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

 TOR1A_HUMAN             Reviewed;         332 AA.
O14656; B2RB58; Q53Y64; Q96CA0;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 169.
RecName: Full=Torsin-1A;
AltName: Full=Dystonia 1 protein;
AltName: Full=Torsin ATPase-1A;
EC=3.6.4.-;
AltName: Full=Torsin family 1 member A;
Flags: Precursor;
Name=TOR1A; Synonyms=DQ2, DYT1, TA, TORA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT DYT1 GLU-303 DEL, AND
VARIANT HIS-264.
TISSUE=Brain cortex, Hippocampus, and Substantia nigra;
PubMed=9288096; DOI=10.1038/ng0997-40;
Ozelius L.J., Hewett J.W., Page C.E., Bressman S.B., Kramer P.L.,
Shalish C., de Leon D., Brin M.F., Raymond D., Corey D.P., Fahn S.,
Risch N.J., Buckler A.J., Gusella J.F., Breakefield X.O.;
"The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding
protein.";
Nat. Genet. 17:40-48(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, and Skin;
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).
[6]
SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-143 AND ASN-158, AND
MUTAGENESIS OF ASN-143 AND ASN-158.
PubMed=10871631; DOI=10.1074/jbc.M910025199;
Kustedjo K., Bracey M.H., Cravatt B.F.;
"Torsin A and its torsion dystonia-associated mutant forms are lumenal
glycoproteins that exhibit distinct subcellular localizations.";
J. Biol. Chem. 275:27933-27939(2000).
[7]
TISSUE SPECIFICITY.
PubMed=10640617; DOI=10.1016/S0006-8993(99)02232-5;
Shashidharan P., Kramer B.C., Walker R.H., Olanow C.W., Brin M.F.;
"Immunohistochemical localization and distribution of torsinA in
normal human and rat brain.";
Brain Res. 853:197-206(2000).
[8]
INTERACTION WITH TOR1B, TISSUE SPECIFICITY, GLYCOSYLATION, AND
SUBCELLULAR LOCATION.
PubMed=15147511; DOI=10.1111/j.1471-4159.2004.02404.x;
Hewett J.W., Kamm C., Boston H., Beauchamp R., Naismith T.,
Ozelius L., Hanson P.I., Breakefield X.O., Ramesh V.;
"TorsinB--perinuclear location and association with torsinA.";
J. Neurochem. 89:1186-1194(2004).
[9]
INTERACTION WITH KLC1, TISSUE SPECIFICITY, AND CHARACTERIZATION OF
VARIANT DYT1 GLU-303 DEL.
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).
[10]
FUNCTION IN CELLULAR TRAFFICKING, SUBUNIT, INTERACTION WITH SLC6A3,
CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL, AND MUTAGENESIS OF
LYS-108.
PubMed=15505207; DOI=10.1073/pnas.0308088101;
Torres G.E., Sweeney A.L., Beaulieu J.M., Shashidharan P., Caron M.G.;
"Effect of torsinA on membrane proteins reveals a loss of function and
a dominant-negative phenotype of the dystonia-associated DeltaE-
torsinA mutant.";
Proc. Natl. Acad. Sci. U.S.A. 101:15650-15655(2004).
[11]
INTERACTION WITH TOR1AIP1 AND TOR1AIP2.
PubMed=15767459; DOI=10.1083/jcb.200411026;
Goodchild R.E., Dauer W.T.;
"The AAA+ protein torsinA interacts with a conserved domain present in
LAP1 and a novel ER protein.";
J. Cell Biol. 168:855-862(2005).
[12]
FUNCTION IN CYTOSKELETON ORGANIZATION, CHARACTERIZATION OF VARIANT
DYT1 GLU-303 DEL, SUBCELLULAR LOCATION, AND INTERACTION WITH VIM.
PubMed=16361107; DOI=10.1016/j.nbd.2005.10.012;
Hewett J.W., Zeng J., Niland B.P., Bragg D.C., Breakefield X.O.;
"Dystonia-causing mutant torsinA inhibits cell adhesion and neurite
extension through interference with cytoskeletal dynamics.";
Neurobiol. Dis. 22:98-111(2006).
