HLAC_HUMAN
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 03-AUG-2022, entry version 203.
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 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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 insures 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=12; IntAct=EBI-1051396, EBI-8684277;
CC P10321; P43627: KIR2DL2; NbExp=4; 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=2; IntAct=EBI-1051396, EBI-15316524;
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 -!- 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. {ECO:0000269|PubMed:28650991,
CC 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}.
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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; 485.
DR IntAct; P10321; 101.
DR MINT; P10321; -.
DR STRING; 9606.ENSP00000365402; -.
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 GlyGen; P10321; 2 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (1 site).
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; P10321; -.
DR PeptideAtlas; P10321; -.
DR PRIDE; 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 Antibodypedia; 26870; 316 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 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; 585877; B-lymphoblastic leukemia/lymphoma with recurrent genetic abnormality.
DR PharmGKB; PA35057; -.
DR VEuPathDB; HostDB:ENSG00000204525; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT00980000198488; -.
DR OMA; EREDQEY; -.
DR OrthoDB; 1390181at2759; -.
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 BioGRID-ORCS; 3107; 292 hits in 998 CRISPR screens.
DR ChiTaRS; HLA-C; human.
DR EvolutionaryTrace; P10321; -.
DR GeneWiki; HLA-C; -.
DR GenomeRNAi; 3107; -.
DR Pharos; P10321; Tbio.
DR Proteomes; UP000005640; Chromosome 6.
DR Bgee; ENSG00000204525; Expressed in blood and 97 other 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: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; 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: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:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; 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; 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.
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 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
