TAP2_HUMAN
ID TAP2_HUMAN Reviewed; 686 AA.
AC Q03519; B0V2J8; O95410; Q53FI6; Q5HY71; Q96PT8; Q9UQ83;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Antigen peptide transporter 2;
DE Short=APT2;
DE EC=7.4.2.- {ECO:0000269|PubMed:11274390, ECO:0000269|PubMed:25377891, ECO:0000269|PubMed:25656091};
DE AltName: Full=ATP-binding cassette sub-family B member 3;
DE AltName: Full=Peptide supply factor 2 {ECO:0000303|PubMed:1946428};
DE AltName: Full=Peptide transporter PSF2;
DE Short=PSF-2 {ECO:0000303|PubMed:1946428};
DE AltName: Full=Peptide transporter TAP2;
DE AltName: Full=Peptide transporter involved in antigen processing 2;
DE AltName: Full=Really interesting new gene 11 protein;
DE Short=RING11 {ECO:0000303|PubMed:1538751};
GN Name=TAP2 {ECO:0000303|PubMed:10605026, ECO:0000312|HGNC:HGNC:44};
GN Synonyms=ABCB3, PSF2, RING11, Y1;
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 [GENOMIC DNA] (ALLELE TAP2*01:01) (ISOFORM 1), AND
RP POLYMORPHISM.
RX PubMed=1453454; DOI=10.1016/0022-2836(92)90832-5;
RA Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., Trowsdale J.;
RT "DNA sequence analysis of 66 kb of the human MHC class II region encoding a
RT cluster of genes for antigen processing.";
RL J. Mol. Biol. 228:433-441(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE TAP2*01:01/TAP2*02:01) (ISOFORM 1), AND
RP POLYMORPHISM.
RX PubMed=1741401; DOI=10.1073/pnas.89.4.1463;
RA Powis S.H., Mockridge I., Kelly A., Kerr L.-A., Glynne R.J., Gileadi U.,
RA Beck S., Trowsdale J.;
RT "Polymorphism in a second ABC transporter gene located within the class II
RT region of the human major histocompatibility complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1463-1467(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE TAP2*02:01) (ISOFORM 1), AND
RP POLYMORPHISM.
RX PubMed=1946428; DOI=10.1073/pnas.88.22.10094;
RA Bahram S., Arnold D., Bresnahan M., Strominger J.L., Spies T.;
RT "Two putative subunits of a peptide pump encoded in the human major
RT histocompatibility complex class II region.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10094-10098(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE TAP2*01:02) (ISOFORM 1), AND
RP POLYMORPHISM.
RX PubMed=8428770; DOI=10.1007/bf00216802;
RA Powis S.H., Tonks S., Mockridge I., Kelly A.P., Bodmer J.G., Trowsdale J.;
RT "Alleles and haplotypes of the MHC-encoded ABC transporters TAP1 and
RT TAP2.";
RL Immunogenetics 37:373-380(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE TAP2*BKY2) (ISOFORM 1), VARIANT
RP TAP2*BKY2 VAL-577, AND POLYMORPHISM.
RC TISSUE=Blood;
RX PubMed=9324024; DOI=10.1002/art.1780400919;
RA Kumagai S., Kanagawa S., Morinobu A., Takada M., Nakamura K., Sugai S.,
RA Maruya E., Saji H.;
RT "Association of a new allele of the TAP2 gene, TAP2*Bky2 (Val577), with
RT susceptibility to Sjogren's syndrome.";
RL Arthritis Rheum. 40:1685-1692(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ILE-379.
RC TISSUE=Spleen;
RX PubMed=9916708;
RA Yan G., Shi L., Faustman D.;
RT "Novel splicing of the human MHC-encoded peptide transporter confers unique
RT properties.";
RL J. Immunol. 162:852-859(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE TAP2*01:01) (ISOFORM 1), AND
RP POLYMORPHISM.
RX PubMed=8568858; DOI=10.1006/jmbi.1996.0001;
RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., Hosking L.K.,
RA Jackson A., Kelly A., Newell W.R., Sanseau P., Radley E., Thorpe K.L.,
RA Trowsdale J.;
RT "Evolutionary dynamics of non-coding sequences within the class II region
RT of the human MHC.";
RL J. Mol. Biol. 255:1-13(1996).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE TAP2*BKY2) (ISOFORM 1).
RC TISSUE=Liver, and Synovium;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES TAP2*03A AND
RP TAP2*BKY2).
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 [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 65-686 (ALLELE TAP2*01:03) (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=7792761; DOI=10.1111/j.1399-0039.1995.tb02431.x;
RA Cano P., Baxter-Lowe L.A.;
RT "Novel human TAP2*103 allele shows further polymorphism in the ATP-binding
RT domain.";
RL Tissue Antigens 45:139-142(1995).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-686 (ISOFORM 1), AND VARIANTS
RP THR-374 AND ILE-467.
RX PubMed=9672156; DOI=10.1111/j.1399-0039.1998.tb02992.x;
RA Tang J., Allen S., Karita E., Musonda R., Kaslow R.A.;
RT "New TAP2 polymorphisms in Africans.";
RL Tissue Antigens 51:556-562(1998).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 517-645 (ALLELE TAP2*01:01/TAP2*01:02)
RP (ISOFORM 1).
RA Singal D.P., Ye M., D'Souza M.;
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 517-645 (ALLELE TAP2*01:01/TAP2*01:02)
RP (ISOFORM 1).
RX PubMed=8162639;
RA Singal D.P., Ye M., Qiu X., D'Souza M.;
RT "Polymorphisms in the TAP2 gene and their association with rheumatoid
RT arthritis.";
RL Clin. Exp. Rheumatol. 12:29-33(1994).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=1589036; DOI=10.1038/357342a0;
RA Kleijmeer M.J., Kelly A., Geuze H.J., Slot J.W., Townsend A., Trowsdale J.;
RT "Location of MHC-encoded transporters in the endoplasmic reticulum and cis-
RT Golgi.";
RL Nature 357:342-344(1992).
RN [16]
RP FUNCTION, AND INTERACTION WITH TAP1.
RX PubMed=1538751; DOI=10.1038/355641a0;
RA Kelly A., Powis S.H., Kerr L.A., Mockridge I., Elliott T., Bastin J.,
RA Uchanska-Ziegler B., Ziegler A., Trowsdale J., Townsend A.;
RT "Assembly and function of the two ABC transporter proteins encoded in the
RT human major histocompatibility complex.";
RL Nature 355:641-644(1992).
RN [17]
RP FUNCTION.
RX PubMed=7500034; DOI=10.1084/jem.182.6.1883;
RA van Endert P.M., Riganelli D., Greco G., Fleischhauer K., Sidney J.,
RA Sette A., Bach J.F.;
RT "The peptide-binding motif for the human transporter associated with
RT antigen processing.";
RL J. Exp. Med. 182:1883-1895(1995).
RN [18]
RP INTERACTION WITH HERPES SIMPLEX VIRUS US12/ICP47 (MICROBIAL INFECTION).
RX PubMed=7760936; DOI=10.1038/375415a0;
RA Frueh K., Ahn K., Djaballah H., Sempe P., van Endert P.M., Tampe R.,
RA Peterson P.A., Yang Y.;
RT "A viral inhibitor of peptide transporters for antigen presentation.";
RL Nature 375:415-418(1995).
RN [19]
RP INTERACTION WITH HLA-A*02-B2M COMPLEX.
RX PubMed=8805302; DOI=10.1016/s0960-9822(02)00611-5;
RA Lewis J.W., Neisig A., Neefjes J., Elliott T.;
RT "Point mutations in the alpha 2 domain of HLA-A2.1 define a functionally
RT relevant interaction with TAP.";
RL Curr. Biol. 6:873-883(1996).
RN [20]
RP INTERACTION WITH HLA-A*02-B2M COMPLEX.
RX PubMed=8630735; DOI=10.1016/s1074-7613(00)80416-1;
RA Peace-Brewer A.L., Tussey L.G., Matsui M., Li G., Quinn D.G.,
RA Frelinger J.A.;
RT "A point mutation in HLA-A*0201 results in failure to bind the TAP complex
RT and to present virus-derived peptides to CTL.";
RL Immunity 4:505-514(1996).
RN [21]
RP PEPTIDE-BINDING SITE.
RX PubMed=8955196;
RA Nijenhuis M., Hammerling G.J.;
RT "Multiple regions of the transporter associated with antigen processing
RT (TAP) contribute to its peptide binding site.";
RL J. Immunol. 157:5467-5477(1996).
RN [22]
RP ACTIVITY REGULATION (MICROBIAL INFECTION), AND INHIBITION BY US12/ICP47.
RX PubMed=8670825; DOI=10.1002/j.1460-2075.1996.tb00689.x;
RA Ahn K., Meyer T.H., Uebel S., Sempe P., Djaballah H., Yang Y.,
RA Peterson P.A., Frueh K., Tampe R.;
RT "Molecular mechanism and species specificity of TAP inhibition by herpes
RT simplex virus ICP47.";
RL EMBO J. 15:3247-3255(1996).
RN [23]
RP ACTIVITY REGULATION (MICROBIAL INFECTION), AND INHIBITION BY US6
RP GLYCOPROTEIN.
RX PubMed=9175839; DOI=10.1016/s1074-7613(00)80349-0;
RA Ahn K., Gruhler A., Galocha B., Jones T.R., Wiertz E.J.H.J., Ploegh H.L.,
RA Peterson P.A., Yang Y., Frueh K.;
RT "The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide
RT translocation by TAP.";
RL Immunity 6:613-621(1997).
RN [24]
RP FUNCTION.
RX PubMed=9256420; DOI=10.1073/pnas.94.17.8976;
RA Uebel S., Kraas W., Kienle S., Wiesmueller K.H., Jung G., Tampe R.;
RT "Recognition principle of the TAP transporter disclosed by combinatorial
RT peptide libraries.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8976-8981(1997).
RN [25]
RP SUBUNIT, AND INTERACTION WITH HLA-E-B2M.
RX PubMed=9427624; DOI=10.1016/s0960-9822(98)70014-4;
RA Braud V.M., Allan D.S., Wilson D., McMichael A.J.;
RT "TAP- and tapasin-dependent HLA-E surface expression correlates with the
RT binding of an MHC class I leader peptide.";
RL Curr. Biol. 8:1-10(1998).
RN [26]
RP ACTIVITY REGULATION (MICROBIAL INFECTION), AND INHIBITION BY US6
RP GLYCOPROTEIN.
RX PubMed=11157746; DOI=10.1093/emboj/20.3.387;
RA Hewitt E.W., Gupta S.S., Lehner P.J.;
RT "The human cytomegalovirus gene product US6 inhibits ATP binding by TAP.";
RL EMBO J. 20:387-396(2001).
RN [27]
RP INTERACTION WITH ADENOVIRUS E3-19K GLYCOPROTEIN (MICROBIAL INFECTION).
RX PubMed=10227971;
RA Bennett E.M., Bennink J.R., Yewdell J.W., Brodsky F.M.;
RT "Adenovirus E19 has two mechanisms for affecting class I MHC expression.";
RL J. Immunol. 162:5049-5052(1999).
RN [28]
RP INTERACTION WITH HLA-F.
RX PubMed=10605026; DOI=10.4049/jimmunol.164.1.319;
RA Wainwright S.D., Biro P.A., Holmes C.H.;
RT "HLA-F is a predominantly empty, intracellular, TAP-associated MHC class Ib
RT protein with a restricted expression pattern.";
RL J. Immunol. 164:319-328(2000).
RN [29]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11274390; DOI=10.1073/pnas.061467898;
RA Gorbulev S., Abele R., Tampe R.;
RT "Allosteric crosstalk between peptide-binding, transport, and ATP
RT hydrolysis of the ABC transporter TAP.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3732-3737(2001).
RN [30]
RP INTERACTION WITH EBV BNLF2A (MICROBIAL INFECTION).
RX PubMed=19201886; DOI=10.4049/jimmunol.0803218;
RA Horst D., van Leeuwen D., Croft N.P., Garstka M.A., Hislop A.D.,
RA Kremmer E., Rickinson A.B., Wiertz E.J.H.J., Ressing M.E.;
RT "Specific targeting of the EBV lytic phase protein BNLF2a to the
RT transporter associated with antigen processing results in impairment of HLA
RT class I-restricted antigen presentation.";
RL J. Immunol. 182:2313-2324(2009).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [32]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TAPBP.
RX PubMed=22638925; DOI=10.1007/s00018-012-1005-6;
RA Hulpke S., Tomioka M., Kremmer E., Ueda K., Abele R., Tampe R.;
RT "Direct evidence that the N-terminal extensions of the TAP complex act as
RT autonomous interaction scaffolds for the assembly of the MHC I peptide-
RT loading complex.";
RL Cell. Mol. Life Sci. 69:3317-3327(2012).
RN [33]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF ASP-638.
RX PubMed=25377891; DOI=10.1038/ncomms6419;
RA Grossmann N., Vakkasoglu A.S., Hulpke S., Abele R., Gaudet R., Tampe R.;
RT "Mechanistic determinants of the directionality and energetics of active
RT export by a heterodimeric ABC transporter.";
RL Nat. Commun. 5:5419-5419(2014).
RN [34]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION (MICROBIAL
RP INFECTION).
RX PubMed=25656091; DOI=10.1038/ncomms7199;
RA Fischbach H., Doering M., Nikles D., Lehnert E., Baldauf C., Kalinke U.,
RA Tampe R.;
RT "Ultrasensitive quantification of TAP-dependent antigen
RT compartmentalization in scarce primary immune cell subsets.";
RL Nat. Commun. 6:6199-6199(2015).
RN [35]
RP FUNCTION, SUBUNIT, INTERACTION WITH TAPBP, SITE, AND MUTAGENESIS OF ASP-16.
RX PubMed=26611325; DOI=10.1038/srep17341;
RA Blees A., Reichel K., Trowitzsch S., Fisette O., Bock C., Abele R.,
RA Hummer G., Schaefer L.V., Tampe R.;
RT "Assembly of the MHC I peptide-loading complex determined by a conserved
RT ionic lock-switch.";
RL Sci. Rep. 5:17341-17341(2015).
RN [36]
RP VARIANTS ILE-379 AND ALA-665.
RX PubMed=1570316; DOI=10.1073/pnas.89.9.3932;
RA Colonna M., Bresnahan M., Bahram S., Strominger J.L., Spies T.;
RT "Allelic variants of the human putative peptide transporter involved in
RT antigen processing.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3932-3936(1992).
RN [37]
RP INVOLVEMENT IN BLS1.
RX PubMed=7517574; DOI=10.1126/science.7517574;
RA de la Salle H., Hanau D., Fricker D., Urlacher A., Kelly A., Salamero J.,
RA Powis S.H., Donato L., Bausinger H., Laforet M., Jeras M., Spehner D.,
RA Bieber T., Falkenrodt A., Cazenave J.-P., Trowsdale J., Tongio M.-M.;
RT "Homozygous human TAP peptide transporter mutation in HLA class I
RT deficiency.";
RL Science 265:237-241(1994).
RN [38]
RP VARIANTS THR-374; ILE-379; ILE-467; SER-513 THR-565; CYS-651; ALA-665 AND
RP GLN-GLU-GLY-GLN-ASP-LEU-TYR-SER-ARG-LEU-VAL-GLN-GLN-ARG-LEU-MET-ASP-686
RP INS, AND POLYMORPHISM.
RX PubMed=11294565; DOI=10.1038/sj.gene.6363731;
RA Tang J., Freedman D.O., Allen S., Karita E., Musonda R., Braga C.,
RA Jamieson B.D., Louie L., Kaslow R.A.;
RT "Genotyping TAP2 variants in North American Caucasians, Brazilians, and
RT Africans.";
RL Genes Immun. 2:32-40(2001).
CC -!- FUNCTION: ABC transporter associated with antigen processing. In
CC complex with TAP1 mediates unidirectional translocation of peptide
CC antigens from cytosol to endoplasmic reticulum (ER) for loading onto
CC MHC class I (MHCI) molecules (PubMed:25656091, PubMed:25377891). Uses
CC the chemical energy of ATP to export peptides against the concentration
CC gradient (PubMed:25377891). During the transport cycle alternates
CC between 'inward-facing' state with peptide binding site facing the
CC cytosol to 'outward-facing' state with peptide binding site facing the
CC ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a
CC switch to hydrolysis-competent 'outward-facing' conformation ready for
CC peptide loading onto nascent MHCI molecules. Subsequently ATP
CC hydrolysis resets the transporter to the 'inward facing' state for a
CC new cycle (PubMed:25377891, PubMed:25656091, PubMed:11274390).
CC Typically transports intracellular peptide antigens of 8 to 13 amino
CC acids that arise from cytosolic proteolysis via IFNG-induced
CC immunoproteasome. Binds peptides with free N- and C-termini, the first
CC three and the C-terminal residues being critical. Preferentially
CC selects peptides having a highly hydrophobic residue at position 3 and
CC hydrophobic or charged residues at the C-terminal anchor. Proline at
CC position 2 has the most destabilizing effect (PubMed:7500034,
CC PubMed:9256420, PubMed:11274390). As a component of the peptide loading
CC complex (PLC), acts as a molecular scaffold essential for peptide-MHCI
CC assembly and antigen presentation (PubMed:26611325, PubMed:1538751,
CC PubMed:25377891). {ECO:0000269|PubMed:11274390,
CC ECO:0000269|PubMed:1538751, ECO:0000269|PubMed:25377891,
CC ECO:0000269|PubMed:25656091, ECO:0000269|PubMed:26611325,
CC ECO:0000269|PubMed:7500034, ECO:0000269|PubMed:9256420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a peptide antigen(in) + ATP + H2O = a peptide antigen(out) +
CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:65972, Rhea:RHEA-COMP:16941,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:166823, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:11274390, ECO:0000269|PubMed:25377891,
CC ECO:0000269|PubMed:25656091};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65973;
CC Evidence={ECO:0000305|PubMed:11274390, ECO:0000305|PubMed:25377891,
CC ECO:0000305|PubMed:25656091};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25377891};
CC -!- ACTIVITY REGULATION: Inhibited at high ER lumenal peptide
CC concentrations. {ECO:0000269|PubMed:25377891}.
CC -!- ACTIVITY REGULATION: (Microbial infection) Inhibited by herpes simplex
CC virus US12/ICP47 protein, which blocks the peptide-binding site of
CC TAP1-TAP2. {ECO:0000269|PubMed:25656091, ECO:0000269|PubMed:8670825}.