[13]
SUBCELLULAR LOCATION, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION,
AND MUTAGENESIS OF VAL-18; ALA-20 AND VAL-33.
PubMed=17037984; DOI=10.1042/BJ20061313;
Callan A.C., Bunning S., Jones O.T., High S., Swanton E.;
"Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the
endoplasmic reticulum.";
Biochem. J. 401:607-612(2007).
[14]
FUNCTION IN PROTEIN PROCESSING, AND CHARACTERIZATION OF VARIANT DYT1
GLU-303 DEL.
PubMed=17428918; DOI=10.1073/pnas.0701185104;
Hewett J.W., Tannous B., Niland B.P., Nery F.C., Zeng J., Li Y.,
Breakefield X.O.;
"Mutant torsinA interferes with protein processing through the
secretory pathway in DYT1 dystonia cells.";
Proc. Natl. Acad. Sci. U.S.A. 104:7271-7276(2007).
[15]
FUNCTION IN VESICLE RECYCLING, INTERACTION WITH SNAPIN, AND
CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL.
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).
[16]
FUNCTION IN NUCLEAR POLARITY, INTERACTION WITH PLEC; SYNE3 AND VIM,
AND CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL.
PubMed=18827015; DOI=10.1242/jcs.029454;
Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D.,
Li Y., Wiche G., Sonnenberg A., Breakefield X.O.;
"TorsinA binds the KASH domain of nesprins and participates in linkage
between nuclear envelope and cytoskeleton.";
J. Cell Sci. 121:3476-3486(2008).
[17]
INTERACTION WITH KLHL14, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LYS-108 AND GLU-171.
PubMed=19535332; DOI=10.1074/jbc.M109.004838;
Giles L.M., Li L., Chin L.S.;
"Printor, a novel torsinA-interacting protein implicated in dystonia
pathogenesis.";
J. Biol. Chem. 284:21765-21775(2009).
[18]
FUNCTION, HEXAMERIZATION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LYS-108 AND GLU-171.
PubMed=19339278; DOI=10.1091/mbc.E09-01-0094;
Vander Heyden A.B., Naismith T.V., Snapp E.L., Hodzic D., Hanson P.I.;
"LULL1 retargets TorsinA to the nuclear envelope revealing an activity
that is impaired by the DYT1 dystonia mutation.";
Mol. Biol. Cell 20:2661-2672(2009).
[19]
FUNCTION AS CHAPERONE, AND CHARACTERIZATION OF VARIANT DYT1 GLU-303
DEL.
PubMed=20169475; DOI=10.1007/s12192-010-0173-2;
Burdette A.J., Churchill P.F., Caldwell G.A., Caldwell K.A.;
"The early-onset torsion dystonia-associated protein, torsinA,
displays molecular chaperone activity in vitro.";
Cell Stress Chaperones 15:605-617(2010).
[20]
SUBUNIT, AND MUTAGENESIS OF GLU-171.
PubMed=20015956; DOI=10.1093/hmg/ddp557;
Jungwirth M., Dear M.L., Brown P., Holbrook K., Goodchild R.;
"Relative tissue expression of homologous torsinB correlates with the
neuronal specific importance of DYT1 dystonia-associated torsinA.";
Hum. Mol. Genet. 19:888-900(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
INTERACTION WITH CSN4; SNAPIN AND STON2, SUBCELLULAR LOCATION, AND
CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL.
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).
[23]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TOR1AIP1 AND TOR1AIP2,
CHARACTERIZATION OF VARIANT GLU-303 DEL, AND MUTAGENESIS OF GLU-171.
PubMed=23569223; DOI=10.1073/pnas.1300676110;
Zhao C., Brown R.S., Chase A.R., Eisele M.R., Schlieker C.;
"Regulation of Torsin ATPases by LAP1 and LULL1.";
Proc. Natl. Acad. Sci. U.S.A. 110:E1545-1554(2013).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[25]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 51-332 IN COMPLEX WITH
TOR1AIP2, CHARACTERIZATION OF VARIANT DYT1 GLU-303 DEL, AND
MUTAGENESIS OF GLU-171.
PubMed=27490483; DOI=10.7554/eLife.17983;
Demircioglu F.E., Sosa B.A., Ingram J., Ploegh H.L., Schwartz T.U.;
"Structures of TorsinA and its disease-mutant complexed with an
activator reveal the molecular basis for primary dystonia.";
Elife 5:0-0(2016).
