ID TPSN_HUMAN Reviewed; 448 AA. AC O15533; A2AB91; A2ABC0; B0V003; B0V0A6; B2ZUA4; E9PGM2; O15210; AC O15272; Q5STJ8; Q5STK6; Q5STQ5; Q5STQ6; Q66K65; Q96KK7; Q9HAN8; AC Q9UEE0; Q9UEE4; Q9UIZ6; Q9Y6K2; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 13-FEB-2019, entry version 186. DE RecName: Full=Tapasin {ECO:0000303|PubMed:12582157}; DE Short=TPN; DE Short=TPSN; DE AltName: Full=NGS-17; DE AltName: Full=TAP-associated protein; DE AltName: Full=TAP-binding protein; DE Flags: Precursor; GN Name=TAPBP {ECO:0000312|HGNC:HGNC:11566}; Synonyms=NGS17, TAPA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Lymphoblast; RX PubMed=9238042; DOI=10.1073/pnas.94.16.8708; RA Li S., Sjoegren H.-O., Hellman U., Pettersson R.F., Wang P.; RT "Cloning and functional characterization of a subunit of the RT transporter associated with antigen processing."; RL Proc. Natl. Acad. Sci. U.S.A. 94:8708-8713(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=B-cell; RX PubMed=9271576; DOI=10.1126/science.277.5330.1306; RA Ortmann B., Copeman J., Lehner P.J., Sadasivan B., Herberg J.A., RA Grandea A.G., Riddell S.R., Tampe R., Spies T., Trowsdale J., RA Cresswell P.; RT "A critical role for tapasin in the assembly and function of RT multimeric MHC class I-TAP complexes."; RL Science 277:1306-1309(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9521053; RX DOI=10.1002/(SICI)1521-4141(199802)28:02<459::AID-IMMU459>3.0.CO;2-Z; RA Herberg J.A., Sgouros J., Jones T., Copeman J., Humphray S.J., RA Sheer D., Cresswell P., Beck S., Trowsdale J.; RT "Genomic analysis of the Tapasin gene, located close to the TAP loci RT in the MHC."; RL Eur. J. Immunol. 28:459-467(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9545376; DOI=10.1006/jmbi.1998.1637; RA Herberg J.A., Beck S., Trowsdale J.; RT "TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a RT dense cluster at the centromeric end of the MHC."; RL J. Mol. Biol. 277:839-857(1998). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), POLYMORPHISM, RP AND VARIANT THR-260. RC TISSUE=Lymphocyte; RX PubMed=9802609; DOI=10.1111/j.1399-0039.1998.tb03044.x; RA Furukawa H., Kashiwase K., Yabe T., Ishikawa Y., Akaza T., RA Tadokoro K., Tohma S., Inoue T., Tokunaga K., Yamamoto K., Juji T.; RT "Polymorphism of TAPASIN and its linkage disequilibria with HLA class RT II genes in the Japanese population."; RL Tissue Antigens 52:279-281(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Neutrophil; RX PubMed=10088603; RA El Ouakfaoui S., Heitz D., Paquin R., Beaulieu A.D.; RT "Granulocyte-macrophage colony-stimulating factor modulates tapasin RT expression in human neutrophils."; RL J. Leukoc. Biol. 65:205-210(1999). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=B-cell; RX PubMed=14668790; DOI=10.1038/sj.gene.6364043; RA Gao B., Williams A., Sewell A., Elliott T.; RT "Generation of a functional, soluble tapasin protein from an RT alternatively spliced mRNA."; RL Genes Immun. 5:101-108(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND ALTERNATIVE SPLICING. RC TISSUE=Melanoma; RX PubMed=20600451; DOI=10.1016/j.humimm.2010.05.019; RA Belicha-Villanueva A., Golding M., McEvoy S., Sarvaiya N., RA Cresswell P., Gollnick S.O., Bangia N.; RT "Identification of an alternate splice form of tapasin in human RT melanoma."; RL Hum. Immunol. 