CC -!- ACTIVITY REGULATION: (Microbial infection) Inhibited by human
CC cytomegalovirus US6 glycoprotein, which binds to the lumenal side of
CC TAP1-TAP2 complex and inhibits peptide translocation by specifically
CC blocking ATP-binding and preventing TAP1-TAP2 conformational
CC rearrangement induced by peptide binding. {ECO:0000269|PubMed:11157746,
CC ECO:0000269|PubMed:25656091, ECO:0000269|PubMed:9175839}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for ATP {ECO:0000269|PubMed:11274390};
CC KM=0.099 mM for ATP {ECO:0000269|PubMed:25377891};
CC Vmax=2 umol/min/mg enzyme toward ATP {ECO:0000269|PubMed:11274390};
CC -!- SUBUNIT: Heterodimer of TAP1 and TAP2 (TAP1-TAP2) (PubMed:1538751). A
CC component of the peptide loading complex (PLC), interacts via TAPBP
CC with MHCI heterodimer; this interaction mediates peptide-MHCI assembly
CC (PubMed:26611325). Recruits TAPBP in a 1:1 stoichiometry
CC (PubMed:22638925). Interacts with classical MHCI such as HLA-A*02-B2M;
CC this interaction is obligatory for the loading of peptide epitopes
CC (PubMed:8805302, PubMed:8630735). Interacts with non-classical MHCI
CC molecules including HLA-E-B2M and HLA-F-B2M as well as PLC component
CC CALR before the peptide loading (PubMed:9427624, PubMed:10605026).
CC {ECO:0000269|PubMed:10605026, ECO:0000269|PubMed:1538751,
CC ECO:0000269|PubMed:22638925, ECO:0000269|PubMed:26611325,
CC ECO:0000269|PubMed:8630735, ECO:0000269|PubMed:8805302,
CC ECO:0000269|PubMed:9427624}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC BLNF2a. {ECO:0000269|PubMed:19201886}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
CC US12/ICP47. {ECO:0000269|PubMed:7760936}.
CC -!- SUBUNIT: (Microbial infection) Interacts with adenovirus E3-19K
CC glycoprotein, which binds TAP1-TAP2 and acts as a TAPBP inhibitor,
CC preventing TAP1-TAP2 association with MHCI.
CC {ECO:0000269|PubMed:10227971}.
CC -!- INTERACTION:
CC Q03519; Q03518: TAP1; NbExp=18; IntAct=EBI-780781, EBI-747259;
CC Q03519; O15533: TAPBP; NbExp=8; IntAct=EBI-780781, EBI-874801;
CC Q03519; P0C739: BNLF2a; Xeno; NbExp=6; IntAct=EBI-780781, EBI-9346744;
CC Q03519; Q77CE4: gN; Xeno; NbExp=2; IntAct=EBI-780781, EBI-11303846;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:1589036, ECO:0000269|PubMed:22638925}; Multi-pass
CC membrane protein {ECO:0000255}. Note=The transmembrane segments seem to
CC form a pore in the membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q03519-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03519-2; Sequence=VSP_038904;
CC -!- DOMAIN: The peptide-binding site is shared between the cytoplasmic
CC loops of TAP1 and TAP2. {ECO:0000269|PubMed:8955196}.
CC -!- DOMAIN: The nucleotide-binding domain (NBD) mediates ATP hydrolysis
CC coupled to peptide translocation. Two ATP molecules are accommodated at
CC distinct nucleotide binding sites (NBS) at TAP1-TAP2 dimer interface.
CC Each NBS is formed by Walker A (GxxGxGKST) and Q-loop motifs from NBD
CC of one subunit, while the NBD from the second subunit completes the
CC active site by contributing the C loop motif (LSGGQ). Each ATP molecule
CC is coordinated via the beta- and gamma-phosphates to a Mg2+ ion, which
CC is necessary for ATP hydrolysis. {ECO:0000250|UniProtKB:P36370}.
CC -!- POLYMORPHISM: 4 common alleles are officially recognized: TAP2*01:01
CC (TAP2A or PSF2A or RING11A), TAP2*01:02 (TAP2E), TAP2*01:03 (TAP2F),
CC and TAP2*02:01 (TAP2B or PSF2B or RING11B). Other relatively common
CC alleles have been identified: TAP2*01D, TAP2*01E, TAP2*01F, TAP2*01G,
CC TAP2*01H, TAP2*02B, TAP2*02C (TAP2*02:02), TAP2*02D, TAP2*02E,
CC TAP2*02F, TAP2*03A and TAP2*04A. The sequence shown is that of
CC TAP2*01:01. {ECO:0000269|PubMed:11294565, ECO:0000269|PubMed:1453454,
CC ECO:0000269|PubMed:1741401, ECO:0000269|PubMed:1946428,
CC ECO:0000269|PubMed:8428770, ECO:0000269|PubMed:8568858}.
