TPSNR_MOUSE
ID TPSNR_MOUSE Reviewed; 451 AA.
AC Q8VD31; E9QN33;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Tapasin-related protein;
DE Short=TAPASIN-R;
DE AltName: Full=TAP-binding protein-like;
DE AltName: Full=TAP-binding protein-related protein;
DE Short=TAPBP-R;
DE AltName: Full=Tapasin-like;
DE Flags: Precursor;
GN Name=Tapbpl;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=11920573;
RX DOI=10.1002/1521-4141(200204)32:4<1059::aid-immu1059>3.0.co;2-g;
RA Teng M.S., Stephens R., Du Pasquier L., Freeman T., Lindquist J.A.,
RA Trowsdale J.;
RT "A human TAPBP (TAPASIN)-related gene, TAPBP-R.";
RL Eur. J. Immunol. 32:1059-1068(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
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: Component of the antigen processing and presentation pathway,
CC which binds to MHC class I coupled with beta2-microglobulin/B2M.
CC Association between TAPBPR and MHC class I occurs in the absence of a
CC functional peptide-loading complex (PLC). Expression seems to slow down
CC and down-regulate MHC class I surface expression.
CC {ECO:0000250|UniProtKB:Q9BX59}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BX59};
CC Single-pass type I membrane protein {ECO:0000250}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q9BX59}; Single-pass type I
CC membrane protein {ECO:0000250}. Microsome membrane
CC {ECO:0000250|UniProtKB:Q9BX59}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9BX59}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9BX59}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9BX59}. Note=Mainly found in endoplasmic
CC reticulum but a minority is found on the cell surface.
CC {ECO:0000250|UniProtKB:Q9BX59}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11920573}.
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DR EMBL; AC140324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017613; AAH17613.1; -; mRNA.
DR CCDS; CCDS20547.1; -.
DR RefSeq; NP_663366.2; NM_145391.2.
DR AlphaFoldDB; Q8VD31; -.
DR SMR; Q8VD31; -.
DR BioGRID; 229407; 2.
DR STRING; 10090.ENSMUSP00000047105; -.
DR GlyGen; Q8VD31; 2 sites.
DR iPTMnet; Q8VD31; -.
DR PhosphoSitePlus; Q8VD31; -.
DR EPD; Q8VD31; -.
DR MaxQB; Q8VD31; -.
DR PaxDb; Q8VD31; -.
DR PeptideAtlas; Q8VD31; -.
DR PRIDE; Q8VD31; -.
DR ProteomicsDB; 259074; -.
DR Antibodypedia; 22408; 352 antibodies from 23 providers.
DR Ensembl; ENSMUST00000043422; ENSMUSP00000047105; ENSMUSG00000038213.
DR GeneID; 213233; -.
DR KEGG; mmu:213233; -.
DR UCSC; uc009dua.1; mouse.
DR CTD; 55080; -.
DR MGI; MGI:2384853; Tapbpl.
DR VEuPathDB; HostDB:ENSMUSG00000038213; -.
DR eggNOG; ENOG502QSXA; Eukaryota.
DR GeneTree; ENSGT00940000160453; -.
DR HOGENOM; CLU_033813_0_0_1; -.
DR InParanoid; Q8VD31; -.
DR OMA; DVVVTWI; -.
DR OrthoDB; 1369855at2759; -.
DR PhylomeDB; Q8VD31; -.
DR TreeFam; TF334274; -.
DR BioGRID-ORCS; 213233; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8VD31; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VD31; protein.
DR Bgee; ENSMUSG00000038213; Expressed in lumbar dorsal root ganglion and 147 other tissues.
DR Genevisible; Q8VD31; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0023024; F:MHC class I protein complex binding; ISO:MGI.
DR GO; GO:0002590; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class I; ISO:MGI.
DR GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; ISO:MGI.
DR GO; GO:0050776; P:regulation of immune response; IBA:GO_Central.
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; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Immunity; Immunoglobulin domain; Membrane; Microsome;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..451
FT /note="Tapasin-related protein"
FT /id="PRO_0000014994"
FT TOPO_DOM 21..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 196..301
FT /note="Ig-like V-type"
FT DOMAIN 302..399
FT /note="Ig-like C1-type"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 217..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 326..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 103
FT /note="V -> L (in Ref. 2; AAH17613)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="G -> D (in Ref. 2; AAH17613)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="N -> T (in Ref. 2; AAH17613)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="I -> V (in Ref. 2; AAH17613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 48733 MW; F494E087AB3D4D62 CRC64;
MGLEPSWYLL LCLAVSGAAG TDPPTAPTTA ERQRQPTDII LDCFLVTEDR HRGAFASSGD
RERALLVLKQ VPVLDDGSLE GITDFQGSTE TKQDSPVIFE ASVDLVQIPQ AEALLHADCS
GKAVTCEISK YFLQARQEAT FEKAHWFISN MQVSRGGPSV SMVMKTLRDA EVGAVRHPTL
NLPLSAQGTV KTQVEFQVTS ETQTLNHLLG SSVSLHCSFS MAPGLDLTGV EWRLQHKGSG
QLVYSWKTGQ GQAKRKGATL EPEELLRAGN ASLTLPNLTL KDEGNYICQI STSLYQAQQI
MPLNILAPPK IQLHLANKDP LPSLVCSIAG YYPLDVGVTW IREELGGIPA QVSGASFSSL
RQSTMGTYSI SSTVMADPGP TGATYTCQVA HVSLEEPLTT SMRVLPNPEQ RGTLGVIFAS
IIFLSALLLF LGLHRQQASS SRSTRPMRHS G