71:1018-1026(2010). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-260. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-260. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Prostate; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP MUTAGENESIS, AND DOMAIN CHARACTERIZATION. RX PubMed=10382748; RX DOI=10.1002/(SICI)1521-4141(199906)29:06<1858::AID-IMMU1858>3.0.CO;2-C; RA Bangia N., Lehner P.J., Hughes E.A., Surman M., Cresswell P.; RT "The N-terminal region of tapasin is required to stabilize the MHC RT class I loading complex."; RL Eur. J. Immunol. 29:1858-1870(1999). RN [13] RP FUNCTION. RX PubMed=10636848; DOI=10.1074/jbc.275.3.1581; RA Li S., Paulsson K.M., Chen S., Sjoegren H.-O., Wang P.; RT "Tapasin is required for efficient peptide binding to transporter RT associated with antigen processing."; RL J. Biol. Chem. 275:1581-1586(2000). RN [14] RP FUNCTION. RX PubMed=12582157; DOI=10.1074/jbc.M212882200; RA Park B., Ahn K.; RT "An essential function of tapasin in quality control of HLA-G RT molecules."; RL J. Biol. Chem. 278:14337-14345(2003). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253. 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 RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [16] 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., RA Buerckstuemmer T., 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 [17] RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-20, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-401 IN COMPLEX WITH PDIA3, RP SUBUNIT, INTERACTION WITH PDIA3, GLYCOSYLATION AT ASN-253, AND RP DISULFIDE BONDS. RX PubMed=19119025; DOI=10.1016/j.immuni.2008.10.018; RA Dong G., Wearsch P.A., Peaper D.R., Cresswell P., Reinisch K.M.; RT "Insights into MHC class I peptide loading from the structure of the RT tapasin-ERp57 thiol oxidoreductase heterodimer."; RL Immunity 30:21-32(2009). RN [19] RP INVOLVEMENT IN BLS1. RX PubMed=12149238; DOI=10.1182/blood-2001-12-0252; RA Yabe T., Kawamura S., Sato M., Kashiwase K., Tanaka H., Ishikawa Y., RA Asao Y., Oyama J., Tsuruta K., Tokunaga K., Tadokoro K., Juji T.; RT "A subject with a novel type I bare lymphocyte syndrome has tapasin RT deficiency due to deletion of 4 exons by Alu-mediated recombination."; RL Blood 100:1496-1498(2002). CC -!- FUNCTION: Involved in the association of MHC class I with CC transporter associated with antigen processing (TAP) and in the CC assembly of MHC class I with peptide (peptide loading). CC {ECO:0000269|PubMed:10636848, ECO:0000269|PubMed:12582157}. CC -!- SUBUNIT: Heterodimer with PDIA3; disulfide-linked. Interacts with CC TAP1 and is thus a subunit of the TAP complex, also known as the CC peptide loading complex (PLC). Interaction with TAP1 is TAP2- CC independent and is required for efficient peptide-TAP interaction. CC Obligatory mediator for the interaction between newly assembled CC MHC class I molecules, calreticulin, PDIA3 and TAP. Up to 4 MHC CC class I/tapasin complexes bind to 1 TAP. Interacts with HLA-G-B2M CC complex; this interaction is required for loading of high affinity CC peptides and translocation to the cell surface. CC {ECO:0000269|PubMed:12582157, ECO:0000269|PubMed:19119025}. CC -!