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Q9ER39 (TOR1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Torsin-1A
Alternative name(s):
Dystonia 1 protein
Torsin ATPase 1
EC=3.6.4.-
Torsin family 1 member A
Gene names
Name:Tor1a
Synonyms:Dyt1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.3 Ref.4 Ref.5 Ref.6 Ref.9

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.6 Ref.7 Ref.9

Subcellular location

Endoplasmic reticulum lumen. Nucleus membrane; Peripheral membrane protein. Cell projectiongrowth cone. Cytoplasmic vesicle membrane By similarity. Cell junctionsynapsesynaptosome By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmic vesiclesecretory vesicle By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle By similarity. 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. Ref.8 Ref.9

Tissue specificity

Widely expressed (at protein level). Ref.3 Ref.8

Developmental stage

At E16 and E18, widely expressed with higher expression levels in neural tissues. In the spinal cord, expressed as early as E12 until p21, the expression levels decrease in the adulthood (at protein level). Ref.3 Ref.8 Ref.9

Post-translational modification

N-glycosylated. Ref.8

Disruption phenotype

Animals fail to feed or vocalize and die within 48 hours of birth. At E18, the global structure of the central nervous system is normal. However, at the cellular level, nuclear envelope abnormalities, with membranous vesicle-appearing structures in the perinuclear space, are observed in multiple areas of the central nervous system, including neurons of the spinal cord, pons, frontal cortex, and hippocampus. Ref.3 Ref.9

Sequence similarities

Belongs to the ClpA/ClpB family. Torsin subfamily.

Ontologies

Keywords
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoplasmic vesicle
Cytoskeleton
Endoplasmic reticulum
Membrane
Nucleus
Synapse
Synaptosome
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

ER-associated misfolded protein catabolic process

Inferred from direct assay Ref.4. Source: UniProtKB

cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

chaperone mediated protein folding requiring cofactor

Inferred from electronic annotation. Source: InterPro

chaperone-mediated protein folding

Inferred from sequence or structural similarity. Source: UniProtKB

chaperone-mediated protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

intermediate filament cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear envelope organization

Inferred from mutant phenotype Ref.3. Source: MGI

nuclear membrane organization

Inferred from mutant phenotype PubMed 20080676Ref.9. Source: MGI

organelle organization

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of synaptic vesicle endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

protein deneddylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein homooligomerization

Inferred from direct assay Ref.8. Source: MGI

protein localization to nucleus

Inferred from mutant phenotype Ref.6. Source: UniProtKB

regulation of dopamine uptake involved in synaptic transmission

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein localization to cell surface

Inferred from sequence or structural similarity. Source: UniProtKB

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle transport

Inferred from sequence or structural similarity. Source: UniProtKB

wound healing, spreading of cells

Inferred from mutant phenotype Ref.6. Source: UniProtKB

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay PubMed 11730696. Source: MGI

cytoplasmic vesicle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum

Inferred from direct assay PubMed 15767459. Source: MGI

endoplasmic reticulum lumen

Inferred from direct assay Ref.8. Source: MGI

extrinsic component of endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

growth cone

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear envelope

Inferred from direct assay Ref.9. Source: MGI

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 11730696. Source: MGI

secretory granule

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

transport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeletal protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

misfolded protein binding

Inferred from physical interaction Ref.4. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 333313Torsin-1A
PRO_0000005508

Regions

Nucleotide binding103 – 1108ATP Potential
Region92 – 252161Interaction with SNAPIN By similarity
Region252 – 33382Interaction with KLC1 By similarity
Region313 – 33321Interaction with SYNE3 By similarity

Amino acid modifications

Glycosylation1441N-linked (GlcNAc...) By similarity
Glycosylation1591N-linked (GlcNAc...) By similarity

Experimental info

Mutagenesis3041Missing: Nuclear envelope abnormalities specific to neurons. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9ER39 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: CD2D7B97E3F03274

FASTA33337,830
        10         20         30         40         50         60 
MKLGRAALAL LLLAPCVVRA VEPISLSLAL AGVLTTYISY PRLYCLFAEC CGQMRSLSRE 

        70         80         90        100        110        120 
ALQKDLDNKL FGQHLAKKVI LNAVSGFLSN PKPKKPLTLS LHGWTGTGKN FASKIIAENI 

       130        140        150        160        170        180 
YEGGLNSDYV HLFVATLHFP HASNITQYKD QLQMWIRGNV SACARSIFIF DEMDKMHAGL 

       190        200        210        220        230        240 
IDAIKPFLDY YDVVDEVSYQ KAIFIFLSNA GAERITDVAL DFWKSGKQRE EIKLRDMEPA 

       250        260        270        280        290        300 
LAVSVFNNKN SGFWHSSLID RNLIDYFVPF LPLEYKHLKM CIRVEMQSRG YEVDEDIISK 

       310        320        330 
VAEEMTFFPK EEKVFSDKGC KTVFTKLDYY LDD 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the mouse torsinA gene."
Kuner R., Teismann P., Trutzel A., Naim J., Richter A., Bach A., Ferger B., Schneider A.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[3]"Loss of the dystonia-associated protein torsinA selectively disrupts the neuronal nuclear envelope."
Goodchild R.E., Kim C.E., Dauer W.T.
Neuron 48:923-932(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEAR ENVELOPE INTEGRITY, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLU-304.
[4]"SGCE missense mutations that cause myoclonus-dystonia syndrome impair epsilon-sarcoglycan trafficking to the plasma membrane: modulation by ubiquitination and torsinA."
Esapa C.T., Waite A., Locke M., Benson M.A., Kraus M., McIlhinney R.A., Sillitoe R.V., Beesley P.W., Blake D.J.
Hum. Mol. Genet. 16:327-342(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DEGRADATION OF MISFOLDED PROTEINS.
[5]"Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells."
Hewett J.W., Tannous B., Niland B.P., Nery F.C., Zeng J., Li Y., Breakefield X.O.
Proc. Natl. Acad. Sci. U.S.A. 104:7271-7276(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PROTEIN PROCESSING.
[6]"TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton."
Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., Wiche G., Sonnenberg A., Breakefield X.O.
J. Cell Sci. 121:3476-3486(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEAR POLARITY, INTERACTION WITH SYNE3; PLEC AND VIM.
[7]"Printor, a novel torsinA-interacting protein implicated in dystonia pathogenesis."
Giles L.M., Li L., Chin L.S.
J. Biol. Chem. 284:21765-21775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KLHL14.
[8]"Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinA."
Jungwirth M., Dear M.L., Brown P., Holbrook K., Goodchild R.
Hum. Mol. Genet. 19:888-900(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION, DEVELOPMENTAL STAGE.
[9]"A molecular mechanism underlying the neural-specific defect in torsinA mutant mice."
Kim C.E., Perez A., Perkins G., Ellisman M.H., Dauer W.T.
Proc. Natl. Acad. Sci. U.S.A. 107:9861-9866(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEAR ENVELOPE INTEGRITY, INTERACTION WITH TOR1AIP1, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ298841 mRNA. Translation: CAC12785.1.
BC017683 mRNA. Translation: AAH17683.1.
CCDSCCDS15891.1.
RefSeqNP_659133.1. NM_144884.2.
UniGeneMm.154994.

3D structure databases

ProteinModelPortalQ9ER39.
SMRQ9ER39. Positions 95-122.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206008. 1 interaction.
MINTMINT-1836416.

PTM databases

PhosphoSiteQ9ER39.

Proteomic databases

MaxQBQ9ER39.
PaxDbQ9ER39.
PRIDEQ9ER39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028200; ENSMUSP00000028200; ENSMUSG00000026849.
GeneID30931.
KEGGmmu:30931.
UCSCuc008jdc.2. mouse.

Organism-specific databases

CTD1861.
MGIMGI:1353568. Tor1a.

Phylogenomic databases

eggNOGNOG283963.
GeneTreeENSGT00390000001920.
HOGENOMHOG000115770.
HOVERGENHBG054188.
InParanoidQ9ER39.
OMACCRPEWI.
OrthoDBEOG7TF791.
PhylomeDBQ9ER39.
TreeFamTF314941.

Gene expression databases

ArrayExpressQ9ER39.
BgeeQ9ER39.
CleanExMM_TOR1A.
GenevestigatorQ9ER39.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR010448. Torsin.
IPR017378. Torsin_subgr.
[Graphical view]
PANTHERPTHR10760. PTHR10760. 1 hit.
PfamPF06309. Torsin. 1 hit.
[Graphical view]
PIRSFPIRSF038079. Torsin_2A. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTOR1A. mouse.
NextBio307342.
PROQ9ER39.
SOURCESearch...

Entry information

Entry nameTOR1A_MOUSE
AccessionPrimary (citable) accession number: Q9ER39
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot