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Q9ER39

- TOR1A_MOUSE

UniProt

Q9ER39 - TOR1A_MOUSE

Protein

Torsin-1A

Gene

Tor1a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi103 – 1108ATPSequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. cytoskeletal protein binding Source: UniProtKB
    4. misfolded protein binding Source: UniProtKB
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cell adhesion Source: UniProtKB
    3. chaperone-mediated protein folding Source: UniProtKB
    4. chaperone mediated protein folding requiring cofactor Source: InterPro
    5. chaperone-mediated protein transport Source: UniProtKB
    6. ER-associated misfolded protein catabolic process Source: UniProtKB
    7. intermediate filament cytoskeleton organization Source: UniProtKB
    8. neuron projection development Source: UniProtKB
    9. nuclear envelope organization Source: MGI
    10. nuclear membrane organization Source: MGI
    11. organelle organization Source: UniProtKB
    12. positive regulation of synaptic vesicle endocytosis Source: UniProtKB
    13. protein deneddylation Source: UniProtKB
    14. protein homooligomerization Source: MGI
    15. protein localization to nucleus Source: UniProtKB
    16. regulation of dopamine uptake involved in synaptic transmission Source: UniProtKB
    17. regulation of protein localization to cell surface Source: UniProtKB
    18. response to oxidative stress Source: Ensembl
    19. synaptic vesicle transport Source: UniProtKB
    20. wound healing, spreading of cells Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone, Hydrolase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Torsin-1A
    Alternative name(s):
    Dystonia 1 protein
    Torsin ATPase 1 (EC:3.6.4.-)
    Torsin family 1 member A
    Gene namesi
    Name:Tor1a
    Synonyms:Dyt1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1353568. Tor1a.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: MGI
    3. cytoplasmic vesicle membrane Source: UniProtKB
    4. cytoskeleton Source: UniProtKB-SubCell
    5. endoplasmic reticulum Source: MGI
    6. endoplasmic reticulum lumen Source: MGI
    7. extrinsic component of endoplasmic reticulum membrane Source: UniProtKB
    8. growth cone Source: UniProtKB
    9. nuclear envelope Source: MGI
    10. nuclear membrane Source: UniProtKB-SubCell
    11. nucleus Source: MGI
    12. secretory granule Source: UniProtKB
    13. synaptic vesicle Source: UniProtKB
    14. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Endoplasmic reticulum, Membrane, Nucleus, Synapse, Synaptosome

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi304 – 3041Missing: Nuclear envelope abnormalities specific to neurons. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Chaini21 – 333313Torsin-1APRO_0000005508Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi144 – 1441N-linked (GlcNAc...)By similarity
    Glycosylationi159 – 1591N-linked (GlcNAc...)By similarity

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ9ER39.
    PaxDbiQ9ER39.
    PRIDEiQ9ER39.

    PTM databases

    PhosphoSiteiQ9ER39.

    Expressioni

    Tissue specificityi

    Widely expressed (at protein level).2 Publications

    Developmental stagei

    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).3 Publications

    Gene expression databases

    ArrayExpressiQ9ER39.
    BgeeiQ9ER39.
    CleanExiMM_TOR1A.
    GenevestigatoriQ9ER39.

    Interactioni

    Subunit structurei

    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.3 Publications

    Protein-protein interaction databases

    BioGridi206008. 1 interaction.
    MINTiMINT-1836416.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ER39.
    SMRiQ9ER39. Positions 95-122.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni92 – 252161Interaction with SNAPINBy similarityAdd
    BLAST
    Regioni252 – 33382Interaction with KLC1By similarityAdd
    BLAST
    Regioni313 – 33321Interaction with SYNE3By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ClpA/ClpB family. Torsin subfamily.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG283963.
    GeneTreeiENSGT00390000001920.
    HOGENOMiHOG000115770.
    HOVERGENiHBG054188.
    InParanoidiQ9ER39.
    OMAiCCRPEWI.
    OrthoDBiEOG7TF791.
    PhylomeDBiQ9ER39.
    TreeFamiTF314941.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR010448. Torsin.
    IPR017378. Torsin_subgr.
    [Graphical view]
    PANTHERiPTHR10760. PTHR10760. 1 hit.
    PfamiPF06309. Torsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038079. Torsin_2A. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9ER39-1 [UniParc]FASTAAdd to Basket

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    MKLGRAALAL LLLAPCVVRA VEPISLSLAL AGVLTTYISY PRLYCLFAEC    50
    CGQMRSLSRE ALQKDLDNKL FGQHLAKKVI LNAVSGFLSN PKPKKPLTLS 100
    LHGWTGTGKN FASKIIAENI YEGGLNSDYV HLFVATLHFP HASNITQYKD 150
    QLQMWIRGNV SACARSIFIF DEMDKMHAGL IDAIKPFLDY YDVVDEVSYQ 200
    KAIFIFLSNA GAERITDVAL DFWKSGKQRE EIKLRDMEPA LAVSVFNNKN 250
    SGFWHSSLID RNLIDYFVPF LPLEYKHLKM CIRVEMQSRG YEVDEDIISK 300
    VAEEMTFFPK EEKVFSDKGC KTVFTKLDYY LDD 333
    Length:333
    Mass (Da):37,830
    Last modified:March 1, 2001 - v1
    Checksum:iCD2D7B97E3F03274
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ298841 mRNA. Translation: CAC12785.1.
    BC017683 mRNA. Translation: AAH17683.1.
    CCDSiCCDS15891.1.
    RefSeqiNP_659133.1. NM_144884.2.
    UniGeneiMm.154994.

    Genome annotation databases

    EnsembliENSMUST00000028200; ENSMUSP00000028200; ENSMUSG00000026849.
    GeneIDi30931.
    KEGGimmu:30931.
    UCSCiuc008jdc.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ298841 mRNA. Translation: CAC12785.1 .
    BC017683 mRNA. Translation: AAH17683.1 .
    CCDSi CCDS15891.1.
    RefSeqi NP_659133.1. NM_144884.2.
    UniGenei Mm.154994.

    3D structure databases

    ProteinModelPortali Q9ER39.
    SMRi Q9ER39. Positions 95-122.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206008. 1 interaction.
    MINTi MINT-1836416.

    PTM databases

    PhosphoSitei Q9ER39.

    Proteomic databases

    MaxQBi Q9ER39.
    PaxDbi Q9ER39.
    PRIDEi Q9ER39.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028200 ; ENSMUSP00000028200 ; ENSMUSG00000026849 .
    GeneIDi 30931.
    KEGGi mmu:30931.
    UCSCi uc008jdc.2. mouse.

    Organism-specific databases

    CTDi 1861.
    MGIi MGI:1353568. Tor1a.

    Phylogenomic databases

    eggNOGi NOG283963.
    GeneTreei ENSGT00390000001920.
    HOGENOMi HOG000115770.
    HOVERGENi HBG054188.
    InParanoidi Q9ER39.
    OMAi CCRPEWI.
    OrthoDBi EOG7TF791.
    PhylomeDBi Q9ER39.
    TreeFami TF314941.

    Miscellaneous databases

    ChiTaRSi TOR1A. mouse.
    NextBioi 307342.
    PROi Q9ER39.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ER39.
    Bgeei Q9ER39.
    CleanExi MM_TOR1A.
    Genevestigatori Q9ER39.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR010448. Torsin.
    IPR017378. Torsin_subgr.
    [Graphical view ]
    PANTHERi PTHR10760. PTHR10760. 1 hit.
    Pfami PF06309. Torsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038079. Torsin_2A. 1 hit.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiTOR1A_MOUSE
    AccessioniPrimary (citable) accession number: Q9ER39
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3