[26]
VARIANT 323-PHE--TYR-328 DEL.
PubMed=11523564; DOI=10.1007/s100480100111;
Leung J.C., Klein C., Friedman J., Vieregge P., Jacobs H., Doheny D.,
Kamm C., DeLeon D., Pramstaller P.P., Penney J.B., Eisengart M.,
Jankovic J., Gasser T., Bressman S.B., Corey D.P., Kramer P.,
Brin M.F., Ozelius L.J., Breakefield X.O.;
"Novel mutation in the TOR1A (DYT1) gene in atypical early onset
dystonia and polymorphisms in dystonia and early onset parkinsonism.";
Neurogenetics 3:133-143(2001).
[27]
VARIANT DYT1 GLN-288, AND CHARACTERIZATION OF VARIANTS DYT1 GLN-288
AND GLU-303 DEL.
PubMed=18477710; DOI=10.1136/jnnp.2008.148270;
Zirn B., Grundmann K., Huppke P., Puthenparampil J., Wolburg H.,
Riess O., Muller U.;
"Novel TOR1A mutation p.Arg288Gln in early-onset dystonia (DYT1).";
J. Neurol. Neurosurg. Psych. 79:1327-1330(2008).
[28]
VARIANT DYT1 ILE-205, AND CHARACTERIZATION OF VARIANTS DYT1 ILE-205
AND GLU-303 DEL.
PubMed=19955557; DOI=10.1136/jmg.2009.072082;
Calakos N., Patel V.D., Gottron M., Wang G., Tran-Viet K.N.,
Brewington D., Beyer J.L., Steffens D.C., Krishnan R.R., Zuechner S.;
"Functional evidence implicating a novel TOR1A mutation in idiopathic,
late-onset focal dystonia.";
J. Med. Genet. 47:646-650(2010).
[29]
VARIANT HIS-216.
PubMed=26940431; DOI=10.1111/ane.12579;
Piovesana L.G., Torres F.R., Azevedo P.C., Amaral T.P.,
Lopes-Cendes I., D'Abreu A.;
"New THAP1 mutation and role of putative modifier in TOR1A.";
Acta Neurol. Scand. 135:183-188(2017).
-!- 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. {ECO:0000269|PubMed:15505207,
ECO:0000269|PubMed:16361107, ECO:0000269|PubMed:17428918,
ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:18827015,
ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:20169475,
ECO:0000269|PubMed:23569223}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:23569223}.
-!- 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:15147511,
ECO:0000269|PubMed:15505207, ECO:0000269|PubMed:15767459,
ECO:0000269|PubMed:16361107, ECO:0000269|PubMed:18167355,
ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19535332,
ECO:0000269|PubMed:20015956, ECO:0000269|PubMed:21102408,
ECO:0000269|PubMed:23569223, ECO:0000269|PubMed:27490483}.
-!- INTERACTION:
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-524257, EBI-10172290;
P60409-2:KRTAP10-7; NbExp=3; IntAct=EBI-524257, EBI-10695388;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Nucleus
membrane; Peripheral membrane protein. Cell projection, growth
cone {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}.
Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Cytoplasmic
vesicle, secretory vesicle, synaptic vesicle. Cytoplasm,
cytoskeleton. Note=Upon oxidative stress, redistributes to
protusions from the cell surface (By similarity). Peripherally
associated with the inner face of the ER membrane, probably
mediated by the interaction with TOR1AIP1. The association with
nucleus membrane is mediated by the interaction with TOR1AIP2.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14656-1; Sequence=Displayed;
Name=2;
IsoId=O14656-2; Sequence=VSP_026605;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Highest levels in kidney and
liver. In the brain, high levels found in the dopaminergic neurons
of the substantia nigra pars compacta, as well as in the
neocortex, hippocampus and cerebellum. Also highly expressed in
the spinal cord. {ECO:0000269|PubMed:10640617,
ECO:0000269|PubMed:14970196, ECO:0000269|PubMed:15147511}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10871631,
ECO:0000269|PubMed:15147511, ECO:0000269|PubMed:17037984}.
-!- DISEASE: Dystonia 1, torsion, autosomal dominant (DYT1)
[MIM:128100]: A primary torsion dystonia, and the most common and
severe form. Dystonia is defined by the presence of sustained
involuntary muscle contractions, often leading to abnormal
postures. Dystonia type 1 is characterized by involuntary,
repetitive, sustained muscle contractions or postures involving
one or more sites of the body, in the absence of other
neurological symptoms. Typically, symptoms develop first in an arm
or leg in middle to late childhood and progress in approximately
30% of patients to other body regions (generalized dystonia)
within about five years. 'Torsion' refers to the twisting nature
of body movements observed in DYT1, often affecting the trunk.
Distribution and severity of symptoms vary widely between affected
individuals, ranging from mild focal dystonia to severe
generalized dystonia, even within families.
{ECO:0000269|PubMed:14970196, ECO:0000269|PubMed:15505207,
ECO:0000269|PubMed:16361107, ECO:0000269|PubMed:17428918,
ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:18477710,
ECO:0000269|PubMed:18827015, ECO:0000269|PubMed:19955557,
ECO:0000269|PubMed:20169475, ECO:0000269|PubMed:21102408,
ECO:0000269|PubMed:27490483, ECO:0000269|PubMed:9288096}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
{ECO:0000305}.
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EMBL; AF007871; AAC51732.1; -; mRNA.
EMBL; AK314505; BAG37105.1; -; mRNA.
EMBL; BT006931; AAP35577.1; -; mRNA.
EMBL; AL158207; CAC88168.1; -; Genomic_DNA.
EMBL; BC000674; AAH00674.1; -; mRNA.
EMBL; BC014484; AAH14484.1; -; mRNA.
CCDS; CCDS6930.1; -. [O14656-1]
RefSeq; NP_000104.1; NM_000113.2. [O14656-1]
UniGene; Hs.534312; -.
PDB; 5J1S; X-ray; 1.40 A; A=51-332.
PDB; 5J1T; X-ray; 1.40 A; A=51-332.
PDBsum; 5J1S; -.
PDBsum; 5J1T; -.
ProteinModelPortal; O14656; -.
SMR; O14656; -.
BioGrid; 108193; 39.
CORUM; O14656; -.
DIP; DIP-34411N; -.
IntAct; O14656; 13.
MINT; MINT-7002075; -.
STRING; 9606.ENSP00000345719; -.
iPTMnet; O14656; -.
PhosphoSitePlus; O14656; -.
BioMuta; TOR1A; -.
EPD; O14656; -.
MaxQB; O14656; -.
PaxDb; O14656; -.
PeptideAtlas; O14656; -.
PRIDE; O14656; -.
DNASU; 1861; -.
Ensembl; ENST00000351698; ENSP00000345719; ENSG00000136827. [O14656-1]
GeneID; 1861; -.
KEGG; hsa:1861; -.
UCSC; uc004byl.4; human. [O14656-1]
CTD; 1861; -.
DisGeNET; 1861; -.
EuPathDB; HostDB:ENSG00000136827.11; -.
GeneCards; TOR1A; -.
GeneReviews; TOR1A; -.
HGNC; HGNC:3098; TOR1A.
HPA; CAB012473; -.
HPA; HPA051195; -.
MalaCards; TOR1A; -.
MIM; 128100; phenotype.
MIM; 605204; gene.
neXtProt; NX_O14656; -.
OpenTargets; ENSG00000136827; -.
Orphanet; 256; Early-onset generalized limb-onset dystonia.
Orphanet; 36899; Myoclonus-dystonia syndrome.
PharmGKB; PA27556; -.
eggNOG; KOG2170; Eukaryota.
eggNOG; ENOG410XR06; LUCA.
GeneTree; ENSGT00390000001920; -.
HOGENOM; HOG000115770; -.
HOVERGEN; HBG054188; -.
InParanoid; O14656; -.
OMA; KMHAGLI; -.
OrthoDB; EOG091G0B5F; -.
PhylomeDB; O14656; -.
TreeFam; TF314941; -.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
ChiTaRS; TOR1A; human.
GeneWiki; Torsin_A; -.
GenomeRNAi; 1861; -.
PRO; PR:O14656; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136827; -.
