bind different CC peptides containing allele-specific binding motifs, which are mainly CC defined by anchor residues at position 2 and 9. Preferentially displays CC peptides having a restricted repertoire of hydrophobic or aromatic CC amino acids (Phe, Ile, Leu, Met, Val and Tyr) at the C-terminal anchor CC (PubMed:8265661, PubMed:25311805). {ECO:0000250|UniProtKB:P04439, CC ECO:0000269|PubMed:11172028, ECO:0000269|PubMed:16141329, CC ECO:0000269|PubMed:20104487, ECO:0000269|PubMed:20439706, CC ECO:0000269|PubMed:20972337, ECO:0000269|PubMed:24091323, CC ECO:0000269|PubMed:25311805, ECO:0000269|PubMed:28649982, CC ECO:0000269|PubMed:29312307, ECO:0000269|PubMed:8265661}. CC -!- FUNCTION: ALLELE C*01:02: The peptide-bound form interacts with KIR2DL2 CC and KIR2DL3 inhibitory receptors on NK cells. The low affinity peptides CC compete with the high affinity peptides impeding KIR-mediated CC inhibition and favoring lysis of infected cells (PubMed:20439706). CC Presents to CD8-positive T cells a CMV epitope derived from UL83/pp65 CC (RCPEMISVL), an immediate-early antigen necessary for initiating viral CC replication (PubMed:12947002). {ECO:0000269|PubMed:12947002, CC ECO:0000269|PubMed:20439706}. CC -!- FUNCTION: ALLELE C*04:01: Presents a conserved HIV-1 epitope derived CC from env (SFNCGGEFF) to memory CD8-positive T cells, eliciting very CC strong IFNG responses (PubMed:20104487). Presents CMV epitope derived CC from UL83/pp65 (QYDPVAALF) to CD8-positive T cells, triggering T cell CC cytotoxic response (PubMed:12947002). {ECO:0000269|PubMed:12947002, CC ECO:0000269|PubMed:20104487}. CC -!- FUNCTION: ALLELE C*05:01: Presents HIV-1 epitope derived from rev CC (SAEPVPLQL) to CD8-positive T cells, triggering T cell cytotoxic CC response. {ECO:0000269|PubMed:11172028}. CC -!- FUNCTION: ALLELE C*06:02: In trophoblasts, interacts with KIR2DS2 on CC uterine NK cells and triggers NK cell activation, including secretion CC of cytokines such as GMCSF that enhances trophoblast migration. CC {ECO:0000269|PubMed:24091323}. CC -!- FUNCTION: ALLELE C*07:02: Plays an important role in the control of CC chronic CMV infection. Presents immunodominant CMV epitopes derived CC from IE1 (LSEFCRVL and CRVLCCYVL) and UL28 (FRCPRRFCF), both antigens CC synthesized during immediate-early period of viral replication. Elicits CC a strong anti-viral CD8-positive T cell immune response that increases CC markedly with age. {ECO:0000269|PubMed:29312307}. CC -!- FUNCTION: ALLELE C*08:01: Presents viral epitopes derived from CMV UL83 CC (VVCAHELVC) and IAV M1 (GILGFVFTL), triggering CD8-positive T cell CC cytotoxic response. {ECO:0000269|PubMed:12947002, CC ECO:0000269|PubMed:24990997}. CC -!- FUNCTION: ALLELE C*12:02: Presents CMV epitope derived from UL83 CC (VAFTSHEHF) to CD8-positive T cells. {ECO:0000269|PubMed:12947002}. CC -!- FUNCTION: ALLELE C*15:02: Presents CMV epitope derived from UL83 CC CC (VVCAHELVC) to CD8-positive T cells, triggering T cell cytotoxic CC response. {ECO:0000269|PubMed:12947002}. CC -!- SUBUNIT: Heterotrimer that consists of an alpha chain HLA-C, a beta CC chain B2M and a peptide (peptide-HLA-C-B2M) (PubMed:28649982, CC PubMed:10850706, PubMed:24990997). Early in biogenesis, HLA-C-B2M dimer CC interacts with the components of the peptide-loading complex composed CC of TAPBP, TAP1-TAP2, TAPBPL, PDIA3/ERP57 and CALR (PubMed:18420581). CC Interacts with TAP1-TAP2 transporter via TAPBP; this interaction is CC obligatory for the loading of peptide epitopes delivered to the CC endoplasmic reticulum (ER) by TAP1-TAP2 transporter (By similarity). CC Being very selective in the peptide binding, forms a stable interaction CC with TAP1-TAP2, often leading to the accumulation of free heavy chains CC in the ER (PubMed:18420581). Only optimally assembled peptide-HLA-C-B2M CC trimer translocates to the surface of antigen-presenting cells, where CC it interacts with TCR and CD8 coreceptor on the surface of T cells. CC HLA-C (via polymorphic alpha-1 and alpha-2 domains) interacts with CC antigen-specific TCR (via CDR3 domains) (By similarity). One HLA-C CC molecule (mainly via nonpolymorphic alpha-3 domain) interacts with one CC CD8A homodimer (via CDR-like loop); this interaction ensures peptide- CC HLA-C-B2M recognition by CD8-positive T cells only (By similarity). The CC peptide-HLA-C-B2M complex also interacts with KIRs. HLA-C type 1 (C1, CC with Asn104), including HLA-C*02, C*04, C*05, C*06 and C*15, interact CC with KIR2DL1 and KIR2DS1, and HLA-C type 2 (C2, with Lys104), including CC HLA-C*01, C*03, C*07 and C*08, interact with KIR2DL2 and KIR2DL3 CC (PubMed:20972337, PubMed:24091323, PubMed:16141329, PubMed:20439706, CC PubMed:11323700, PubMed:10850706). {ECO:0000250|UniProtKB:P04439, CC ECO:0000269|PubMed:10850706, ECO:0000269|PubMed:11323700, CC ECO:0000269|PubMed:16141329, ECO:0000269|PubMed:18420581, CC ECO:0000269|PubMed:20439706, ECO:0000269|PubMed:20972337, CC ECO:0000269|PubMed:24091323, ECO:0000269|PubMed:24990997, CC ECO:0000269|PubMed:28649982}. CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 p12I accessory CC protein. {ECO:0000269|PubMed:11390610}. CC -!