Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Torsin-1A (Dystonia 1 protein) (Torsin ATPase 1) (EC 3.6.4.-)

 TOR1A_RAT               Reviewed;         333 AA.
Q68G38; Q8K3L8;
11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
12-SEP-2018, entry version 96.
RecName: Full=Torsin-1A;
AltName: Full=Dystonia 1 protein;
AltName: Full=Torsin ATPase 1;
Flags: Precursor;
Name=Tor1a; Synonyms=Dyt1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
PubMed=12007841; DOI=10.1016/S0169-328X(02)00176-6;
Ziefer P., Leung J., Razzano T., Shalish C., LeDoux M.S., Lorden J.F.,
Ozelius L., Breakefield X.O., Standaert D.G., Augood S.J.;
"Molecular cloning and expression of rat torsinA in the normal and
genetically dystonic (dt) rat.";
Brain Res. Mol. Brain Res. 101:132-135(2002).
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
PubMed=12671990; DOI=10.1002/jnr.10567;
Hewett J., Ziefer P., Bergeron D., Naismith T., Boston H., Slater D.,
Wilbur J., Schuback D., Kamm C., Smith N., Camp S., Ozelius L.J.,
Ramesh V., Hanson P.I., Breakefield X.O.;
"TorsinA in PC12 cells: localization in the endoplasmic reticulum and
response to stress.";
J. Neurosci. Res. 72:158-168(2003).
PubMed=14970196; DOI=10.1074/jbc.M401332200;
Kamm C., Boston H., Hewett J., Wilbur J., Corey D.P., Hanson P.I.,
Ramesh V., Breakefield X.O.;
"The early onset dystonia protein torsinA interacts with kinesin light
chain 1.";
J. Biol. Chem. 279:19882-19892(2004).
PubMed=18167355; DOI=10.1074/jbc.M704097200;
Granata A., Watson R., Collinson L.M., Schiavo G., Warner T.T.;
"The dystonia-associated protein torsinA modulates synaptic vesicle
J. Biol. Chem. 283:7568-7579(2008).
PubMed=21102408; DOI=10.1038/emboj.2010.285;
Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.;
"CSN complex controls the stability of selected synaptic proteins via
a torsinA-dependent process.";
EMBO J. 30:181-193(2011).
-!- FUNCTION: Protein with chaperone functions important for the
control of protein folding, processing, stability and localization
as well as for the reduction of misfolded protein aggregates.
Involved in the regulation of synaptic vesicle recycling, controls
STON2 protein stability in collaboration with the COP9 signalosome
complex (CSN). In the nucleus, may link the cytoskeleton with the
nuclear envelope, this mechanism seems to be crucial for the
control of nuclear polarity, cell movement and, specifically in
neurons, nuclear envelope integrity. Participates in the cellular
trafficking and may regulate the subcellular location of multipass
membrane proteins such as the dopamine transporter SLC6A3, leading
to the modulation of dopamine neurotransmission. In the
endoplasmic reticulum, plays a role in the quality control of
protein folding by increasing clearance of misfolded proteins such
as SGCE variants or holding them in an intermediate state for
proper refolding. May have a redundant function with TOR1B in non-
neural tissues (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Homohexamer. Interacts with TOR1B; the interaction may be
specific of neural tissues. Interacts (ATP-bound) with TOR1AIP1
and TOR1AIP2; the interactions induce ATPase activity. Interacts
with KLHL14; preferentially when ATP-free. Interacts with KLC1
(via TPR repeats); the interaction associates TOR1A with the
kinesin oligomeric complex. Interacts with COPS4; the interaction
associates TOR1A with the CSN complex. Interacts with SNAPIN; the
interaction is direct and associates SNAPIN with the CSN complex.
Interacts with STON2. Interacts (ATP-bound) with SYNE3 (via KASH
domain); the interaction is required for SYNE3 nuclear envelope
localization. Interacts with VIM; the interaction associates TOR1A
with the cytoskeleton. Interacts with PLEC. Interacts (ATP-bound)
with SLC6A3; regulates SLC6A3 transport to the plasma membrane.
{ECO:0000269|PubMed:14970196, ECO:0000269|PubMed:21102408}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Nucleus inner
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Cell projection, growth cone. Cytoplasmic vesicle membrane.
Cytoplasmic vesicle, secretory vesicle. Cytoplasmic vesicle,
secretory vesicle, synaptic vesicle. Note=Peripherally associated
with the inner face of the ER membrane, probably mediated by the
interaction with TOR1AIP1. The association with nucleus envelope
is mediated by the interaction with TOR1AIP2. Upon oxidative
stress, redistributes to protusions from the cell surface.
-!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12671990,
-!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AY054303; AAL05259.1; -; mRNA.
EMBL; AABR06022147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474001; EDL93286.1; -; Genomic_DNA.
EMBL; BC078714; AAH78714.1; -; mRNA.
RefSeq; NP_695215.2; NM_153303.2.
UniGene; Rn.20041; -.
ProteinModelPortal; Q68G38; -.
SMR; Q68G38; -.
BioGrid; 251758; 1.
IntAct; Q68G38; 2.
MINT; Q68G38; -.
STRING; 10116.ENSRNOP00000063691; -.
PaxDb; Q68G38; -.
PRIDE; Q68G38; -.
Ensembl; ENSRNOT00000064660; ENSRNOP00000063691; ENSRNOG00000006894.
GeneID; 266606; -.
KEGG; rno:266606; -.
UCSC; RGD:628863; rat.
CTD; 1861; -.
RGD; 628863; Tor1a.
eggNOG; KOG2170; Eukaryota.
eggNOG; ENOG410XR06; LUCA.
GeneTree; ENSGT00390000001920; -.
HOGENOM; HOG000115770; -.
HOVERGEN; HBG054188; -.
InParanoid; Q68G38; -.
OrthoDB; EOG091G0B5F; -.
PhylomeDB; Q68G38; -.
TreeFam; TF314941; -.
Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
PRO; PR:Q68G38; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000006894; Expressed in 10 organ(s), highest expression level in liver.
Genevisible; Q68G38; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:RGD.
GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0019894; F:kinesin binding; IDA:RGD.
GO; GO:0051787; F:misfolded protein binding; IEA:Ensembl.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:InterPro.
GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
GO; GO:0072321; P:chaperone-mediated protein transport; ISS:UniProtKB.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISS:UniProtKB.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
GO; GO:0071763; P:nuclear membrane organization; ISS:UniProtKB.
GO; GO:0006996; P:organelle organization; ISS:UniProtKB.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISS:UniProtKB.
GO; GO:0000338; P:protein deneddylation; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; ISS:UniProtKB.
GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IDA:RGD.
GO; GO:0048489; P:synaptic vesicle transport; ISS:UniProtKB.
GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR010448; Torsin.
InterPro; IPR030549; Torsin-1A.
InterPro; IPR017378; Torsin_1/2.
PANTHER; PTHR10760; PTHR10760; 1.
PANTHER; PTHR10760:SF15; PTHR10760:SF15; 1.
Pfam; PF06309; Torsin; 1.
PIRSF; PIRSF038079; Torsin_2A; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
Cell junction; Cell projection; Complete proteome;
Cytoplasmic vesicle; Endoplasmic reticulum; Glycoprotein; Hydrolase;
Membrane; Nucleus; Reference proteome; Signal; Synapse.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 333 Torsin-1A.
REGION 92 252 Interaction with SNAPIN. {ECO:0000250}.
REGION 252 333 Interaction with KLC1. {ECO:0000250}.
REGION 313 333 Interaction with SYNE3. {ECO:0000250}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
CONFLICT 179 179 G -> S (in Ref. 1; AAL05259).
SEQUENCE 333 AA; 37949 MW; 8DE5E15F43B67447 CRC64;

Related products :

Catalog number Product name Quantity
EIAAB43451 Dystonia 1 protein,Dyt1,Mouse,Mus musculus,Tor1a,Torsin family 1 member A,Torsin-1A
EIAAB43450 DQ2,Dystonia 1 protein,DYT1,Homo sapiens,Human,TOR1A,Torsin family 1 member A,Torsin-1A
EIAAB43454 Homo sapiens,Human,TOR2A,TORP1,Torsin family 2 member A,Torsin-2A,Torsin-related protein 1,UNQ6408_PRO21181
EIAAB43462 Adir,ATP-dependent interferon-responsive protein,Mouse,Mus musculus,Tor3a,Torsin family 3 member A,Torsin-3A
EIAAB43464 ADIR,ATP-dependent interferon-responsive protein,Homo sapiens,Human,TOR3A,Torsin family 3 member A,Torsin-3A
GS-2278a torsin family 1, member A (torsin A) primary antibody, Host: Rabbit 200ul
EIAAB43460 Bos taurus,Bovine,Prosalusin,TOR2A,Torsin family 2 member A,Torsin-2A
EIAAB43461 Prosalusin,Rat,Rattus norvegicus,Tor2a,Torsin family 2 member A,Torsin-2A
EIAAB43459 Mouse,Mus musculus,Prosalusin,Tor2a,Torsin family 2 member A,Torsin-2A
EIAAB43453 Mouse,Mus musculus,Tor1b,Torsin family 1 member B,Torsin-1B
EIAAB43455 Mouse,Mus musculus,Tor2a,Torsin family 2 member A,Torsin-2A
EIAAB43456 Bos taurus,Bovine,TOR2A,Torsin family 2 member A,Torsin-2A
EIAAB43463 Rat,Rattus norvegicus,Tor3a,Torsin family 3 member A,Torsin-3A
EIAAB43457 Rat,Rattus norvegicus,Tor2a,Torsin family 2 member A,Torsin-2A
EIAAB43452 DQ1,FKSG18,Homo sapiens,Human,TOR1B,Torsin family 1 member B,Torsin-1B
201-20-6007 TOR1A{torsin family 1, member A (torsin A)}rabbit.pAb 0.2ml
EIAAB43458 HEMBA1005096,Homo sapiens,Human,Prosalusin,PSEC0218,TOR2A,Torsin family 2 member A,Torsin-2A
CSB-EL024070MO Mouse torsin family 1, member B (torsin B) (TOR1B) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL024067MO Mouse torsin family 1, member A (torsin A) (TOR1A) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL024070HU Human torsin family 1, member B (torsin B) (TOR1B) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL024067HU Human torsin family 1, member A (torsin A) (TOR1A) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-PA024067GA01HU Rabbit anti-human torsin family 1, member A (torsin A) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
CSB-PA024067GA01HU Rabbit anti-human torsin family 1, member A (torsin A) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
TOR1B TOR1B Gene torsin family 1, member B (torsin B)
TOR1A TOR1A Gene torsin family 1, member A (torsin A)


GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur

Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur



9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017


france@gentaur.com | Gentaur

Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123

GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U

spain@gentaur.com | Gentaur

ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636

GENTAUR Poland Sp. z o.o.

ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556


Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur