ID TOR1B_HUMAN Reviewed; 336 AA.
AC O14657;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 27-MAR-2024, entry version 192.
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; Synonyms=DQ1; ORFNames=FKSG18;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Y.-G., Gong L.;
RT "Cloning of FKSG18, a novel gene located on human chromosome 9.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 71-336.
RC TISSUE=Brain cortex, Fetal brain, and Liver;
RX PubMed=9288096; DOI=10.1038/ng0997-40;
RA Ozelius L.J., Hewett J.W., Page C.E., Bressman S.B., Kramer P.L.,
RA Shalish C., de Leon D., Brin M.F., Raymond D., Corey D.P., Fahn S.,
RA Risch N.J., Buckler A.J., Gusella J.F., Breakefield X.O.;
RT "The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding
RT protein.";
RL Nat. Genet. 17:40-48(1997).
RN [5]
RP INTERACTION WITH TOR1A, TISSUE SPECIFICITY, GLYCOSYLATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15147511; DOI=10.1111/j.1471-4159.2004.02404.x;
RA Hewett J.W., Kamm C., Boston H., Beauchamp R., Naismith T., Ozelius L.,
RA Hanson P.I., Breakefield X.O., Ramesh V.;
RT "TorsinB--perinuclear location and association with torsinA.";
RL J. Neurochem. 89:1186-1194(2004).
RN [6]
RP SUBUNIT, INTERACTION WITH TOR1A, AND MUTAGENESIS OF GLU-178.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION AS ATPASE, AND CATALYTIC ACTIVITY.
RX PubMed=23569223; DOI=10.1073/pnas.1300676110;
RA Zhao C., Brown R.S., Chase A.R., Eisele M.R., Schlieker C.;
RT "Regulation of Torsin ATPases by LAP1 and LULL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1545-1554(2013).
RN [9]
RP FUNCTION IN ENDOPLASMIC RETICULUM INTEGRITY, CATALYTIC ACTIVITY,
RP INTERACTION WITH TOR1AIP2, AND MUTAGENESIS OF GLU-178; 334-ASP--HIS-336 AND
RP PHE-335.
RX PubMed=24275647; DOI=10.1074/jbc.m113.515791;
RA Rose A.E., Zhao C., Turner E.M., Steyer A.M., Schlieker C.;
RT "Arresting a Torsin ATPase reshapes the endoplasmic reticulum.";
RL J. Biol. Chem. 289:552-564(2014).
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:23569223, ECO:0000269|PubMed:24275647}.
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 Evidence={ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:24275647};
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:15147511, ECO:0000269|PubMed:20015956,
CC ECO:0000269|PubMed:24275647}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:15147511}. Nucleus membrane
CC {ECO:0000269|PubMed:15147511}.
CC -!- TISSUE SPECIFICITY: Widely expressed with low levels in brain.
CC {ECO:0000269|PubMed:15147511}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15147511}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000305}.
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DR EMBL; AF317129; AAG50271.1; -; mRNA.
DR EMBL; AL158207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015578; AAH15578.1; -; mRNA.
DR EMBL; AF007872; AAC51733.1; -; mRNA.
DR CCDS; CCDS6929.1; -.
DR RefSeq; NP_001304822.1; NM_001317893.1.
DR RefSeq; NP_001304823.1; NM_001317894.1.
DR RefSeq; NP_055321.1; NM_014506.2.
DR AlphaFoldDB; O14657; -.
DR SMR; O14657; -.
DR BioGRID; 118160; 104.
DR CORUM; O14657; -.
DR DIP; DIP-56930N; -.
DR IntAct; O14657; 18.
DR MINT; O14657; -.
DR STRING; 9606.ENSP00000259339; -.
DR GlyConnect; 1824; 4 N-Linked glycans (1 site).
DR GlyCosmos; O14657; 2 sites, 4 glycans.
DR GlyGen; O14657; 5 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (3 sites).
DR iPTMnet; O14657; -.
DR PhosphoSitePlus; O14657; -.
DR SwissPalm; O14657; -.
DR BioMuta; TOR1B; -.
DR EPD; O14657; -.
DR jPOST; O14657; -.
DR MassIVE; O14657; -.
DR MaxQB; O14657; -.
DR PaxDb; 9606-ENSP00000259339; -.
DR PeptideAtlas; O14657; -.
DR ProteomicsDB; 48154; -.
DR Pumba; O14657; -.
DR Antibodypedia; 17905; 206 antibodies from 21 providers.
DR DNASU; 27348; -.
DR Ensembl; ENST00000259339.7; ENSP00000259339.2; ENSG00000136816.16.
DR GeneID; 27348; -.
DR KEGG; hsa:27348; -.
DR MANE-Select; ENST00000259339.7; ENSP00000259339.2; NM_014506.3; NP_055321.1.
DR UCSC; uc004byk.1; human.
DR AGR; HGNC:11995; -.
DR CTD; 27348; -.
DR DisGeNET; 27348; -.
DR GeneCards; TOR1B; -.
DR HGNC; HGNC:11995; TOR1B.
DR HPA; ENSG00000136816; Low tissue specificity.
DR MIM; 608050; gene.
DR neXtProt; NX_O14657; -.
DR OpenTargets; ENSG00000136816; -.
DR PharmGKB; PA36676; -.
DR VEuPathDB; HostDB:ENSG00000136816; -.
DR eggNOG; KOG2170; Eukaryota.
DR GeneTree; ENSGT00950000182888; -.
DR HOGENOM; CLU_053537_0_0_1; -.
DR InParanoid; O14657; -.
DR OMA; CCDDRSI; -.
DR OrthoDB; 5087at2759; -.
DR PhylomeDB; O14657; -.
DR TreeFam; TF314941; -.
DR PathwayCommons; O14657; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR SignaLink; O14657; -.
DR BioGRID-ORCS; 27348; 13 hits in 1163 CRISPR screens.
DR ChiTaRS; TOR1B; human.
DR GenomeRNAi; 27348; -.
DR Pharos; O14657; Tbio.
DR PRO; PR:O14657; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O14657; Protein.
DR Bgee; ENSG00000136816; Expressed in mucosa of sigmoid colon and 193 other cell types or tissues.
DR ExpressionAtlas; O14657; baseline and differential.
DR Genevisible; O14657; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:MGI.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
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; IDA: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; IDA:UniProtKB.
DR GO; GO:0071763; P:nuclear membrane organization; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; IBA:GO_Central.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049337; TOR1A_C.
DR InterPro; IPR010448; Torsin.
DR InterPro; IPR017378; Torsin_1/2.
DR PANTHER; PTHR10760; TORSIN; 1.
DR PANTHER; PTHR10760:SF14; TORSIN-1B; 1.
DR Pfam; PF21376; TOR1A_C; 1.
DR Pfam; PF06309; Torsin; 1.
DR PIRSF; PIRSF038079; Torsin_2A; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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_0000005509"
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 VARIANT 54
FT /note="A -> T (in dbSNP:rs10988518)"
FT /id="VAR_059220"
FT MUTAGEN 178
FT /note="E->Q: Loss of ATPase activity. Produces sinusoidal
FT endoplasmic reticulum structures where it accumulates.
FT Highly enhances interaction with TOR1AIP2. Localizes in the
FT nuclear envelope."
FT /evidence="ECO:0000269|PubMed:20015956,
FT ECO:0000269|PubMed:24275647"
FT MUTAGEN 334..336
FT /note="DFH->GGG: Highly reduces ATPase activity induced by
FT TOR1AIP2."
FT /evidence="ECO:0000269|PubMed:24275647"
FT MUTAGEN 334..336
FT /note="Missing: Decreases interaction with TOR1AIP2."
FT /evidence="ECO:0000269|PubMed:24275647"
FT MUTAGEN 335
FT /note="F->A: No effect on interaction with TOR1AIP2."
FT /evidence="ECO:0000269|PubMed:24275647"
SQ SEQUENCE 336 AA; 37979 MW; E729360E6468A3FC CRC64;
MLRAGWLRGA AALALLLAAR VVAAFEPITV GLAIGAASAI TGYLSYNDIY CRFAECCREE
RPLNASALKL DLEEKLFGQH LATEVIFKAL TGFRNNKNPK KPLTLSLHGW AGTGKNFVSQ
IVAENLHPKG LKSNFVHLFV STLHFPHEQK IKLYQDQLQK WIRGNVSACA NSVFIFDEMD
KLHPGIIDAI KPFLDYYEQV DGVSYRKAIF IFLSNAGGDL ITKTALDFWR AGRKREDIQL
KDLEPVLSVG VFNNKHSGLW HSGLIDKNLI DYFIPFLPLE YRHVKMCVRA EMRARGSAID
EDIVTRVAEE MTFFPRDEKI YSDKGCKTVQ SRLDFH
//
