ID   TPSN_CHLAE              Reviewed;         448 AA.
AC   Q6PZD2;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Tapasin;
DE            Short=TPN;
DE            Short=TPSN;
DE   AltName: Full=TAP-binding protein;
DE   Flags: Precursor;
GN   Name=TAPBP;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15905525; DOI=10.4049/jimmunol.174.11.6839;
RA   York I.A., Grant E.P., Dahl A.M., Rock K.L.;
RT   "A mutant cell with a novel defect in MHC class I quality control.";
RL   J. Immunol. 174:6839-6846(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).
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:0000305};
CC       Single-pass type I membrane protein {ECO:0000305}.
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; AY570382; AAS77386.1; -; mRNA.
DR   AlphaFoldDB; Q6PZD2; -.
DR   SMR; Q6PZD2; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..448
FT                   /note="Tapasin"
FT                   /id="PRO_0000014989"
FT   TOPO_DOM        21..414
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        436..448
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   448 AA;  47972 MW;  981EFCE52F6A9EAD CRC64;
     MKSLSLLLAV ALGLATAVSA GPAVIECWFV EDTSGKGLAK RPGALLLRQG QGEPPPRPDL
     DPELYLNVHD PTGFLQAAFR RYPRDAPAPH CEMSRFVPLP ASANWASGLT PARNCPRALD
     GAWLMVSMSS PVLSLSSLLR PQPEPQQEPV LITMATVVLT VLTHTPAPRV RLGQDALLDL
     SFAYMPPTSE AASSLAAGPP PFGLEWRRQH LGKGHLLLAA TPGLNGQMPA AQEGAVAFAA
     WDDDEPWGPW TGNGTFWLPR VQPFQEGTYL ATIHLPYLQG QVTLELAVYK PPKVSLMPAT
     LAWAAPGEAP PELLCLVSHF YPPGGLEVEW ELRGGPGGRS QKAEGQRWLS ALRHHSDGSV
     SLSGHLQPPP VTTEQHGARY ACRIHHPSLP ASGRSAEVTL EVAGLSGPSL EDSIGLFLSA
     FFLLGLFKAL GWAAVYLSTC KDSKKKAE