CleanEx; HS_TOR1A; -.
Genevisible; O14656; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB.
GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
GO; GO:0051787; F:misfolded protein binding; IEA:Ensembl.
GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IEA:InterPro.
GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
GO; GO:0072321; P:chaperone-mediated protein transport; IDA:UniProtKB.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISS:UniProtKB.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:UniProtKB.
GO; GO:0031175; P:neuron projection development; IMP: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; IMP:UniProtKB.
GO; GO:0000338; P:protein deneddylation; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; IDA:UniProtKB.
GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0048489; P:synaptic vesicle transport; IMP: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;
3D-structure; Alternative splicing; ATP-binding; Cell junction;
Cell projection; Chaperone; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Disease mutation; Dystonia;
Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Signal;
Synapse.
SIGNAL 1 20 {ECO:0000305|PubMed:17037984}.
CHAIN 21 332 Torsin-1A.
/FTId=PRO_0000005506.
NP_BIND 102 109 ATP.
REGION 91 251 Interaction with SNAPIN.
REGION 251 332 Interaction with KLC1.
{ECO:0000269|PubMed:14970196}.
REGION 312 332 Interaction with SYNE3.
{ECO:0000269|PubMed:18827015}.
CARBOHYD 143 143 N-linked (GlcNAc...) (high mannose)
asparagine.
{ECO:0000269|PubMed:10871631}.
CARBOHYD 158 158 N-linked (GlcNAc...) (high mannose)
asparagine.
{ECO:0000269|PubMed:10871631}.
VAR_SEQ 149 332 DQLQLWIRGNVSACARSIFIFDEMDKMHAGLIDAIKPFLDY
YDLVDGVSYQKAMFIFLSNAGAERITDVALDFWRSGKQRED
IKLKDIEHALSVSVFNNKNSGFWHSSLIDRNLIDYFVPFLP
LEYKHLKMCIRVEMQSRGYEIDEDIVSRVAEEMTFFPKEER
VFSDKGCKTVFTKLDYYYDD -> ARMEVWNPFLDVIGFGV
SLLWDEIWEFYVEMSEPGKRFMSQFPLERCRS (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_026605.
VARIANT 205 205 F -> I (in DYT1; produces intracellular
misfolded protein aggregates;
dbSNP:rs267607134).
{ECO:0000269|PubMed:19955557}.
/FTId=VAR_070932.
VARIANT 216 216 D -> H (in dbSNP:rs1801968).
{ECO:0000269|PubMed:26940431}.
/FTId=VAR_020449.
VARIANT 264 264 D -> H. {ECO:0000269|PubMed:9288096}.
/FTId=VAR_010788.
VARIANT 288 288 R -> Q (in DYT1; produces an enlarged
perinuclear space; dbSNP:rs727502811).
{ECO:0000269|PubMed:18477710}.
/FTId=VAR_070933.
VARIANT 303 303 Missing (in DYT1; dominant negative; loss
of interaction with TOR1AIP1 and TOR1AIP2
with loss of ATPase activity induction;
enriched in the nuclear envelope; impairs
secretory pathway; produces intracellular
misfolded protein aggregates; produces an
enlarged perinuclear space;
dbSNP:rs80358233).
{ECO:0000269|PubMed:14970196,
ECO:0000269|PubMed:15505207,
ECO:0000269|PubMed:16361107,
ECO:0000269|PubMed:17428918,
ECO:0000269|PubMed:18167355,
ECO:0000269|PubMed:18477710,
ECO:0000269|PubMed:18827015,
ECO:0000269|PubMed:19955557,
ECO:0000269|PubMed:20169475,
ECO:0000269|PubMed:21102408,
ECO:0000269|PubMed:23569223,
ECO:0000269|PubMed:27490483,
ECO:0000269|PubMed:9288096}.
/FTId=VAR_010789.
VARIANT 323 328 Missing (found in a patient with early-
onset atypical dystonia and myoclonic
features; dbSNP:rs80358235).
{ECO:0000269|PubMed:11523564}.
/FTId=VAR_070934.
MUTAGEN 18 18 V->F: Inhibits sequence signal cleavage.
{ECO:0000269|PubMed:17037984}.
