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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.
23-MAY-2018, entry version 95.
RecName: Full=Torsin-1A;
AltName: Full=Dystonia 1 protein;
AltName: Full=Torsin ATPase 1;
EC=3.6.4.-;
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.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
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).
[6]
INTERACTION WITH KLC1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
GLYCOSYLATION.
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).
[7]
SUBCELLULAR LOCATION.
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
recycling.";
J. Biol. Chem. 283:7568-7579(2008).
[8]
INTERACTION WITH COPS4; SNAPIN AND STON2, AND SUBCELLULAR LOCATION.
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).
{ECO:0000269|PubMed:14970196}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12671990,
ECO:0000269|PubMed:14970196}.
-!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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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; -.
OMA; KMHAGLI; -.
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; -.
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.
/FTId=PRO_0000429276.
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).
{ECO:0000305}.
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


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CSB-EL024067HU Human torsin family 1, member A (torsin A) (TOR1A) ELISA kit, Species Human, Sample Type serum, plasma 96T
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TOR1A TOR1A Gene torsin family 1, member A (torsin A)


 

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