TOR1B_MOUSE
ID TOR1B_MOUSE Reviewed; 336 AA.
AC Q9ER41; Q8VEI4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Torsin-1B;
DE AltName: Full=Torsin ATPase-1B;
DE EC=3.6.4.-;
DE AltName: Full=Torsin family 1 member B;
DE Flags: Precursor;
GN Name=Tor1b;
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 [MRNA].
RC TISSUE=Brain;
RA Kuner R., Teismann P., Trutzel A., Naim J., Richter A., Bach A., Ferger B.,
RA Schneider A.;
RT "Characterization of the mouse torsinA gene.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Lung, Pancreas, Spleen, and 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).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=20015956; DOI=10.1093/hmg/ddp557;
RA Jungwirth M., Dear M.L., Brown P., Holbrook K., Goodchild R.;
RT "Relative tissue expression of homologous torsinB correlates with the
RT neuronal specific importance of DYT1 dystonia-associated torsinA.";
RL Hum. Mol. Genet. 19:888-900(2010).
RN [8]
RP FUNCTION IN NUCLEAR ENVELOPE INTEGRITY, DEVELOPMENTAL STAGE, INTERACTION
RP WITH TOR1AIP1, AND SUBCELLULAR LOCATION.
RX PubMed=20457914; DOI=10.1073/pnas.0912877107;
RA Kim C.E., Perez A., Perkins G., Ellisman M.H., Dauer W.T.;
RT "A molecular mechanism underlying the neural-specific defect in torsinA
RT mutant mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9861-9866(2010).
CC -!- FUNCTION: May serve as a molecular chaperone assisting in the proper
CC folding of secreted and/or membrane proteins. Plays a role in non-
CC neural cells nuclear envelope and endoplasmic reticulum integrity. May
CC have a redundant function with TOR1A in non-neural tissues.
CC {ECO:0000269|PubMed:20457914}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBUNIT: Homohexamer. Interacts with TOR1A; the interaction may be
CC specific of neural tissues. Interacts with TOR1AIP1; TOR1AIP1 is
CC required for TOR1B location on the nuclear membrane. Interacts (ATP-
CC bound) with TOR1AIP2; important for endoplasmic reticulum integrity.
CC {ECO:0000269|PubMed:20457914}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Nucleus membrane.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and muscle; lower
CC expression levels are observed in brain (at protein level).
CC {ECO:0000269|PubMed:20015956}.
CC -!- DEVELOPMENTAL STAGE: At 16 dpc and 18 dpc, widely expressed with higher
CC expression levels in non-neural cells and hippocampus (at protein
CC level). {ECO:0000269|PubMed:20015956, ECO:0000269|PubMed:20457914}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20015956}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {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; AJ297743; CAC12814.1; -; mRNA.
DR EMBL; AK149754; BAE29062.1; -; mRNA.
DR EMBL; AK159843; BAE35421.1; -; mRNA.
DR EMBL; AL844532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08496.1; -; Genomic_DNA.
DR EMBL; BC018456; AAH18456.1; -; mRNA.
DR CCDS; CCDS15890.1; -.
DR RefSeq; NP_598434.2; NM_133673.3.
DR AlphaFoldDB; Q9ER41; -.
DR SMR; Q9ER41; -.
DR BioGRID; 206011; 1.
DR STRING; 10090.ENSMUSP00000028199; -.
DR GlyConnect; 2774; 4 N-Linked glycans (1 site).
DR GlyGen; Q9ER41; 2 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q9ER41; -.
DR PhosphoSitePlus; Q9ER41; -.
DR EPD; Q9ER41; -.
DR MaxQB; Q9ER41; -.
DR PaxDb; Q9ER41; -.
DR PeptideAtlas; Q9ER41; -.
DR PRIDE; Q9ER41; -.
DR ProteomicsDB; 258953; -.
DR Antibodypedia; 17905; 187 antibodies from 21 providers.
DR DNASU; 30934; -.
DR Ensembl; ENSMUST00000028199; ENSMUSP00000028199; ENSMUSG00000026848.
DR GeneID; 30934; -.
DR KEGG; mmu:30934; -.
DR UCSC; uc008jda.1; mouse.
DR CTD; 27348; -.
DR MGI; MGI:1353605; Tor1b.
DR VEuPathDB; HostDB:ENSMUSG00000026848; -.
DR eggNOG; KOG2170; Eukaryota.
DR GeneTree; ENSGT00950000182888; -.
DR HOGENOM; CLU_053537_0_0_1; -.
DR InParanoid; Q9ER41; -.
DR OMA; SHPRFYC; -.
DR OrthoDB; 1453168at2759; -.
DR PhylomeDB; Q9ER41; -.
DR TreeFam; TF314941; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR BioGRID-ORCS; 30934; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Tor1b; mouse.
DR PRO; PR:Q9ER41; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ER41; protein.
DR Bgee; ENSMUSG00000026848; Expressed in rostral migratory stream and 260 other tissues.
DR ExpressionAtlas; Q9ER41; baseline and differential.
DR Genevisible; Q9ER41; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:InterPro.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:0071763; P:nuclear membrane organization; IGI:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010448; Torsin.
DR InterPro; IPR030550; Torsin-1B.
DR InterPro; IPR017378; Torsin_1/2.
DR PANTHER; PTHR10760; PTHR10760; 1.
DR PANTHER; PTHR10760:SF14; PTHR10760:SF14; 1.
DR Pfam; PF06309; Torsin; 1.
DR PIRSF; PIRSF038079; Torsin_2A; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Membrane; Nucleotide-binding; Nucleus; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..336
FT /note="Torsin-1B"
FT /id="PRO_0000005510"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CONFLICT 238
FT /note="I -> D (in Ref. 1; CAC12814)"
FT /evidence="ECO:0000305"
FT CONFLICT 243..245
FT /note="LEP -> MEH (in Ref. 1; CAC12814)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 37818 MW; 1BC3EA2364AF3BE4 CRC64;
MRRIGAFGGS TALWALLAAH VAGAFEPVSV GIAIGAVSAL TGYLSYTDFY CRFTECCHEE
RPLNTSALKL DLEEKLFGQH LATEVILKAL TGFRNNKNSK KPLTLSLHGW AGTGKNFISQ
IVAENLYPKG LKSNFVHLFV STLHFPHEQK IKVYQDQLQK WIRGNVSACG SSVFIFDEMD
KLHPGIIDAI KPFLDYYEQV DGISYRRAIF IFLSNAGGDL ITKTALDFWR AGRKREEIQL
KDLEPVLSVG VFNNKHSGLW HSGLIDKNLI DYFIPFLPLE YKHVKMCVRA EMRARGAAVD
EDVVTSVADE MTFFPKDEKI YSDKGCKTVQ SRLDFH