MUTAGEN 20 20 A->F: Inhibits sequence signal cleavage.
{ECO:0000269|PubMed:17037984}.
MUTAGEN 33 33 V->N: N-glycosylated.
{ECO:0000269|PubMed:17037984}.
MUTAGEN 108 108 K->A: Loss of ATP-binding. No effect on
interaction with KLHL14. Increases
interaction with TOR1AIP1 and TOR1AIP2.
Abolishes interaction with SLC6A3.
{ECO:0000269|PubMed:15505207,
ECO:0000269|PubMed:19339278,
ECO:0000269|PubMed:19535332}.
MUTAGEN 143 143 N->Q: Reduces N-glycosylation.
{ECO:0000269|PubMed:10871631}.
MUTAGEN 158 158 N->Q: Reduces N-glycosylation.
{ECO:0000269|PubMed:10871631}.
MUTAGEN 171 171 E->Q: Loss of ATP hydrolysis. Loss of
interaction with KLHL14. Localizes in the
nuclear envelope. No effect on
interaction with TOR1AIP1.
{ECO:0000269|PubMed:19339278,
ECO:0000269|PubMed:19535332,
ECO:0000269|PubMed:20015956,
ECO:0000269|PubMed:23569223,
ECO:0000269|PubMed:27490483}.
CONFLICT 259 259 D -> H (in Ref. 3; AAP35577 and 5;
AAH00674). {ECO:0000305}.
HELIX 58 68 {ECO:0000244|PDB:5J1S}.
HELIX 73 87 {ECO:0000244|PDB:5J1S}.
STRAND 96 102 {ECO:0000244|PDB:5J1S}.
HELIX 108 119 {ECO:0000244|PDB:5J1S}.
HELIX 123 125 {ECO:0000244|PDB:5J1S}.
STRAND 129 133 {ECO:0000244|PDB:5J1S}.
HELIX 134 137 {ECO:0000244|PDB:5J1S}.
HELIX 141 143 {ECO:0000244|PDB:5J1S}.
HELIX 144 161 {ECO:0000244|PDB:5J1S}.
STRAND 166 170 {ECO:0000244|PDB:5J1S}.
HELIX 172 174 {ECO:0000244|PDB:5J1S}.
HELIX 177 187 {ECO:0000244|PDB:5J1S}.
STRAND 202 207 {ECO:0000244|PDB:5J1S}.
HELIX 211 223 {ECO:0000244|PDB:5J1S}.
HELIX 228 230 {ECO:0000244|PDB:5J1S}.
HELIX 233 239 {ECO:0000244|PDB:5J1S}.
TURN 240 245 {ECO:0000244|PDB:5J1S}.
HELIX 247 252 {ECO:0000244|PDB:5J1S}.
STRAND 256 262 {ECO:0000244|PDB:5J1S}.
STRAND 264 269 {ECO:0000244|PDB:5J1S}.
HELIX 274 287 {ECO:0000244|PDB:5J1S}.
HELIX 294 303 {ECO:0000244|PDB:5J1S}.
STRAND 306 308 {ECO:0000244|PDB:5J1S}.
TURN 309 311 {ECO:0000244|PDB:5J1S}.
TURN 316 322 {ECO:0000244|PDB:5J1S}.
HELIX 323 328 {ECO:0000244|PDB:5J1S}.
SEQUENCE 332 AA; 37809 MW; B69B28D0B4112080 CRC64;
MKLGRAVLGL LLLAPSVVQA VEPISLGLAL AGVLTGYIYP RLYCLFAECC GQKRSLSREA
LQKDLDDNLF GQHLAKKIIL NAVFGFINNP KPKKPLTLSL HGWTGTGKNF VSKIIAENIY
EGGLNSDYVH LFVATLHFPH ASNITLYKDQ LQLWIRGNVS ACARSIFIFD EMDKMHAGLI
DAIKPFLDYY DLVDGVSYQK AMFIFLSNAG AERITDVALD FWRSGKQRED IKLKDIEHAL
SVSVFNNKNS GFWHSSLIDR NLIDYFVPFL PLEYKHLKMC IRVEMQSRGY EIDEDIVSRV
AEEMTFFPKE ERVFSDKGCK TVFTKLDYYY DD


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