TUSC3_MOUSE
ID TUSC3_MOUSE Reviewed; 347 AA.
AC Q8BTV1;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
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 AltName: Full=Protein N33;
DE Flags: Precursor;
GN Name=Tusc3; Synonyms=N33;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK088616; BAC40455.1; -; mRNA.
DR EMBL; AK132766; BAE21346.1; -; mRNA.
DR EMBL; AC168314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC174643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01027656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069898; AAH69898.1; -; mRNA.
DR CCDS; CCDS85529.1; -.
DR RefSeq; NP_084530.3; NM_030254.3.
DR AlphaFoldDB; Q8BTV1; -.
DR SMR; Q8BTV1; -.
DR BioGRID; 219774; 2.
DR STRING; 10090.ENSMUSP00000126080; -.
DR GlyConnect; 2802; 2 N-Linked glycans (1 site).
DR GlyGen; Q8BTV1; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q8BTV1; -.
DR PhosphoSitePlus; Q8BTV1; -.
DR SwissPalm; Q8BTV1; -.
DR MaxQB; Q8BTV1; -.
DR PaxDb; Q8BTV1; -.
DR PeptideAtlas; Q8BTV1; -.
DR PRIDE; Q8BTV1; -.
DR ProteomicsDB; 298031; -.
DR Antibodypedia; 22197; 187 antibodies from 29 providers.
DR DNASU; 80286; -.
DR Ensembl; ENSMUST00000239508; ENSMUSP00000159386; ENSMUSG00000118664.
DR GeneID; 80286; -.
DR KEGG; mmu:80286; -.
DR UCSC; uc009lmf.1; mouse.
DR CTD; 7991; -.
DR MGI; MGI:1933134; Tusc3.
DR VEuPathDB; HostDB:ENSMUSG00000039530; -.
DR eggNOG; KOG2603; Eukaryota.
DR GeneTree; ENSGT00390000012030; -.
DR HOGENOM; CLU_052855_0_0_1; -.
DR InParanoid; Q8BTV1; -.
DR OrthoDB; 1460433at2759; -.
DR PhylomeDB; Q8BTV1; -.
DR TreeFam; TF314850; -.
DR Reactome; R-MMU-5223345; Miscellaneous transport and binding events.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 80286; 0 hits in 53 CRISPR screens.
DR ChiTaRS; Tusc3; mouse.
DR PRO; PR:Q8BTV1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BTV1; protein.
DR ExpressionAtlas; Q8BTV1; baseline and differential.
DR Genevisible; Q8BTV1; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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 1: Evidence at protein 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_0000414923"
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; 39548 MW; A2C6A79FA2A979C9 CRC64;
MSARAAPSRR RQAGRRLRYL PTGSFPFLLL LLLLCIQLGG GQKKKENLLA EKVEQLMEWS
SRRSIFRMNG DKFRKFVKAP PRNYSMIVMF TALQPQRQCS VCRQANEEYQ ILANSWRYSS
AFCNKLFFGM VDYDEGTDVF QQLNMNSAPT FMHFPSKGRP KRADTFDLQR IGFAAEQLAK
WIADRTDVHI RVFRPPNYSG TIALALLVSL VGGLLYLRRN NLEFIYNKTG WAMVSLCIVF
AMTSGQMWNH IRGPPYAHKN PHNGQVSYIH GSSQAQFVAE SHIILVLNAA ITMGMVLLNE
AATSKGDVGK RRIICLVGLG LVVFFFSFLL SIFRSKYHGY PYSFLIK