- INTERACTION: CC P10321; P43626: KIR2DL1; NbExp=15; IntAct=EBI-1051396, EBI-8684277; CC P10321; P43627: KIR2DL2; NbExp=5; IntAct=EBI-1051396, EBI-13941368; CC P10321; P43628: KIR2DL3; NbExp=9; IntAct=EBI-1051396, EBI-8632435; CC P10321; Q14954: KIR2DS1; NbExp=7; IntAct=EBI-1051396, EBI-2865976; CC P10321; P43632: KIR2DS4; NbExp=8; IntAct=EBI-1051396, EBI-13916812; CC P10321; Q14953: KIR2DS5; NbExp=30; IntAct=EBI-1051396, EBI-16823921; CC P10321; Q14943: KIR3DS1; NbExp=4; IntAct=EBI-1051396, EBI-15316524; CC P10321; Q8N423: LILRB2; NbExp=6; IntAct=EBI-1051396, EBI-2816428; CC P10321; F2VZG2: KIR2DS4; Xeno; NbExp=2; IntAct=EBI-1051396, EBI-13917082; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18420581, CC ECO:0000269|PubMed:20972337, ECO:0000269|PubMed:28649982}; Single-pass CC type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:18420581}; Single-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P10321-1; Sequence=Displayed; CC Name=2; CC IsoId=P10321-2; Sequence=VSP_060393, VSP_060394; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in fetal extravillous CC trophoblasts in the decidua basalis (at protein level). CC {ECO:0000269|PubMed:20972337}. CC -!- DOMAIN: The alpha-1 domain is a structural part of the peptide-binding CC cleft. {ECO:0000269|PubMed:28649982}. CC -!- DOMAIN: The alpha-2 domain is a structural part of the peptide-binding CC cleft (PubMed:28649982, PubMed:10850706, PubMed:24990997). Mediates the CC interaction with TAP1-TAP2 complex. {ECO:0000269|PubMed:10850706, CC ECO:0000269|PubMed:24990997, ECO:0000269|PubMed:28649982}. CC -!- DOMAIN: The alpha-3 Ig-like domain mediates the interaction with CD8 CC coreceptor. {ECO:0000250|UniProtKB:P04439}. CC -!- DOMAIN: The VL9 peptide/epitope (VMAPRT[V/L][L/V/I/F]L) derived from CC the signal sequence is loaded onto HLA-E and enables HLA-E expression CC at the plasma membrane. Distinct VL9 peptides presented by HLA-E CC variably affect its recognition by KLRD1-KLRC1 or KLRD1-KLRC2 receptors CC on NK cells, setting NK cell activation threshold. Common HLA-C CC allotypes contain functional VL9 peptides (VMAPRTLIL and VMAPRTLLL). CC VL9 peptides (VMAPRTALL and VMAPRQALL) derived from HLA-C*07, C*17 and CC C*18 allotypes display low affinity for HLA-E and fail to drive NK cell CC activation. {ECO:0000269|PubMed:37264229}. CC -!- PTM: N-linked glycosylation at Asn-110 is required for efficient CC interaction with CANX and CALR chaperones and appropriate HLA-C-B2M CC folded conformers prior to peptide loading. CC {ECO:0000269|PubMed:18420581, ECO:0000269|PubMed:19159218}. CC -!- POLYMORPHISM: Displays lower polymorphism than HLA-A and HLA-B. CC Polymorphic residues encode for alpha-1 and alpha-2 domains of the CC peptide-binding cleft, where they contribute to variations in peptide CC binding and TCR recognition among different alleles. The human CC population is estimated to have millions of HLA-C alleles. But only 14 CC common HLA-C alleles are considered core alleles, representing all CC functionally significant variation (polymorphism) in alpha-1 and alpha- CC 2 domains. These are: C*01:02; C*02:02; C*03:02; C*04:01; C*05:01; CC C*06:02; C*07:01; C*07:04; C*08:01; C*12:02; C*14:02; C*15:02; C*16:01 CC and C*17:01. Among these, C*01:02; C*02:02; C*03:02; C*08:01; C*12:02; CC C*14:02 and C*15:02, were likely passed by introgression from archaic CC to modern humans. Functional alleles of more recent origin (non-core) CC were derived by recombination (PubMed:28650991). The sequence shown is CC that of C*07:02. The sequences of core alleles and common CC representative alleles of serologically distinct allele groups are CC described as variants of C*07:02. Allelic variations of HLA-C signal CC peptide regulate HLA-E recognition by KLRD1-KLRC1 and KLRD1-KLRC2 CC receptors in viral infection and tumorigenesis by affecting its CC processing and by changing the affinity of HLA-E-VL9 complex for KLRD1- CC KLRC1 and KLRD1-KLRC2 receptors. {ECO:0000269|PubMed:28650991, CC ECO:0000269|PubMed:37264229, ECO:0000305}. CC -!