TUSC3_BOVIN
ID TUSC3_BOVIN Reviewed; 347 AA.
AC Q32L57;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Tumor suppressor candidate 3;
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3;
DE Short=Oligosaccharyl transferase subunit TUSC3;
DE AltName: Full=Magnesium uptake/transporter TUSC3;
DE Flags: Precursor;
GN Name=TUSC3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as accessory component of the N-oligosaccharyl
CC transferase (OST) complex which catalyzes the transfer of a high
CC mannose oligosaccharide from a lipid-linked oligosaccharide donor to an
CC asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent
CC polypeptide chains. Involved in N-glycosylation of STT3B-dependent
CC substrates. Specifically required for the glycosylation of a subset of
CC acceptor sites that are near cysteine residues; in this function seems
CC to act redundantly with MAGT1. In its oxidized form proposed to form
CC transient mixed disulfides with a glycoprotein substrate to facilitate
CC access of STT3B to the unmodified acceptor site. Has also
CC oxidoreductase-independent functions in the STT3B-containing OST
CC complex possibly involving substrate recognition.
CC {ECO:0000250|UniProtKB:Q13454}.
CC -!- FUNCTION: Magnesium transporter. {ECO:0000250|UniProtKB:Q13454}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Accessory component of the STT3B-containing form of the
CC oligosaccharyltransferase (OST) complex. OST exists in two different
CC complex forms which contain common core subunits RPN1, RPN2, OST48,
CC OST4, DAD1 and TMEM258, either STT3A or STT3B as catalytic subunits,
CC and form-specific accessory subunits. OST can form stable complexes
CC with the Sec61 complex or with both the Sec61 and TRAP complexes. The
CC association of TUSC3 or MAGT1 with the STT3B-containing complex seems
CC to be mutually exclusvice. {ECO:0000250|UniProtKB:Q13454}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OST3/OST6 family. {ECO:0000305}.
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DR EMBL; BC109753; AAI09754.1; -; mRNA.
DR RefSeq; NP_001074383.1; NM_001080914.2.
DR AlphaFoldDB; Q32L57; -.
DR SMR; Q32L57; -.
DR STRING; 9913.ENSBTAP00000012110; -.
DR PaxDb; Q32L57; -.
DR PRIDE; Q32L57; -.
DR GeneID; 615007; -.
DR KEGG; bta:615007; -.
DR CTD; 7991; -.
DR eggNOG; KOG2603; Eukaryota.
DR InParanoid; Q32L57; -.
DR OrthoDB; 1460433at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:UniProtKB.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0062062; F:oligosaccharyltransferase complex binding; ISS:UniProtKB.
DR GO; GO:0050890; P:cognition; ISS:UniProtKB.
DR GO; GO:0015693; P:magnesium ion transport; ISS:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12692; PTHR12692; 1.
DR Pfam; PF04756; OST3_OST6; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Magnesium; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..347
FT /note="Tumor suppressor candidate 3"
FT /id="PRO_0000245498"
FT TOPO_DOM 42..196
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..276
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..347
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 59..187
FT /note="Thioredoxin"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..102
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 39536 MW; 0DCE9CF408D8859D CRC64;
MGARGAPSRR RQAGRRPRYL PTGSFPFLLL LLLLCIQLGG GQKKKENLLA EKVEQLMEWS
SRRSVFRMNG DKFRKFIKAP PRNYSMIVMF TALQPQRQCS VCRLANEEYQ ILANSWRYSS
AFCNKLFFSK VDYDEGTDIF QQLNINSAPT FMHFPPKGRP KRADTFDLQR IGFGAEQLAK
WIADRTDVHI RVFRPPNYSG TIALALLVSL VGGLLYLRRN NLEFIYNKTG WAMVSLCIVF
AMTSGQMWNH IRGPPYAHKN PHNGQVSYIH GSSQVQFVAE SHIILVLNAA ITMGMDLLNE
AATSKGDVGK RRIICLVGLG LVVFFFSFLL SIFRSKYHGY PYSFLIK
