TPSN_CHICK
ID TPSN_CHICK Reviewed; 430 AA.
AC O73895; O73886; O73887; O93604;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 136.
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=B-TAPBPL;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM LONG).
RX PubMed=3141149; DOI=10.1002/j.1460-2075.1988.tb03132.x;
RA Guillemot F., Billault A., Pourquie O., Behar G., Chausse A.M., Zoorob R.,
RA Kreibich G., Auffray C.;
RT "A molecular map of the chicken major histocompatibility complex: the class
RT II beta genes are closely linked to the class I genes and the nucleolar
RT organizer.";
RL EMBO J. 7:2775-2785(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM LONG).
RA Milne S., Kaufman J., Beck S.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT).
RX PubMed=10079297; DOI=10.1007/s002510050500;
RA Frangoulis B., Park I., Guillemot F., Severac V., Auffray C., Zoorob R.;
RT "Identification of the Tapasin gene in the chicken major histocompatibility
RT complex.";
RL Immunogenetics 49:328-337(1999).
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: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=O73895-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O73895-2; Sequence=VSP_002579;
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; AL023516; CAA18963.1; -; Genomic_DNA.
DR EMBL; AJ004999; CAA06273.1; -; Genomic_DNA.
DR EMBL; AJ005071; CAA06327.1; -; mRNA.
DR EMBL; AJ005072; CAA06328.1; -; mRNA.
DR PIR; T28143; T28143.
DR AlphaFoldDB; O73895; -.
DR SMR; O73895; -.
DR STRING; 9031.ENSGALP00000000202; -.
DR PaxDb; O73895; -.
DR VEuPathDB; HostDB:geneid_417048; -.
DR eggNOG; ENOG502QSXA; Eukaryota.
DR InParanoid; O73895; -.
DR PhylomeDB; O73895; -.
DR PRO; PR:O73895; -.
DR Proteomes; UP000000539; Unplaced.
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: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; 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; 2.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00290; IG_MHC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..430
FT /note="Tapasin"
FT /id="PRO_0000014992"
FT TOPO_DOM 16..399
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 139..273
FT /note="Ig-like C1-type 1"
FT DOMAIN 278..382
FT /note="Ig-like C1-type 2"
FT REGION 61..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 413
FT /note="May be involved in interaction with TAP"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 299..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 161..275
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:10079297"
FT /id="VSP_002579"
FT CONFLICT 222
FT /note="H -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 45456 MW; 2F89F72FFEFFDC59 CRC64;
MAAGLRLLLA GLCWSQFRVE DAASPPPPPA PVRCALLEGV GRGGGLPGGG NARPALLRFG
GDAETPPEPG PEPEVTFNVS DPWGTLTPLG VPPRTPPSCE LNPTNPQTGS DPWSRPLHPD
ARSPPTAGGQ WWVAAVGTPQ YGVTALLQGG MGTEGTITAA VALAVLTHTP TLRARVGSPI
HLHCAFAAPP SSFVLEWRHQ NRGAGRVLLA YDSSTARAPR AHPGAELLLG TRDGDGVTAV
TLRLARPSPG DEGTYICSVF LPHGHTQTVL QLHVFEPPKV TLSPKNLVVA PGTSAELRCH
VSGFYPLDVT VTWQRRAGGS GTSQSPRDTV MDSWTSGHRQ AADGTYSRTA AARLIPARPQ
HHGDIYSCVV THTALAKPMR VSVRLLLAGT EGPHLEDITG LFLVAFVLCG LIRWLYPKAA
RPKEETKKSQ