- DISEASE: Psoriasis 1 (PSORS1) [MIM:177900]: A common, chronic CC inflammatory disease of the skin with multifactorial etiology. It is CC characterized by red, scaly plaques usually found on the scalp, elbows CC and knees. These lesions are caused by abnormal keratinocyte CC proliferation and infiltration of inflammatory cells into the dermis CC and epidermis. {ECO:0000269|PubMed:16642438}. Note=Disease CC susceptibility is associated with variants affecting the gene CC represented in this entry. Allele C*06:02 presents a melanocyte CC autoantigen ADAMTSL5 (VRSRRCLRL) to Valpha3S1/Vbeta13S1 TCR on CD8- CC positive T cells, and may trigger an autoimmune response against CC melanocytes. {ECO:0000269|PubMed:26621454}. CC -!- MISCELLANEOUS: [Isoform 2]: A transcript of allele C*16:01. This CC isoform lacks the transmembrane domain and is predicted to be a CC secreted protein. {ECO:0000305|PubMed:2914713}. 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; M24097; AAA59656.1; -; mRNA. DR EMBL; X58536; CAA41427.1; -; mRNA. DR EMBL; M84386; AAA59705.1; -; mRNA. DR EMBL; M84171; AAA59685.1; -; mRNA. DR EMBL; M84172; AAA59686.1; -; mRNA. DR EMBL; M84174; AAA59688.1; -; mRNA. DR EMBL; X70856; CAA50209.1; -; mRNA. DR EMBL; X67818; CAA48029.1; -; mRNA. DR EMBL; X83394; CAA58313.1; -; mRNA. DR EMBL; D38526; BAA07531.1; -; mRNA. DR EMBL; D49819; BAA08625.1; -; mRNA. DR EMBL; X96582; CAA65401.1; -; mRNA. DR EMBL; U62824; AAB67322.1; -; mRNA. DR EMBL; X98742; CAA67294.1; -; mRNA. DR EMBL; AJ010748; CAA09340.1; -; mRNA. DR EMBL; M28172; AAA59670.1; -; Genomic_DNA. DR EMBL; M24030; AAA59671.1; -; Genomic_DNA. DR EMBL; Z22752; CAA80437.1; -; Genomic_DNA. DR EMBL; Z22753; CAA80437.1; JOINED; Genomic_DNA. DR EMBL; Z22754; CAA80437.1; JOINED; Genomic_DNA. DR EMBL; Y18533; CAB71800.1; -; Genomic_DNA. DR EMBL; Y18534; CAB71800.1; JOINED; Genomic_DNA. DR EMBL; Y18535; CAB71800.1; JOINED; Genomic_DNA. DR EMBL; Y18536; CAB71800.1; JOINED; Genomic_DNA. DR EMBL; AJ293016; CAC04321.1; -; Genomic_DNA. DR EMBL; AJ293017; CAC04322.1; -; Genomic_DNA. DR EMBL; AJ278494; CAB95011.1; -; Genomic_DNA. DR EMBL; AJ420250; CAD12435.1; -; Genomic_DNA. DR EMBL; AJ420253; CAD12438.1; -; Genomic_DNA. DR EMBL; M99389; AAA88088.1; -; mRNA. DR EMBL; U41386; AAC32743.1; -; mRNA. DR EMBL; U57028; AAD11469.1; -; mRNA. DR EMBL; AL671883; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS34393.1; -. [P10321-1] DR RefSeq; NP_002108.4; NM_002117.5. [P10321-1] DR PDB; 1EFX; X-ray; 3.00 A; A=25-302. DR PDB; 1IM9; X-ray; 2.80 A; A/E=25-299. DR PDB; 1QQD; X-ray; 2.70 A; A=26-298. DR PDB; 3BZF; X-ray; 2.50 A; P/Q=3-11. DR PDB; 4NT6; X-ray; 1.84 A; A=26-298. DR PDB; 5VGD; X-ray; 2.32 A; A=26-302. DR PDB; 5VGE; X-ray; 2.60 A; A=26-300. DR PDB; 5W67; X-ray; 2.30 A; A=25-300. DR PDB; 5W69; X-ray; 2.80 A; A/C/E/G=25-300. DR PDB; 5W6A; X-ray; 1.74 A; A/C=25-300. DR PDB; 6JTO; X-ray; 1.70 A; A=26-298. DR PDB; 6PA1; X-ray; 3.01 A; A/E=25-301. DR PDB; 6PAG; X-ray; 2.50 A; A=25-302. DR PDBsum; 1EFX; -. DR PDBsum; 1IM9; -. DR PDBsum; 1QQD; -. DR PDBsum; 3BZF; -. DR PDBsum; 4NT6; -. DR PDBsum; 5VGD; -. DR PDBsum; 5VGE; -. DR PDBsum; 5W67; -. DR PDBsum; 5W69; -. DR PDBsum; 5W6A; -. DR PDBsum; 6JTO; -. DR PDBsum; 6PA1; -. DR PDBsum; 6PAG; -. DR AlphaFoldDB; P10321; -. DR SMR; P10321; -. DR BioGRID; 109352; 511. DR IntAct; P10321; 111. DR MINT; P10321; -. DR STRING; 9606.ENSP00000365402; -. DR TCDB; 9.A.75.1.3; the mhc ii receptor (mhc2r) family. DR GlyConnect; 1352; 8 N-Linked glycans (1 site). DR GlyConnect; 1353; 1 N-Linked glycan (1 site). DR GlyConnect; 1354; 5 N-Linked glycans (1 site). DR GlyConnect; 1355; 1 N-Linked glycan (1 site). DR GlyConnect; 1356; 8 N-Linked glycans (1 site). DR GlyConnect; 1357; 4 N-Linked glycans (1 site). DR GlyConnect; 1358; 1 N-Linked glycan (1 site). DR GlyConnect; 1359; 8 N-Linked glycans (1 site). DR GlyConnect; 1360; 5 N-Linked glycans (1 site). DR GlyConnect; 1361; 4 N-Linked glycans (1 site). DR GlyConnect; 1362; 8 N-Linked glycans (1 site). DR GlyConnect; 1363; 4 N-Linked glycans (1 site). DR GlyConnect; 1364; 8 N-Linked glycans (1 site). DR GlyCosmos; P10321; 2 sites, 5 glycans. DR GlyGen; P10321; 5 sites, 4 N-linked glycans (1 site), 2 O-linked glycans (4 sites). DR iPTMnet; P10321; -. DR MetOSite; P10321; -. DR PhosphoSitePlus; P10321; -. DR SwissPalm; P10321; -. DR BioMuta; HLA-C; -. DR DMDM; 34223716; -. DR EPD; P10321; -. DR jPOST; P10321; -. DR MassIVE; P10321; -. DR PaxDb; 9606-ENSP00000365402; -. DR PeptideAtlas; P10321; -. DR ProteomicsDB; 51687; -. DR ProteomicsDB; 52599; -. DR ProteomicsDB; 54698; -. DR ProteomicsDB; 54699; -. DR ProteomicsDB; 54700; -. DR ProteomicsDB; 54701; -. DR ProteomicsDB; 54702; -. DR ProteomicsDB; 54703; -. DR ProteomicsDB; 58493; -. DR ProteomicsDB; 61274; -. DR ProteomicsDB; 61277; -. DR ProteomicsDB; 61278; -. DR ProteomicsDB; 61279; -. DR ProteomicsDB; 75736; -. DR ProteomicsDB; 83917; -. DR Pumba; P10321; -. DR Antibodypedia; 26870; 372 antibodies from 26 providers. DR CPTC; P10321; 1 antibody. DR DNASU; 3107; -. DR Ensembl; ENST00000376228.10; ENSP00000365402.5; ENSG00000204525.18. [P10321-1] DR GeneID; 3107; -. DR KEGG; hsa:3107; -. DR MANE-Select; ENST00000376228.10; ENSP00000365402.5; NM_002117.6; NP_002108.4. DR UCSC; uc063wnd.1; human. DR UCSC; uc063yse.1; human. DR AGR; HGNC:4933; -. DR CTD; 3107; -. DR DisGeNET; 3107; -. DR GeneCards; HLA-C; -. DR HGNC; HGNC:4933; HLA-C. DR HPA; ENSG00000204525; Tissue enhanced (lymphoid). DR MalaCards; HLA-C; -. DR MIM; 177900; phenotype. DR neXtProt; NX_P10321; -. DR OpenTargets; ENSG00000204525; -. DR Orphanet; 585909; B-lymphoblastic leukemia/lymphoma with t(9;22)(q34.1;q11.2). DR PharmGKB; PA35057; -. DR VEuPathDB; HostDB:ENSG00000204525; -. DR eggNOG; ENOG502RQEK; Eukaryota. DR GeneTree; ENSGT00980000198488; -. DR InParanoid; P10321; -. DR OMA; PETERWI; -. DR OrthoDB; 3840485at2759; -. DR PhylomeDB; P10321; -. DR TreeFam; TF336617; -. DR PathwayCommons; P10321; -. 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-2172127; DAP12 interactions. 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-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC. DR SignaLink; P10321; -. DR SIGNOR; P10321; -. DR BioGRID-ORCS; 3107; 296 hits in 1058 CRISPR screens. DR ChiTaRS; HLA-C; human. DR EvolutionaryTrace; P10321; -. DR GeneWiki; HLA-C; -. DR GenomeRNAi; 3107; -. DR Pharos; P10321; Tbio. DR PRO; PR:P10321; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000204525; Expressed in blood and 99 other cell types or tissues. DR ExpressionAtlas; P10321; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA: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:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042612; C:MHC class I protein complex; IDA: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; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0046977; F:TAP binding; IDA:UniProtKB. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IDA:UniProtKB. DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:GO_Central. DR CDD; cd07698; IgC1_MHC_I_alpha3; 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; 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 PANTHER; PTHR16675:SF252; HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, C ALPHA CHAIN; 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. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Cell membrane; KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; KW Host-virus interaction; Immunity; Innate immunity; Membrane; MHC I; KW Phosphoprotein; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..24 FT /evidence="ECO:0000255" FT CHAIN 25..366 FT /note="HLA class I histocompatibility antigen, C alpha FT chain" FT /id="PRO_0000018868" FT TOPO_DOM 25..308 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 309..333 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 334..366 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 209..297 FT /note="Ig-like C1-type" FT REGION 3..11 FT /note="VL9 epitope" FT /evidence="ECO:0000269|PubMed:37264229" FT REGION 25..114 FT /note="Alpha-1" FT /evidence="ECO:0000255" FT REGION 115..206 FT /note="Alpha-2" FT /evidence="ECO:0000255" FT REGION 207..298 FT /note="Alpha-3" FT /evidence="ECO:0000255" FT REGION 299..308 FT /note="Connecting peptide" FT BINDING 87 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_note="self- and pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:28649982" FT BINDING 94 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_note="self- and pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:28649982" FT BINDING 101 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_note="self- and pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:28649982" FT BINDING 183 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_note="self- and pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:28649982" FT BINDING 195 FT /ligand="a peptide antigen" FT /ligand_id="ChEBI:CHEBI:166823" FT /ligand_note="self- and pathogen-derived peptide antigen" FT /evidence="ECO:0000269|PubMed:28649982" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01900" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P01900" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT DISULFID 125..188 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:10850706, ECO:0000269|PubMed:24990997" FT DISULFID 227..283 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:10850706, ECO:0000269|PubMed:24990997" FT VAR_SEQ 153..157 FT /note="DLRSW -> HLRSC (in isoform 2)" FT /evidence="ECO:0000269|PubMed:2914713" FT /id="VSP_060393" FT VAR_SEQ 297..338 FT /note="SWEPSSQPTIPIMGIVAGLAVLVVLAVLGAVVTAMMCRRKSS -> RW (in FT isoform 2)" FT /evidence="ECO:0000269|PubMed:2914713" FT /id="VSP_060394" FT VARIANT 7 FT /note="R -> Q (in allele C*17:01; dbSNP:rs41548123)" FT /evidence="ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082408" FT VARIANT 8 FT /note="A -> T (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02 and allele C*16:01; FT dbSNP:rs2308525)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|Ref.18, FT ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082409" FT VARIANT 10 FT /note="L -> I (in allele C*01:02, allele C*03:02, allele FT C*03:04, allele C*04:01, allele C*05:01, allele C*06:02, FT allele C*08:01, allele C*12:02, allele C*14:02 and allele FT C*16:01; dbSNP:rs2308527)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2787363, FT ECO:0000269|PubMed:2914713, ECO:0000269|PubMed:7905471, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082410" FT VARIANT 16 FT /note="G -> A (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01 and allele C*17:01; FT dbSNP:rs1050451)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742, ECO:0000269|Ref.18, FT ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082411" FT VARIANT 20 FT /note="T -> I (in allele C*17:01; dbSNP:rs41549413)" FT /evidence="ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082412" FT VARIANT 25 FT /note="C -> G (in allele C*03:02, allele C*03:04, allele FT C*04:01 and allele C*17:01; dbSNP:rs2074493)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1317015, ECO:0000269|PubMed:1384166, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742, ECO:0000269|Ref.18" FT /id="VAR_082413" FT VARIANT 30 FT /note="R -> K (in allele C*01:02; dbSNP:rs1131151)" FT /evidence="ECO:0000269|PubMed:1384166" FT /id="VAR_082414" FT VARIANT 33 FT /note="D -> F (in allele C*01:02; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:1384166" FT /id="VAR_082415" FT VARIANT 33 FT /note="D -> S (in allele C*04:01 and allele C*14:02; FT requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1317015, ECO:0000269|PubMed:1711567, FT ECO:0000269|Ref.19" FT /id="VAR_082416" FT VARIANT 33 FT /note="D -> Y (in allele C*02:02, allele C*03:02, allele FT C*03:04, allele C*05:01, allele C*08:01, allele C*12:02, FT allele C*15:02, allele C*16:01 and allele C*17:01; FT dbSNP:rs9264668)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1711567, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:2787363, FT ECO:0000269|PubMed:2914713, ECO:0000269|PubMed:7905471, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.20" FT /id="VAR_082417" FT VARIANT 35 FT /note="A -> S (in allele C*01:02, allele C*04:01 and allele FT C*14:02; dbSNP:rs1050445)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1317015, ECO:0000269|PubMed:1384166, FT ECO:0000269|PubMed:1711567, ECO:0000269|Ref.19" FT /id="VAR_082418" FT VARIANT 38 FT /note="R -> W (in allele C*04:01; dbSNP:rs41542423)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1317015, ECO:0000269|PubMed:1711567" FT /id="VAR_082419" FT VARIANT 40 FT /note="G -> S (in allele C*02:02; dbSNP:rs151341100)" FT /evidence="ECO:0000269|PubMed:2715640" FT /id="VAR_082420" FT VARIANT 45 FT /note="R -> H (in allele C*02:02, allele C*03:02, allele FT C*03:04 and allele C*15:02; dbSNP:rs1050437)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:7905471, FT ECO:0000269|Ref.18" FT /id="VAR_082421" FT VARIANT 48 FT /note="S -> A (in allele C*02:02, allele C*03:02, allele FT C*03:04, allele C*04:01, allele C*05:01, allele C*08:01, FT allele C*12:02, allele C*14:02, allele C*15:02, allele FT C*16:01 and allele C*17:01; dbSNP:rs707911)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1711567, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:2787363, FT ECO:0000269|PubMed:2914713, ECO:0000269|PubMed:7905471, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082422" FT VARIANT 59 FT /note="R -> Q (in allele C*05:01 and C*08:01; FT dbSNP:rs1050428)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:1384166, ECO:0000269|Ref.20" FT /id="VAR_082423" FT VARIANT 73 FT /note="A -> E (in allele C*04:01; dbSNP:rs1050409)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1317015, ECO:0000269|PubMed:1711567" FT /id="VAR_082424" FT VARIANT 90 FT /note="K -> N (in allele C*07:01, C*15:02; FT dbSNP:rs28626310)" FT /evidence="ECO:0000269|PubMed:10488744, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:2714852, FT ECO:0000269|PubMed:7905471" FT /id="VAR_082425" FT VARIANT 97 FT /note="A -> T (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*05:01, allele C*08:01, FT allele C*14:02, allele C*15:02 and allele C*16:01; FT dbSNP:rs41543814)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1384166, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|Ref.18, FT ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082426" FT VARIANT 101 FT /note="S -> N (in allele C*02:02, allele C*04:01, allele FT C*05:01, allele C*06:02, allele C*15:02, allele C*17:01 and FT allele C*18:01; dbSNP:rs2308557)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1598685, ECO:0000269|PubMed:1711567, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:7905471, FT ECO:0000269|PubMed:9008313, ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742, ECO:0000269|Ref.20" FT /id="VAR_082427" FT VARIANT 104 FT /note="N -> K (in allele C*02:02, allele C*04:01, allele FT C*05:01, allele C*06:02, allele C*15:02, allele C*17:01 and FT allele C*18:01; dbSNP:rs17408553)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1598685, ECO:0000269|PubMed:1711567, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:7905471, FT ECO:0000269|PubMed:9008313, ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742, ECO:0000269|Ref.20" FT /id="VAR_082428" FT VARIANT 114 FT /note="D -> A (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*05:01, allele C*08:01, FT allele C*12:02, allele C*14:02, allele C*15:02, allele FT C*16:01 and allele C*17:01; dbSNP:rs1131123)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1384166, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:2787363, FT ECO:0000269|PubMed:2914713, ECO:0000269|PubMed:7905471, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082429" FT VARIANT 118 FT /note="T -> I (in allele C*03:02, allele C*03:04 and allele FT C*15:02; dbSNP:rs1131119)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:7905471, FT ECO:0000269|Ref.18" FT /id="VAR_082430" FT VARIANT 119 FT /note="L -> F (in allele C*07:04; dbSNP:rs1071649)" FT /evidence="ECO:0000269|PubMed:7482492" FT /id="VAR_082431" FT VARIANT 119 FT /note="L -> I (in allele C*03:04, allele C*15:02 and allele FT C*17:01; dbSNP:rs1071649)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742, ECO:0000269|Ref.18" FT /id="VAR_082432" FT VARIANT 121 FT /note="R -> W (in allele C*01:02, allele C*06:02, allele FT C*14:02 and allele C*16:01; dbSNP:rs1131118)" FT /evidence="ECO:0000269|PubMed:1384166, FT ECO:0000269|PubMed:1598685, ECO:0000269|PubMed:2914713, FT ECO:0000269|Ref.19" FT /id="VAR_082433" FT VARIANT 123 FT /note="S -> C (in allele C*01:02; dbSNP:rs1131115)" FT /evidence="ECO:0000269|PubMed:1384166" FT /id="VAR_082434" FT VARIANT 123 FT /note="S -> F (in allele C*04:01, allele C*14:02 and allele FT C*18:01; dbSNP:rs1131115)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1317015, ECO:0000269|PubMed:1711567, FT ECO:0000269|PubMed:9008313, ECO:0000269|Ref.19" FT /id="VAR_082435" FT VARIANT 123 FT /note="S -> Y (in allele C*07:01, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*05:01, allele C*06:02, FT allele C*07:04, allele C*08:01, allele C*12:02, allele FT C*15:02, allele C*16:01 and allele C*17:01; FT dbSNP:rs1131115)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:10488744, ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:2714852, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742, ECO:0000269|Ref.18, FT ECO:0000269|Ref.20" FT /id="VAR_082436" FT VARIANT 127 FT /note="L -> V (in allele C*03:02 and allele C*03:04; FT dbSNP:rs34592426)" FT /evidence="ECO:0000269|PubMed:1384166, ECO:0000269|Ref.18" FT /id="VAR_082437" FT VARIANT 137 FT /note="Y -> H (in allele C*15:02; dbSNP:rs2308574)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:7905471" FT /id="VAR_082438" FT VARIANT 138 FT /note="D -> N (in allele C*04:01, allele C*05:01, allele FT C*08:01, allele C*17:01 and allele C*18:01; FT dbSNP:rs2308575)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1711567, FT ECO:0000269|PubMed:9008313, ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742, ECO:0000269|Ref.20" FT /id="VAR_082439" FT VARIANT 140 FT /note="S -> F (in allele C*04:01, allele C*05:01, allele FT C*07:04, allele C*08:01, allele C*17:01 and allele C*18:01; FT dbSNP:rs713032)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1711567, FT ECO:0000269|PubMed:7482492, ECO:0000269|PubMed:9008313, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.20" FT /id="VAR_082440" FT VARIANT 140 FT /note="S -> L (in allele C*15:02)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:7905471" FT /id="VAR_082441" FT VARIANT 140 FT /note="S -> Y (in alleles C*01:02, C*03:04; FT dbSNP:rs713032)" FT /evidence="ECO:0000269|PubMed:1384166, ECO:0000269|Ref.18" FT /id="VAR_082442" FT VARIANT 162 FT /note="T -> K (in allele C*05:01)" FT /evidence="ECO:0000269|PubMed:10372547, ECO:0000269|Ref.20" FT /id="VAR_082443" FT VARIANT 167 FT /note="T -> S (in allele C*17:01; dbSNP:rs142570222)" FT /evidence="ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082444" FT VARIANT 171 FT /note="L -> W (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01; FT dbSNP:rs1050366)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082445" FT VARIANT 176 FT /note="A -> E (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*12:02, allele C*14:02, allele FT C*15:02, allele C*17:01 and allele C*18:01; FT dbSNP:rs2308590)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:7905471, FT ECO:0000269|PubMed:9008313, ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742, ECO:0000269|Ref.18, FT ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082446" FT VARIANT 176 FT /note="A -> T (in allele C*08:01; dbSNP:rs41552817)" FT /evidence="ECO:0000269|PubMed:1384166" FT /id="VAR_082447" FT VARIANT 180 FT /note="L -> D (in allele C*07:04; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:7482492" FT /id="VAR_082448" FT VARIANT 180 FT /note="L -> Q (in allele C*16:01; dbSNP:rs2308592)" FT /evidence="ECO:0000269|PubMed:2914713" FT /id="VAR_082449" FT VARIANT 180 FT /note="L -> R (in allele C*01:02, allele C*04:01, allele FT C*05:01, allele C*14:02 and allele C*18:01; FT dbSNP:rs2308592)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1711567, FT ECO:0000269|PubMed:9008313, ECO:0000269|Ref.19, FT ECO:0000269|Ref.20" FT /id="VAR_082450" FT VARIANT 180 FT /note="L -> W (in allele C*02:02, allele C*06:02 and allele FT C*12:02; dbSNP:rs796925732)" FT /evidence="ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:2715640, ECO:0000269|PubMed:2787363, FT ECO:0000269|PubMed:7905471" FT /id="VAR_082451" FT VARIANT 187 FT /note="T -> E (in alleles C*02:02 and allele C*17:01; FT requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742" FT /id="VAR_082452" FT VARIANT 187 FT /note="T -> L (in allele C*03:02 and allele C*03:04; FT requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:1384166, ECO:0000269|Ref.18" FT /id="VAR_082453" FT VARIANT 194 FT /note="R -> G (in allele C*17:01; dbSNP:rs2308598)" FT /evidence="ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082454" FT VARIANT 197 FT /note="E -> K (in allele C*03:02 and allele C*03:04; FT dbSNP:rs1050357)" FT /evidence="ECO:0000269|PubMed:1384166, ECO:0000269|Ref.18" FT /id="VAR_082455" FT VARIANT 201 FT /note="E -> K (in allele C*05:01, allele C*07:04 and allele FT C*08:01; dbSNP:rs1131103)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:7482492, FT ECO:0000269|Ref.20" FT /id="VAR_082456" FT VARIANT 208 FT /note="P -> H (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01; FT dbSNP:rs1131096)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082457" FT VARIANT 208 FT /note="P -> R (in allele C*17:01; dbSNP:rs1131096)" FT /evidence="ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082458" FT VARIANT 217 FT /note="P -> L (in allele C*16:01; dbSNP:rs1050343)" FT /evidence="ECO:0000269|PubMed:2914713" FT /id="VAR_082459" FT VARIANT 218 FT /note="L -> V (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and FT allele C*18:01; dbSNP:rs1050716)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082460" FT VARIANT 235 FT /note="A -> T (in allele C*02:02; dbSNP:rs41562012)" FT /evidence="ECO:0000269|PubMed:2715640" FT /id="VAR_082461" FT VARIANT 243 FT /note="R -> W (in alleles C*01:02, allele C*03:02, allele FT C*03:04, allele C*04:01, allele C*14:02 and allele C*18:01; FT dbSNP:rs1050328)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1317015, ECO:0000269|PubMed:1384166, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:9008313, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19" FT /id="VAR_082462" FT VARIANT 272 FT /note="V -> M (in allele C*01:02; dbSNP:rs1050276)" FT /evidence="ECO:0000269|PubMed:1384166, FT ECO:0007744|PubMed:25944712" FT /id="VAR_082463" FT VARIANT 277 FT /note="Q -> E (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01; FT dbSNP:rs707908)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082464" FT VARIANT 285 FT /note="M -> V (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and FT allele C*18:01; dbSNP:rs2308622)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082465" FT VARIANT 291 FT /note="Q -> P (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01; FT dbSNP:rs1131015)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082466" FT VARIANT 294 FT /note="L -> C (in allele C*17:01; requires 2 nucleotide FT substitutions; dbSNP:rs1211800658)" FT /evidence="ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082467" FT VARIANT 297 FT /note="S -> R (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and FT allele C*18:01; dbSNP:rs2308628)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082468" FT VARIANT 299 FT /note="E -> G (in alleles C*05:01 and allele C*08:01)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:1384166, ECO:0000269|Ref.20" FT /id="VAR_082469" FT VARIANT 299 FT /note="E -> K (in allele C*04:01, allele C*17:01 and allele FT C*18:01; dbSNP:rs41556321)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1317015, ECO:0000269|PubMed:1711567, FT ECO:0000269|PubMed:9008313, ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082470" FT VARIANT 308..319 FT /note="IMGIVAGLAVLV -> NLGIVSGPAVLAVLAVLA (in allele FT C*17:01)" FT /evidence="ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082471" FT VARIANT 309 FT /note="M -> V (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01 and allele C*18:01; FT dbSNP:rs1050180)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082472" FT VARIANT 319 FT /note="V -> A (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02 and allele C*16:01; FT dbSNP:rs1050147)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|Ref.18, FT ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082473" FT VARIANT 327 FT /note="V -> M (in allele C*04:01; dbSNP:rs146911342)" FT /evidence="ECO:0000269|PubMed:12622774, FT ECO:0000269|PubMed:1317015, ECO:0000269|PubMed:1711567" FT /id="VAR_082474" FT VARIANT 328 FT /note="V -> M (in allele C*05:01, allele C*06:02, allele FT C*08:01, allele C*12:02 and allele C*15:02)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1384166, FT ECO:0000269|PubMed:1598685, ECO:0000269|PubMed:2787363, FT ECO:0000269|PubMed:7905471, ECO:0000269|Ref.20" FT /id="VAR_082475" FT VARIANT 329 FT /note="T -> A (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and FT allele C*18:01; dbSNP:rs1130947)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082476" FT VARIANT 330 FT /note="A -> V (in allele C*02:02, allele C*04:01, allele FT C*05:01, allele C*06:02, allele C*08:01, allele C*12:02, FT allele C*14:02, allele C*15:02, allele C*16:01 and allele FT C*18:01; dbSNP:rs1050105)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082477" FT VARIANT 331 FT /note="M -> V (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and FT allele C*18:01; dbSNP:rs1130935)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082478" FT VARIANT 332 FT /note="M -> I (in allele C*17:01; dbSNP:rs41540416)" FT /evidence="ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082479" FT VARIANT 333 FT /note="C -> H (in allele C*17:01; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:9098935, FT ECO:0000269|PubMed:9211742" FT /id="VAR_082480" FT VARIANT 350 FT /note="C -> S (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and FT allele C*18:01; dbSNP:rs3177824)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082481" FT VARIANT 363 FT /note="T -> A (in allele C*01:02, allele C*02:02, allele FT C*03:02, allele C*03:04, allele C*04:01, allele C*05:01, FT allele C*06:02, allele C*08:01, allele C*12:02, allele FT C*14:02, allele C*15:02, allele C*16:01, allele C*17:01 and FT allele C*18:01; dbSNP:rs1130838)" FT /evidence="ECO:0000269|PubMed:10372547, FT ECO:0000269|PubMed:12622774, ECO:0000269|PubMed:1317015, FT ECO:0000269|PubMed:1384166, ECO:0000269|PubMed:1598685, FT ECO:0000269|PubMed:1711567, ECO:0000269|PubMed:2715640, FT ECO:0000269|PubMed:2787363, ECO:0000269|PubMed:2914713, FT ECO:0000269|PubMed:7905471, ECO:0000269|PubMed:9008313, FT ECO:0000269|PubMed:9098935, ECO:0000269|PubMed:9211742, FT ECO:0000269|Ref.18, ECO:0000269|Ref.19, ECO:0000269|Ref.20" FT /id="VAR_082482" FT MUTAGEN 112 FT /note="S->G: Impairs N-linked glycosylation resulting in FT impaired interaction with CANX and CALR chaperones as well FT as TAPBPL." FT /evidence="ECO:0000269|PubMed:18420581" FT STRAND 27..36 FT /evidence="ECO:0007829|PDB:6JTO" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:1QQD" FT HELIX 74..77 FT /evidence="ECO:0007829|PDB:6JTO" FT HELIX 81..109 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:5VGD" FT STRAND 118..127 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 131..142 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 145..150 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:6JTO" FT HELIX 162..174 FT /evidence="ECO:0007829|PDB:6JTO" FT HELIX 176..185 FT /evidence="ECO:0007829|PDB:6JTO" FT HELIX 187..198 FT /evidence="ECO:0007829|PDB:6JTO" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 210..217 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 219..235 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:6JTO" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:4NT6" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 265..274 FT /evidence="ECO:0007829|PDB:6JTO" FT HELIX 278..280 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 281..286 FT /evidence="ECO:0007829|PDB:6JTO" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:1IM9" FT STRAND 294..297 FT /evidence="ECO:0007829|PDB:6JTO" SQ SEQUENCE 366 AA; 40649 MW; 59C23D95FD1D0BC8 CRC64; MRVMAPRALL LLLSGGLALT ETWACSHSMR YFDTAVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV SLRNLRGYYN QSEDGSHTLQ RMSGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK LEAARAAEQL RAYLEGTCVE WLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL QEPLTLSWEP SSQPTIPIMG IVAGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA //