TOR1A_RAT
ID TOR1A_RAT Reviewed; 333 AA.
AC Q68G38; Q8K3L8;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Torsin-1A;
DE AltName: Full=Dystonia 1 protein;
DE AltName: Full=Torsin ATPase 1;
DE EC=3.6.4.-;
DE Flags: Precursor;
GN Name=Tor1a; Synonyms=Dyt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12007841; DOI=10.1016/s0169-328x(02)00176-6;
RA Ziefer P., Leung J., Razzano T., Shalish C., LeDoux M.S., Lorden J.F.,
RA Ozelius L., Breakefield X.O., Standaert D.G., Augood S.J.;
RT "Molecular cloning and expression of rat torsinA in the normal and
RT genetically dystonic (dt) rat.";
RL Brain Res. Mol. Brain Res. 101:132-135(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=12671990; DOI=10.1002/jnr.10567;
RA Hewett J., Ziefer P., Bergeron D., Naismith T., Boston H., Slater D.,
RA Wilbur J., Schuback D., Kamm C., Smith N., Camp S., Ozelius L.J.,
RA Ramesh V., Hanson P.I., Breakefield X.O.;
RT "TorsinA in PC12 cells: localization in the endoplasmic reticulum and
RT response to stress.";
RL J. Neurosci. Res. 72:158-168(2003).
RN [6]
RP INTERACTION WITH KLC1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RX PubMed=14970196; DOI=10.1074/jbc.m401332200;
RA Kamm C., Boston H., Hewett J., Wilbur J., Corey D.P., Hanson P.I.,
RA Ramesh V., Breakefield X.O.;
RT "The early onset dystonia protein torsinA interacts with kinesin light
RT chain 1.";
RL J. Biol. Chem. 279:19882-19892(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=18167355; DOI=10.1074/jbc.m704097200;
RA Granata A., Watson R., Collinson L.M., Schiavo G., Warner T.T.;
RT "The dystonia-associated protein torsinA modulates synaptic vesicle
RT recycling.";
RL J. Biol. Chem. 283:7568-7579(2008).
RN [8]
RP INTERACTION WITH COPS4; SNAPIN AND STON2, AND SUBCELLULAR LOCATION.
RX PubMed=21102408; DOI=10.1038/emboj.2010.285;
RA Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.;
RT "CSN complex controls the stability of selected synaptic proteins via a
RT torsinA-dependent process.";
RL EMBO J. 30:181-193(2011).
CC -!- FUNCTION: Protein with chaperone functions important for the control of
CC protein folding, processing, stability and localization as well as for
CC the reduction of misfolded protein aggregates. Involved in the
CC regulation of synaptic vesicle recycling, controls STON2 protein
CC stability in collaboration with the COP9 signalosome complex (CSN). In
CC the nucleus, may link the cytoskeleton with the nuclear envelope, this
CC mechanism seems to be crucial for the control of nuclear polarity, cell
CC movement and, specifically in neurons, nuclear envelope integrity.
CC Participates in the cellular trafficking and may regulate the
CC subcellular location of multipass membrane proteins such as the
CC dopamine transporter SLC6A3, leading to the modulation of dopamine
CC neurotransmission. In the endoplasmic reticulum, plays a role in the
CC quality control of protein folding by increasing clearance of misfolded
CC proteins such as SGCE variants or holding them in an intermediate state
CC for proper refolding. May have a redundant function with TOR1B in non-
CC neural tissues (By similarity). {ECO:0000250|UniProtKB:O14656}.
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 TOR1B; the interaction may be
CC specific of neural tissues. Interacts (ATP-bound) with TOR1AIP1 and
CC TOR1AIP2; the interactions induce ATPase activity. Interacts with
CC KLHL14; preferentially when ATP-free. Interacts with KLC1 (via TPR
CC repeats); the interaction associates TOR1A with the kinesin oligomeric
CC complex. Interacts with COPS4; the interaction associates TOR1A with
CC the CSN complex. Interacts with SNAPIN; the interaction is direct and
CC associates SNAPIN with the CSN complex. Interacts with STON2. Interacts
CC (ATP-bound) with SYNE3 (via KASH domain); the interaction is required
CC for SYNE3 nuclear envelope localization. Interacts with VIM; the
CC interaction associates TOR1A with the cytoskeleton. Interacts with
CC PLEC. Interacts (ATP-bound) with SLC6A3; regulates SLC6A3 transport to
CC the plasma membrane. {ECO:0000269|PubMed:14970196,
CC ECO:0000269|PubMed:21102408}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:O14656}. Nucleus inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell projection, growth
CC cone. Cytoplasmic vesicle membrane. Cytoplasmic vesicle, secretory
CC vesicle. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle.
CC Note=Peripherally associated with the inner face of the ER membrane,
CC probably mediated by the interaction with TOR1AIP1. The association
CC with nucleus envelope is mediated by the interaction with TOR1AIP2.
CC Upon oxidative stress, redistributes to protusions from the cell
CC surface.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:14970196}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12671990,
CC ECO:0000269|PubMed:14970196}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000305}.
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DR EMBL; AY054303; AAL05259.1; -; mRNA.
DR EMBL; AABR06022147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474001; EDL93286.1; -; Genomic_DNA.
DR EMBL; BC078714; AAH78714.1; -; mRNA.
DR RefSeq; NP_695215.2; NM_153303.2.
DR AlphaFoldDB; Q68G38; -.
DR SMR; Q68G38; -.
DR BioGRID; 251758; 1.
DR IntAct; Q68G38; 2.
DR MINT; Q68G38; -.
DR STRING; 10116.ENSRNOP00000063691; -.
DR GlyGen; Q68G38; 2 sites.
DR jPOST; Q68G38; -.
DR PaxDb; Q68G38; -.
DR PRIDE; Q68G38; -.
DR Ensembl; ENSRNOT00000064660; ENSRNOP00000063691; ENSRNOG00000006894.
DR GeneID; 266606; -.
DR KEGG; rno:266606; -.
DR UCSC; RGD:628863; rat.
DR CTD; 1861; -.
DR RGD; 628863; Tor1a.
DR eggNOG; KOG2170; Eukaryota.
DR GeneTree; ENSGT00950000182888; -.
DR HOGENOM; CLU_053537_0_0_1; -.
DR InParanoid; Q68G38; -.
DR OMA; RGYETNE; -.
DR OrthoDB; 1453168at2759; -.
DR PhylomeDB; Q68G38; -.
DR TreeFam; TF314941; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:Q68G38; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000006894; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q68G38; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; ISS:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IDA:RGD.
DR GO; GO:0051787; F:misfolded protein binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:InterPro.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISS:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR GO; GO:0071763; P:nuclear membrane organization; ISS:UniProtKB.
DR GO; GO:0006996; P:organelle organization; ISS:UniProtKB.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISS:UniProtKB.
DR GO; GO:0000338; P:protein deneddylation; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; ISS:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; ISS:UniProtKB.
DR GO; GO:0048489; P:synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010448; Torsin.
DR InterPro; IPR030549; Torsin-1A.
DR InterPro; IPR017378; Torsin_1/2.
DR PANTHER; PTHR10760; PTHR10760; 1.
DR PANTHER; PTHR10760:SF15; PTHR10760:SF15; 1.
DR Pfam; PF06309; Torsin; 1.
DR PIRSF; PIRSF038079; Torsin_2A; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasmic vesicle; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Membrane; Nucleus; Reference proteome; Signal; Synapse.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..333
FT /note="Torsin-1A"
FT /id="PRO_0000429276"
FT REGION 92..252
FT /note="Interaction with SNAPIN"
FT /evidence="ECO:0000250"
FT REGION 252..333
FT /note="Interaction with KLC1"
FT /evidence="ECO:0000250"
FT REGION 313..333
FT /note="Interaction with SYNE3"
FT /evidence="ECO:0000250"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT CONFLICT 179
FT /note="G -> S (in Ref. 1; AAL05259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 37949 MW; 8DE5E15F43B67447 CRC64;
MKLGRATLAL LLLVPCVVRA VEPISLGLAL AGVLTGYISY PRLYCLFAEC CGQKRSLSRE
ALQKDLDNKL FGQHLAKRVI LNAVSGFLSN PKPKKPLTLS LHGWTGTGKN FASKIIAENI
YEGGLNSDYV HLFVATLHFP HASNITLYKD QLQMWIRGNV SACARSIFIF DEMDKMHAGL
IDAIKPFLDY YDVVDEVSYQ KAIFIFLSNA GAERITDVAL DFWRSGKQRE EIKLRDMEHA
LAVSVFNNKN SGFWHSSLID RNLIDYFVPF LPLEYKHLKM CIRVEMQSRG YEEDEDIINK
VAEEMTFFPK EEKVFSDKGC KTVFTKLDYY LDD