- INTERACTION: CC P0C739:BNLF2a (xeno); NbExp=6; IntAct=EBI-874801, EBI-9346744; CC Q77CE4:gN (xeno); NbExp=2; IntAct=EBI-874801, EBI-11303846; CC P01892:HLA-A; NbExp=10; IntAct=EBI-874801, EBI-2839473; CC Q03518:TAP1; NbExp=14; IntAct=EBI-874801, EBI-747259; CC Q03519:TAP2; NbExp=8; IntAct=EBI-874801, EBI-780781; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=O15533-1; Sequence=Displayed; CC Name=2; CC IsoId=O15533-2; Sequence=VSP_002577; CC Note=Due to a partial intron retention.; CC Name=3; CC IsoId=O15533-3; Sequence=VSP_017055; CC Note=No experimental confirmation available.; CC Name=4; Synonyms=tpsnDeltaEx3; CC IsoId=O15533-4; Sequence=VSP_044455; CC -!- TISSUE SPECIFICITY: Neutrophils, mostly in fully differentiated CC cells. CC -!- DOMAIN: The N-terminus is required for efficient association with CC MHC class I molecule and for a stable interaction between MHC I CC and calreticulin. Binding to TAP is mediated by the C-terminal CC region. {ECO:0000269|PubMed:10382748}. CC -!- POLYMORPHISM: The 2 alleles of TAPBP; TAPBP*01 (Tapasin*01) (shown CC here) and TAPBP*02 (Tapasin*02); are in linkage disequilibria with CC the HLA-DRB1 locus in a Japanese population. CC {ECO:0000269|PubMed:9802609}. CC -!- DISEASE: Bare lymphocyte syndrome 1 (BLS1) [MIM:604571]: A HLA CC class I deficiency. Contrary to bare lymphocyte syndromes type 2 CC and type 3, which are characterized by early-onset severe combined CC immunodeficiency, class I antigen deficiencies are not accompanied CC by particular pathologic manifestations during the first years of CC life. Systemic infections have not been described. Chronic CC bacterial infections, often beginning in the first decade of life, CC are restricted to the respiratory tract. CC {ECO:0000269|PubMed:12149238}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAD32924.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=TAPBPbase; Note=TAPBP mutation db; CC URL="http://structure.bmc.lu.se/idbase/TAPBPbase/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; Y13582; CAA73909.1; -; mRNA. DR EMBL; AF009510; AAC20076.1; -; mRNA. DR EMBL; AB010639; BAA28757.1; -; mRNA. DR EMBL; AB012622; BAA28758.1; -; Genomic_DNA. DR EMBL; AB012920; BAA28759.1; -; Genomic_DNA. DR EMBL; AF029750; AAB82949.1; -; mRNA. DR EMBL; AF067286; AAD32924.2; ALT_SEQ; mRNA. DR EMBL; AF314222; AAG33061.1; -; mRNA. DR EMBL; EU693375; ACD68200.1; -; mRNA. DR EMBL; AL662820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662827; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX248088; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759786; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z97183; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z97184; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03717.1; -; Genomic_DNA. DR EMBL; BC080574; AAH80574.1; -; mRNA. DR CCDS; CCDS34426.1; -. [O15533-1] DR CCDS; CCDS34427.2; -. [O15533-4] DR CCDS; CCDS34428.2; -. [O15533-3] DR RefSeq; NP_003181.3; NM_003190.4. DR RefSeq; NP_757345.2; NM_172208.2. DR RefSeq; NP_757346.2; NM_172209.2. DR UniGene; Hs.370937; -. DR PDB; 3F8U; X-ray; 2.60 A; B/D=1-401. DR PDB; 6ENY; EM; 5.80 A; C=21-448. DR PDBsum; 3F8U; -. DR PDBsum; 6ENY; -. DR ProteinModelPortal; O15533; -. DR SMR; O15533; -. DR BioGrid; 112755; 18. DR ComplexPortal; CPX-2375; Tapasin-ERp57 complex. DR IntAct; O15533; 14. DR MINT; O15533; -. DR STRING; 9606.ENSP00000404833; -. DR GlyConnect; 1784; -. DR iPTMnet; O15533; -. DR PhosphoSitePlus; O15533; -. DR BioMuta; TAPBP; -. DR EPD; O15533; -. DR jPOST; O15533; -. DR MaxQB; O15533; -. DR PaxDb; O15533; -. DR PeptideAtlas; O15533; -. DR PRIDE; O15533; -. DR ProteomicsDB; 48740; -. DR ProteomicsDB; 48741; -. [O15533-2] DR ProteomicsDB; 48742; -. [O15533-3] DR TopDownProteomics; O15533-3; -. [O15533-3] DR DNASU; 6892; -. DR Ensembl; ENST00000374572; ENSP00000363700; ENSG00000112493. [O15533-1] DR Ensembl; ENST00000383066; ENSP00000372543; ENSG00000206208. DR Ensembl; ENST00000383197; ENSP00000372684; ENSG00000206281. [O15533-3] DR Ensembl; ENST00000383198; ENSP00000372685; ENSG00000206281. [O15533-1] DR Ensembl; ENST00000395114; ENSP00000378546; ENSG00000112493. [O15533-3] DR Ensembl; ENST00000417059; ENSP00000402087; ENSG00000236490. [O15533-1] DR Ensembl; ENST00000434618; ENSP00000395701; ENSG00000231925. DR Ensembl; ENST00000456807; ENSP00000407195; ENSG00000236490. [O15533-3] DR GeneID; 6892; -. DR KEGG; hsa:6892; -. DR UCSC; uc003odx.3; human. [O15533-1] DR CTD; 6892; -. DR DisGeNET; 6892; -. DR EuPathDB; HostDB:ENSG00000231925.11; -. DR GeneCards; TAPBP; -. DR H-InvDB; HIX0058157; -. DR H-InvDB; HIX0166135; -. DR H-InvDB; HIX0166410; -. DR HGNC; HGNC:11566; TAPBP. DR HPA; HPA007066; -. DR MalaCards; TAPBP; -. DR MIM; 601962; gene. DR MIM; 604571; phenotype. DR neXtProt; NX_O15533; -. DR Orphanet; 34592; Immunodeficiency by defective expression of HLA class 1. DR PharmGKB; PA36331; -. DR eggNOG; ENOG410II43; Eukaryota. DR eggNOG; ENOG4111QPK; LUCA. DR HOVERGEN; HBG005156; -. DR InParanoid; O15533; -. DR KO; K08058; -. DR OrthoDB; 865957at2759; -. DR PhylomeDB; O15533; -. DR TreeFam; TF334274; -. 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 ChiTaRS; TAPBP; human. DR EvolutionaryTrace; O15533; -. DR GeneWiki; Tapasin; -. DR GenomeRNAi; 6892; -. DR PRO; PR:O15533; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000231925; Expressed in 222 organ(s), highest expression level in islet of Langerhans. DR ExpressionAtlas; O15533; baseline and differential. DR Genevisible; O15533; HS. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc. DR GO; GO:0042824; C:MHC class I peptide loading complex; IDA:UniProtKB. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0042288; F:MHC class I protein binding; TAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; TAS:UniProtKB. DR GO; GO:0015433; F:peptide antigen-transporting ATPase activity; TAS:ProtInc. DR GO; GO:0062061; F:TAP complex binding; IDA:UniProtKB. DR GO; GO:0046978; F:TAP1 binding; IPI:UniProtKB. DR GO; GO:0046979; F:TAP2 binding; IPI:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; TAS:UniProtKB. DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0002398; P:MHC class Ib protein complex assembly; IMP:UniProtKB. DR GO; GO:0050823; P:peptide antigen stabilization; ISS:UniProtKB. DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; IMP:AgBase. DR GO; GO:0061635; P:regulation of protein complex stability; IDA:AgBase. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; NAS:UniProtKB. DR GO; GO:1990668; P:vesicle fusion with endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 3. 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; IPR008056; Tapasin. DR Pfam; PF07654; C1-set; 1. DR PRINTS; PR01669; TAPASIN. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 20 {ECO:0000244|PubMed:25944712}. FT CHAIN 21 448 Tapasin. FT /FTId=PRO_0000014990. FT TOPO_DOM 21 414 Lumenal. {ECO:0000255}. FT TRANSMEM 415 435 Helical. {ECO:0000255}. FT TOPO_DOM 436 448 Cytoplasmic. {ECO:0000255}. FT DOMAIN 292 399 Ig-like C1-type. FT SITE 428 428 May be involved in interaction with TAP. FT CARBOHYD 253 253 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19119025, FT ECO:0000269|PubMed:19159218}. FT DISULFID 27 91 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:19119025}. FT DISULFID 115 115 Interchain (with C-57 in PDIA3). FT {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:19119025}. FT DISULFID 315 382 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:19119025}. FT VAR_SEQ 70 156 Missing (in isoform 4). FT {ECO:0000303|PubMed:20600451}. FT /FTId=VSP_044455. FT VAR_SEQ 405 448 LSGPSLEDSVGLFLSAFLLLGLFKALGWAAVYLSTCKDSKK FT KAE -> KSWELCGI (in isoform 2). FT {ECO:0000303|PubMed:14668790}. FT /FTId=VSP_002577. FT VAR_SEQ 446 448 KAE -> VQCSTSLYLSLVTLSPHPISKPMEGGCWCGRQNL FT GLEFTLIWVKTWHYILTVGLFEHAT (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_017055. FT VARIANT 260 260 R -> T (in allele TAPBP*02; FT dbSNP:rs2071888). FT {ECO:0000269|PubMed:14574404, FT ECO:0000269|PubMed:9802609, FT ECO:0000269|Ref.10}. FT /FTId=VAR_010253. FT CONFLICT 274 274 H -> Y (in Ref. 11; AAH80574). FT {ECO:0000305}. FT CONFLICT 296 296 L -> P (in Ref. 8; ACD68200). FT {ECO:0000305}. FT CONFLICT 412 412 D -> N (in Ref. 7; AAD32924). FT {ECO:0000305}. FT STRAND 23 29 {ECO:0000244|PDB:3F8U}. FT STRAND 41 46 {ECO:0000244|PDB:3F8U}. FT STRAND 65 69 {ECO:0000244|PDB:3F8U}. FT HELIX 74 81 {ECO:0000244|PDB:3F8U}. FT STRAND 90 96 {ECO:0000244|PDB:3F8U}. FT HELIX 104 109 {ECO:0000244|PDB:3F8U}. FT STRAND 112 116 {ECO:0000244|PDB:3F8U}. FT HELIX 117 119 {ECO:0000244|PDB:3F8U}. FT STRAND 123 129 {ECO:0000244|PDB:3F8U}. FT STRAND 134 141 {ECO:0000244|PDB:3F8U}. FT STRAND 148 150 {ECO:0000244|PDB:3F8U}. FT STRAND 153 164 {ECO:0000244|PDB:3F8U}. FT STRAND 169 171 {ECO:0000244|PDB:3F8U}. FT STRAND 176 178 {ECO:0000244|PDB:3F8U}. FT STRAND 181 184 {ECO:0000244|PDB:3F8U}. FT STRAND 203 210 {ECO:0000244|PDB:3F8U}. FT STRAND 213 220 {ECO:0000244|PDB:3F8U}. FT STRAND 236 242 {ECO:0000244|PDB:3F8U}. FT STRAND 250 258 {ECO:0000244|PDB:3F8U}. FT HELIX 263 265 {ECO:0000244|PDB:3F8U}. FT STRAND 267 275 {ECO:0000244|PDB:3F8U}. FT STRAND 278 290 {ECO:0000244|PDB:3F8U}. FT STRAND 293 300 {ECO:0000244|PDB:3F8U}. FT STRAND 313 323 {ECO:0000244|PDB:3F8U}. FT STRAND 327 337 {ECO:0000244|PDB:3F8U}. FT STRAND 345 349 {ECO:0000244|PDB:3F8U}. FT STRAND 360 367 {ECO:0000244|PDB:3F8U}. FT HELIX 373 375 {ECO:0000244|PDB:3F8U}. FT STRAND 379 385 {ECO:0000244|PDB:3F8U}. FT STRAND 394 399 {ECO:0000244|PDB:3F8U}. SQ SEQUENCE 448 AA; 47626 MW; 7340549519B288AD CRC64; MKSLSLLLAV ALGLATAVSA GPAVIECWFV EDASGKGLAK RPGALLLRQG PGEPPPRPDL DPELYLSVHD PAGALQAAFR RYPRGAPAPH CEMSRFVPLP ASAKWASGLT PAQNCPRALD GAWLMVSISS PVLSLSSLLR PQPEPQQEPV LITMATVVLT VLTHTPAPRV RLGQDALLDL SFAYMPPTSE AASSLAPGPP PFGLEWRRQH LGKGHLLLAA TPGLNGQMPA AQEGAVAFAA WDDDEPWGPW TGNGTFWLPR VQPFQEGTYL ATIHLPYLQG QVTLELAVYK PPKVSLMPAT LARAAPGEAP PELLCLVSHF YPSGGLEVEW ELRGGPGGRS QKAEGQRWLS ALRHHSDGSV SLSGHLQPPP VTTEQHGARY ACRIHHPSLP ASGRSAEVTL EVAGLSGPSL EDSVGLFLSA FLLLGLFKAL GWAAVYLSTC KDSKKKAE //