TPSN_MOUSE
ID TPSN_MOUSE Reviewed; 465 AA.
AC Q9R233; O70317; Q91YE0; Q91YE1; Q9QWT7; Q9Z1W3;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Tapasin;
DE Short=TPN;
DE Short=TPSN;
DE AltName: Full=TAP-associated protein;
DE AltName: Full=TAP-binding protein;
DE Flags: Precursor;
GN Name=Tapbp; Synonyms=Tapa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Liver;
RX PubMed=10085102; DOI=10.1074/jbc.274.13.8649;
RA Li S., Paulsson K.M., Sjoegren H.-O., Wang P.;
RT "Peptide-bound major histocompatibility complex class I molecules associate
RT with tapasin before dissociation from transporter associated with antigen
RT processing.";
RL J. Biol. Chem. 274:8649-8654(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORMS LONG AND SHORT).
RC STRAIN=129;
RA Rowen L., Qin S., Madan A., Loretz C., Hall J., James R., Dors M.,
RA Shaffer T., Abbasi N., Ratcliffe A., Dickhoff R., Lasky S., Hood L.;
RT "Sequence of the mouse major histocomaptibility locus class II region.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX PubMed=9716645; DOI=10.1007/s002510050430;
RA Grandea A.G. III, Comber P.G., Wenderfer S.E., Schoenhals G., Frueh K.,
RA Monaco J.J., Spies T.;
RT "Sequence, linkage to H2-K, and function of mouse tapasin in MHC class I
RT assembly.";
RL Immunogenetics 48:260-265(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM LONG).
RC STRAIN=C57BL/10;
RX PubMed=12095710; DOI=10.1016/s0165-2478(02)00104-9;
RA Abarca-Heidemann K., Friederichs S., Klamp T., Boehm U., Guethlein L.A.,
RA Ortmann B.;
RT "Regulation of the expression of mouse TAP-associated glycoprotein
RT (tapasin) by cytokines.";
RL Immunol. Lett. 83:197-207(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in the association of MHC class I with transporter
CC associated with antigen processing (TAP) and in the assembly of MHC
CC class I with peptide (peptide loading).
CC -!- SUBUNIT: Interacts with TAP1 and is thus a subunit of the TAP complex.
CC Interaction with TAP1 is TAP2 independent and is required for efficient
CC peptide-TAP interaction. Obligatory mediator for the interaction
CC between newly assembled MHC class I molecules, calreticulin, ERp57 and
CC TAP. Up to 4 MHC class I/tapasin complexes bind to 1 TAP.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9R233-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9R233-2; Sequence=VSP_002578;
CC -!- DOMAIN: The N-terminus is required for efficient association with MHC
CC class I molecule and for a stable interaction between MHC I and
CC calreticulin. Binding to TAP is mediated by the C-terminal region (By
CC similarity). {ECO:0000250}.
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DR EMBL; AF106278; AAD17964.1; -; mRNA.
DR EMBL; AF110520; AAC97973.1; -; Genomic_DNA.
DR EMBL; AF100956; AAC69893.1; -; Genomic_DNA.
DR EMBL; AF043943; AAC61676.1; -; mRNA.
DR EMBL; AJ316612; CAC69993.1; -; Genomic_DNA.
DR EMBL; AJ316613; CAC70721.2; -; mRNA.
DR CCDS; CCDS89072.1; -. [Q9R233-1]
DR RefSeq; NP_033344.1; NM_009318.2. [Q9R233-1]
DR PDB; 6GB7; X-ray; 2.15 A; P/R=34-43.
DR PDBsum; 6GB7; -.
DR AlphaFoldDB; Q9R233; -.
DR SMR; Q9R233; -.
DR BioGRID; 203968; 8.
DR ComplexPortal; CPX-531; Tapasin-ERp57 complex.
DR IntAct; Q9R233; 1.
DR STRING; 10090.ENSMUSP00000025161; -.
DR GlyGen; Q9R233; 1 site.
DR iPTMnet; Q9R233; -.
DR PhosphoSitePlus; Q9R233; -.
DR EPD; Q9R233; -.
DR jPOST; Q9R233; -.
DR MaxQB; Q9R233; -.
DR PaxDb; Q9R233; -.
DR PeptideAtlas; Q9R233; -.
DR PRIDE; Q9R233; -.
DR ProteomicsDB; 259075; -. [Q9R233-1]
DR ProteomicsDB; 259076; -. [Q9R233-2]
DR Antibodypedia; 45647; 205 antibodies from 29 providers.
DR DNASU; 21356; -.
DR Ensembl; ENSMUST00000234247; ENSMUSP00000157315; ENSMUSG00000024308. [Q9R233-1]
DR GeneID; 21356; -.
DR KEGG; mmu:21356; -.
DR UCSC; uc008cae.1; mouse. [Q9R233-1]
DR CTD; 6892; -.
DR MGI; MGI:1201689; Tapbp.
DR VEuPathDB; HostDB:ENSMUSG00000024308; -.
DR eggNOG; ENOG502QR0A; Eukaryota.
DR GeneTree; ENSGT00940000159200; -.
DR InParanoid; Q9R233; -.
DR PhylomeDB; Q9R233; -.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 21356; 21 hits in 76 CRISPR screens.
DR ChiTaRS; Tapbp; mouse.
DR PRO; PR:Q9R233; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9R233; protein.
DR Bgee; ENSMUSG00000024308; Expressed in peripheral lymph node and 251 other tissues.
DR ExpressionAtlas; Q9R233; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0042824; C:MHC class I peptide loading complex; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0061779; C:Tapasin-ERp57 complex; ISO:MGI.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0062061; F:TAP complex binding; ISO:MGI.
DR GO; GO:0046978; F:TAP1 binding; ISO:MGI.
DR GO; GO:0046979; F:TAP2 binding; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0006952; P:defense response; IMP:MGI.
DR GO; GO:0002397; P:MHC class I protein complex assembly; IBA:GO_Central.
DR GO; GO:0002398; P:MHC class Ib protein complex assembly; ISO:MGI.
DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; ISO:MGI.
DR GO; GO:0050823; P:peptide antigen stabilization; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
DR GO; GO:0061635; P:regulation of protein complex stability; ISO:MGI.
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; IPR003006; Ig/MHC_CS.
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.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..465
FT /note="Tapasin"
FT /id="PRO_0000014991"
FT TOPO_DOM 24..416
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 295..402
FT /note="Ig-like C1-type"
FT SITE 431
FT /note="May be involved in interaction with TAP"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 118
FT /note="Interchain (with C-57 in PDIA3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 318..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 407..436
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_002578"
FT CONFLICT 17
FT /note="V -> F (in Ref. 3; AAC61676)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="A -> G (in Ref. 3; AAC61676)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="A -> G (in Ref. 3; AAC61676)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="A -> S (in Ref. 1; AAD17964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 49736 MW; DCADF445A1437C3C CRC64;
MKPLLLLVAV ALGLATVVSV VSAGPEAIEC WFVEDAGGGG LSKKPATLLL RHGPRGPPPR
PDLDPKLYFK VDDPAGMLLA AFRRYPAGAS APHCEMSRFI PFPASAKWAR SLSPEQNCPR
ALDGDWLLVS VSSTLFSLSS LLRPQPEPLR EPVVITMATV VLTVLTHNPA PRVQLGKDAV
LDLRFAYAPS ALEGSPSLDA GPPPFGLEWR RQHRGKGHLL LAATPGLAGR MPPAQEKATA
FAAWDDDEPW GPWTGNGTFW LPAVKPSQEG VYLATVHLPY LQGQVSLELT VHKAPRVSLT
PAPVVWAAPG EAPPELLCLA SHFFPAEGLE VKWELRGGPG GSSRKVEGKT WLSTIRHHSD
GSVSQSGHLQ LPPVTAKQHG VHYVCRVYHS SLPASGRSAD VTLEVAGFSG PSIEDGIGLF
LSAFLLLGLL KVLGWLAAYW TIPEVSKEKA TAASLTIPRN SKKSQ
