ID   TPSNR_PONAB             Reviewed;         468 AA.
AC   Q5R8H1;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   25-MAY-2022, entry version 81.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAH91939.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CR859781; CAH91939.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_001126125.1; NM_001132653.1.
DR   AlphaFoldDB; Q5R8H1; -.
DR   SMR; Q5R8H1; -.
DR   STRING; 9601.ENSPPYP00000004769; -.
DR   GeneID; 100173081; -.
DR   CTD; 55080; -.
DR   eggNOG; ENOG502QSXA; Eukaryota.
DR   InParanoid; Q5R8H1; -.
DR   Proteomes; UP000001595; Unplaced.
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:0002376; P:immune system process; IEA:UniProtKB-KW.
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   2: Evidence at transcript 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..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..468
FT                   /note="Tapasin-related protein"
FT                   /id="PRO_0000014995"
FT   TOPO_DOM        19..405
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        427..468
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          181..297
FT                   /note="Ig-like V-type"
FT   DOMAIN          304..394
FT                   /note="Ig-like C1-type"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        212..283
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        321..382
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   468 AA;  50429 MW;  C9A66CECDE01D43D CRC64;
     MGTQEGWCLL LCLALSGAAE TKPHPAERQW RAADVVLDCF LAKDGGHRAA LASSEDRARA
     SLVLKQVPVL DDGSLEDFTD FQGGTLAQDD PPIIFEASVD LVQIPQAEAL LHADCSGKEV
     TCEISRYFLQ MKGTTVETEA WFMANVQVSG GGPSISMVMK TPRDAKNEAL WHPTLNLPLS
     PQGTVRTAVE FQVMTQTQSL SFLLGSSASL DCGFSMTPGL DLISVEWRLQ HKGRGQLVYS
     WTTGQGQAVR KGATLEPEQL GMARNASLTL PSLTIQDEGT YICQITTSLY RAQQIIQLNI
     QASPKVRLSL ANEALLPTLI CNIAGYYPLD VVVTWTREEL GGSPAQVSGA SFSSLRQSVA
     GTYSISSSLT AEPGSAGATY TCQVMHISLE EPLGASTQVV PPERRTALGV IFASSLFLLA
     LLFLGLQRRQ APTRVGLLQA ERWKTTSCAD TQSSHLHEDR TACVSQPS