CC -!- POLYMORPHISM: The allele TAP2*Bky2 is commonly found only in the
CC Japanese population. It may be associated with susceptibility to
CC Sjoegren syndrome, an autoimmune disorder characterized by abnormal
CC dryness of the conjunctiva, cornea and mouth due to exocrine glands
CC dysfunction. {ECO:0000269|PubMed:9324024}.
CC -!- DISEASE: Bare lymphocyte syndrome 1 (BLS1) [MIM:604571]: A HLA class I
CC deficiency. Contrary to bare lymphocyte syndromes type 2 and type 3,
CC which are characterized by early-onset severe combined
CC immunodeficiency, class I antigen deficiencies are not accompanied by
CC particular pathologic manifestations during the first years of life.
CC Systemic infections have not been described. Chronic bacterial
CC infections, often beginning in the first decade of life, are restricted
CC to the respiratory tract. {ECO:0000269|PubMed:7517574}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC MHC peptide exporter (TC 3.A.1.209) subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=TAP2base; Note=TAP2 mutation db;
CC URL="http://structure.bmc.lu.se/idbase/TAP2base/";
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; X66401; CAA47027.1; -; Genomic_DNA.
DR EMBL; M84748; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M74447; AAA59841.1; -; mRNA.
DR EMBL; Z22935; CAA80522.1; -; mRNA.
DR EMBL; Z22936; CAA80523.1; -; mRNA.
DR EMBL; AB073779; BAB71769.1; -; mRNA.
DR EMBL; AF105151; AAD12059.1; -; mRNA.
DR EMBL; X87344; CAA60788.1; -; Genomic_DNA.
DR EMBL; AK222823; BAD96543.1; -; mRNA.
DR EMBL; AK223300; BAD97020.1; -; mRNA.
DR EMBL; BX296564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR788227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX682530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR762476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002751; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U07844; AAA79901.1; -; mRNA.
DR EMBL; AH007554; AAD23381.1; -; Genomic_DNA.
DR EMBL; L09191; AAA58648.1; -; mRNA.
DR EMBL; L10287; AAA58649.1; -; mRNA.
DR CCDS; CCDS4755.1; -. [Q03519-2]
DR CCDS; CCDS78129.1; -. [Q03519-1]
DR PIR; B41538; B41538.
DR RefSeq; NP_000535.3; NM_000544.3.
DR RefSeq; NP_001276972.1; NM_001290043.1. [Q03519-1]
DR RefSeq; NP_061313.2; NM_018833.2. [Q03519-2]
DR PDB; 5U1D; EM; 3.97 A; B=1-686.
DR PDBsum; 5U1D; -.
DR AlphaFoldDB; Q03519; -.
DR SMR; Q03519; -.
DR BioGRID; 112754; 131.
DR DIP; DIP-322N; -.
DR IntAct; Q03519; 29.
DR MINT; Q03519; -.
DR STRING; 9606.ENSP00000364034; -.
DR ChEMBL; CHEMBL4523654; -.
DR TCDB; 3.A.1.209.1; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q03519; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q03519; -.
DR PhosphoSitePlus; Q03519; -.
DR BioMuta; TAP2; -.
DR DMDM; 549044; -.
DR EPD; Q03519; -.
DR jPOST; Q03519; -.
DR MassIVE; Q03519; -.
DR PaxDb; Q03519; -.
DR PeptideAtlas; Q03519; -.
DR PRIDE; Q03519; -.
DR ProteomicsDB; 58215; -. [Q03519-1]
DR ProteomicsDB; 58216; -. [Q03519-2]
DR ProteomicsDB; 62921; -.
DR TopDownProteomics; Q03519-2; -. [Q03519-2]
DR Antibodypedia; 684; 238 antibodies from 33 providers.
DR CPTC; Q03519; 1 antibody.
DR DNASU; 6891; -.
DR Ensembl; ENST00000374897.4; ENSP00000364032.3; ENSG00000204267.17. [Q03519-1]
DR Ensembl; ENST00000383118.8; ENSP00000372599.4; ENSG00000206235.8. [Q03519-1]
DR Ensembl; ENST00000383119.8; ENSP00000372600.4; ENSG00000206235.8. [Q03519-2]
DR Ensembl; ENST00000383239.8; ENSP00000372726.4; ENSG00000206299.8. [Q03519-1]
DR Ensembl; ENST00000383240.8; ENSP00000372727.4; ENSG00000206299.8. [Q03519-2]
DR Ensembl; ENST00000414145.6; ENSP00000401377.2; ENSG00000228582.9. [Q03519-2]
DR Ensembl; ENST00000419142.6; ENSP00000390013.2; ENSG00000237599.9.
