TPSN_CANLF
ID TPSN_CANLF Reviewed; 449 AA.
AC Q5TJE4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Tapasin;
DE Short=TPN;
DE Short=TPSN;
DE AltName: Full=TAP-binding protein;
DE Flags: Precursor;
GN Name=TAPBP;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Doberman pinscher;
RX PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009;
RA Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A.,
RA Ollier W.E.R., Binns M.M.;
RT "Genomic sequence of the class II region of the canine MHC: comparison with
RT the MHC of other mammalian species.";
RL Genomics 85:48-59(2005).
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). {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
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; AJ630366; CAI11444.1; -; Genomic_DNA.
DR RefSeq; NP_001041566.1; NM_001048101.2.
DR AlphaFoldDB; Q5TJE4; -.
DR SMR; Q5TJE4; -.
DR STRING; 9612.ENSCAFP00000001381; -.
DR PaxDb; Q5TJE4; -.
DR PRIDE; Q5TJE4; -.
DR Ensembl; ENSCAFT00030023379; ENSCAFP00030020382; ENSCAFG00030012619.
DR Ensembl; ENSCAFT00040039393; ENSCAFP00040034371; ENSCAFG00040021218.
DR Ensembl; ENSCAFT00845037810; ENSCAFP00845029626; ENSCAFG00845021421.
DR GeneID; 481740; -.
DR KEGG; cfa:481740; -.
DR CTD; 6892; -.
DR VEuPathDB; HostDB:ENSCAFG00845021421; -.
DR eggNOG; ENOG502QR0A; Eukaryota.
DR GeneTree; ENSGT00940000159200; -.
DR HOGENOM; CLU_043155_0_0_1; -.
DR InParanoid; Q5TJE4; -.
DR OMA; KVLCWAA; -.
DR OrthoDB; 865957at2759; -.
DR TreeFam; TF334274; -.
DR Proteomes; UP000002254; Chromosome 12.
DR Bgee; ENSCAFG00000000972; Expressed in mucosa of urinary bladder and 47 other tissues.
DR GO; GO:0042824; C:MHC class I peptide loading complex; IBA:GO_Central.
DR GO; GO:0003823; F:antigen binding; IBA:GO_Central.
DR GO; GO:0062061; F:TAP complex binding; IBA:GO_Central.
DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro.
DR GO; GO:0002397; P:MHC class I protein complex assembly; IBA:GO_Central.
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; 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 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..449
FT /note="Tapasin"
FT /id="PRO_0000041838"
FT TOPO_DOM 21..413
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 292..399
FT /note="Ig-like C1-type"
FT SITE 428
FT /note="May be involved in interaction with TAP"
FT /evidence="ECO:0000250"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 115
FT /note="Interchain (with C-57 in PDIA3)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 315..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 449 AA; 47774 MW; A6A661D28ACDA7BB CRC64;
MKPLSLLLAV ASALGTAVSA GPAVIECWMV EDAGGGRLAK KPAALLLRQG PGTPPPRPDL
EPELYLKVHD PAGTLQAAVR RYPSDAPPPH CELSRFIPLP ASARWARGLT PGRSCPRALD
GAWLMASVLS PIFSLSCLLR PQSEPQPEPA LFTSATAVLT VLTYSPIAQI QLGQDALLDL
RFAYMPSISE AAASLAPGPP PFGLEWRRQH LGKGHLLLAA TPGLHEQMPA AQDGAVAFAA
WDDDDPWGPW TGNGTLWLPA VQPFQEGTYL ATVHLPYLQG QVALELSVQK PPKISLTPAP
LVWAAPGEAP PELLCLVSRF YPAKGLEVEW ELRGGPEGSF QKAEGQSWLS ALRHHSDGSV
SLSAHLQPIP VTAKHHGARY ACRVHHPTLP TLGRSAEVTL EVAGLSGPSL EDSVGLFLSA
FLLLGLIKAL GWVAASRSTS KDPKEKKAQ