DR Ensembl; ENST00000426977.2; ENSP00000387553.2; ENSG00000232326.9. [Q03519-2]
DR Ensembl; ENST00000439425.6; ENSP00000396156.2; ENSG00000225967.9. [Q03519-2]
DR Ensembl; ENST00000443713.6; ENSP00000394101.2; ENSG00000228582.9. [Q03519-1]
DR Ensembl; ENST00000451907.2; ENSP00000392172.2; ENSG00000223481.9. [Q03519-2]
DR Ensembl; ENST00000652259.1; ENSP00000498827.1; ENSG00000204267.17. [Q03519-2]
DR GeneID; 6891; -.
DR KEGG; hsa:6891; -.
DR MANE-Select; ENST00000374897.4; ENSP00000364032.3; NM_001290043.2; NP_001276972.1.
DR UCSC; uc063yci.1; human. [Q03519-1]
DR CTD; 6891; -.
DR DisGeNET; 6891; -.
DR GeneCards; TAP2; -.
DR HGNC; HGNC:44; TAP2.
DR HPA; ENSG00000204267; Low tissue specificity.
DR MalaCards; TAP2; -.
DR MIM; 170261; gene.
DR MIM; 604571; phenotype.
DR neXtProt; NX_Q03519; -.
DR OpenTargets; ENSG00000204267; -.
DR Orphanet; 34592; Immunodeficiency by defective expression of MHC class I.
DR PharmGKB; PA35022; -.
DR VEuPathDB; HostDB:ENSG00000204267; -.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000160499; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; Q03519; -.
DR OMA; RYFEVMD; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; Q03519; -.
DR TreeFam; TF105197; -.
DR BRENDA; 7.4.2.14; 2681.
DR BRENDA; 7.4.2.5; 2681.
DR PathwayCommons; Q03519; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR SignaLink; Q03519; -.
DR BioGRID-ORCS; 6891; 20 hits in 1082 CRISPR screens.
DR GeneWiki; TAP2; -.
DR GenomeRNAi; 6891; -.
DR Pharos; Q03519; Tbio.
DR PRO; PR:Q03519; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q03519; protein.
DR Bgee; ENSG00000204267; Expressed in vermiform appendix and 96 other tissues.
DR ExpressionAtlas; Q03519; baseline and differential.
DR Genevisible; Q03519; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042824; C:MHC class I peptide loading complex; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0042825; C:TAP complex; IDA:UniProtKB.
DR GO; GO:0015433; F:ABC-type peptide antigen transporter activity; IDA:UniProtKB.
DR GO; GO:0015440; F:ABC-type peptide transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0023029; F:MHC class Ib protein binding; IPI:UniProtKB.
DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB.
DR GO; GO:0046978; F:TAP1 binding; IPI:UniProtKB.
DR GO; GO:0046980; F:tapasin binding; ISS:UniProtKB.
DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IDA:UniProtKB.
DR GO; GO:0002485; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent; IEA:Ensembl.
DR GO; GO:0002489; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent; IMP:UniProtKB.
DR GO; GO:0002481; P:antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent; IEA:Ensembl.
DR GO; GO:0046967; P:cytosol to endoplasmic reticulum transport; IMP:UniProtKB.
DR GO; GO:0046968; P:peptide antigen transport; IDA:UniProtKB.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEA:Ensembl.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR DisProt; DP02210; -.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR013305; ABC_Tap-like.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005293; Tap2/ABCB3.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR PRINTS; PR01897; TAP2PROTEIN.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR00958; 3a01208; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
KW Endoplasmic reticulum; Host-virus interaction; Immunity; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Peptide transport;
KW Protein transport; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..686
FT /note="Antigen peptide transporter 2"
FT /id="PRO_0000093329"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 28..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 78..98
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 120..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 170..187
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 209..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 288..293
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 315..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 396..408
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 430..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 152..435
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 468..686
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 301..389
FT /note="Part of the peptide-binding site"
FT /evidence="ECO:0000269|PubMed:8955196"
FT REGION 414..433
FT /note="Part of the peptide-binding site"
FT /evidence="ECO:0000269|PubMed:8955196"
FT BINDING 503..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT SITE 16
FT /note="Inter-subunit salt bridge with TAPBP"
FT /evidence="ECO:0000269|PubMed:26611325"
FT VAR_SEQ 645..686
FT /note="LQDWNSRGDRTVLVIAHRLQTVQRAHQILVLQEGKLQKLAQL -> KTLWKF
FT MIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9916708"
FT /id="VSP_038904"
FT VARIANT 56
FT /note="R -> K (in dbSNP:rs17220192)"
FT /id="VAR_036873"
FT VARIANT 374
FT /note="A -> T (in allele TAP2*01F, allele TAP2*01G, allele
FT TAP2*01H, allele TAP2*02B and allele TAP2*02D;
FT dbSNP:rs111303994)"
FT /evidence="ECO:0000269|PubMed:11294565,
FT ECO:0000269|PubMed:9672156"
FT /id="VAR_014997"
FT VARIANT 379
FT /note="V -> I (in allele TAP2*01D, allele TAP2*01E, allele
FT TAP2*01G, allele TAP2*02C and allele TAP2*02F;
FT dbSNP:rs1800454)"
FT /evidence="ECO:0000269|PubMed:11294565,
FT ECO:0000269|PubMed:1570316, ECO:0000269|PubMed:9916708"
FT /id="VAR_000094"
FT VARIANT 467
FT /note="V -> I (in allele TAP2*01F and allele TAP2*02D;
FT dbSNP:rs150253319)"
FT /evidence="ECO:0000269|PubMed:11294565,
FT ECO:0000269|PubMed:9672156"
FT /id="VAR_014998"
FT VARIANT 513
FT /note="A -> S (variant of uncertain significance)"
FT /id="VAR_014999"
FT VARIANT 565
FT /note="A -> T (in allele TAP2*01:02, allele TAP2*01D,
FT allele TAP2*02E and allele TAP2*02F; dbSNP:rs2228396)"
FT /evidence="ECO:0000269|PubMed:11294565"
FT /id="VAR_000095"
FT VARIANT 577
FT /note="M -> V (in allele TAP2*BKY2; dbSNP:rs2228391)"
FT /evidence="ECO:0000269|PubMed:9324024"
FT /id="VAR_015000"
FT VARIANT 651
FT /note="R -> C (in allele TAP2*01:03 and allele TAP2*01G;
FT dbSNP:rs4148876)"
FT /evidence="ECO:0000269|PubMed:11294565"
FT /id="VAR_000096"
FT VARIANT 665
FT /note="T -> A (in allele TAP2*02:01, allele TAP2*02B,
FT allele TAP2*02C, allele TAP2*02D, allele TAP2*02E, allele
FT TAP2*02F, allele TAP2*04A and allele TAP2*Bky2;
FT dbSNP:rs241447)"
FT /evidence="ECO:0000269|PubMed:11294565,
FT ECO:0000269|PubMed:1570316"
FT /id="VAR_000097"
FT VARIANT 686
FT /note="L -> LQEGQDLYSRLVQQRLMD (in allele TAP2*02:01,
FT allele TAP2*02B, allele TAP2*02C, allele TAP2*02D, allele
FT TAP2*02E, allele TAP2*02F, allele TAP2*03A and allele
FT TAP2*BKY2)"
FT /id="VAR_000098"
FT MUTAGEN 16
FT /note="D->K: Complete loss of interaction with TAPBP,
FT resulting in impaired PLC assembly and antigen
FT presentation."
FT /evidence="ECO:0000269|PubMed:26611325"
FT MUTAGEN 638
FT /note="D->A: Inactive in peptide transport when associated
FT with 'A-734' of TAP1."
FT /evidence="ECO:0000269|PubMed:25377891"
FT CONFLICT 345
FT /note="F -> I (in Ref. 8; BAD97020)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="Y -> N (in Ref. 8; BAD97020)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="T -> A (in Ref. 8; BAD97020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 75664 MW; E7E4A7F6A2A3B48B CRC64;
MRLPDLRPWT SLLLVDAALL WLLQGPLGTL LPQGLPGLWL EGTLRLGGLW GLLKLRGLLG
FVGTLLLPLC LATPLTVSLR ALVAGASRAP PARVASAPWS WLLVGYGAAG LSWSLWAVLS
PPGAQEKEQD QVNNKVLMWR LLKLSRPDLP LLVAAFFFLV LAVLGETLIP HYSGRVIDIL
GGDFDPHAFA SAIFFMCLFS FGSSLSAGCR GGCFTYTMSR INLRIREQLF SSLLRQDLGF
FQETKTGELN SRLSSDTTLM SNWLPLNANV LLRSLVKVVG LYGFMLSISP RLTLLSLLHM
PFTIAAEKVY NTRHQEVLRE IQDAVARAGQ VVREAVGGLQ TVRSFGAEEH EVCRYKEALE
QCRQLYWRRD LERALYLLVR RVLHLGVQML MLSCGLQQMQ DGELTQGSLL SFMIYQESVG
SYVQTLVYIY GDMLSNVGAA EKVFSYMDRQ PNLPSPGTLA PTTLQGVVKF QDVSFAYPNR
PDRPVLKGLT FTLRPGEVTA LVGPNGSGKS TVAALLQNLY QPTGGQVLLD EKPISQYEHC
YLHSQVVSVG QEPVLFSGSV RNNIAYGLQS CEDDKVMAAA QAAHADDFIQ EMEHGIYTDV
GEKGSQLAAG QKQRLAIARA LVRDPRVLIL DEATSALDVQ CEQALQDWNS RGDRTVLVIA
HRLQTVQRAH QILVLQEGKL QKLAQL
