TOR1A_CRICR
ID TOR1A_CRICR Reviewed; 273 AA.
AC Q9ERA9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Torsin-1A;
DE AltName: Full=Dystonia 1 protein;
DE AltName: Full=Torsin ATPase 1;
DE EC=3.6.4.-;
DE AltName: Full=Torsin family 1 member A;
DE Flags: Fragment;
GN Name=TOR1A; Synonyms=DYT1;
OS Cricetus cricetus (Black-bellied hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetus.
OX NCBI_TaxID=10034;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Kuner R., Teismann P., Trutzel A., Naim J., Richter A., Bach A., Ferger B.,
RA Schneider A.;
RT "Characterization of the mouse torsinA gene.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein with chaperone functions important for the control of
CC protein folding, processing, stability and localization as well as for
CC the reduction of misfolded protein aggregates. Involved in the
CC regulation of synaptic vesicle recycling, controls STON2 protein
CC stability in collaboration with the COP9 signalosome complex (CSN). In
CC the nucleus, may link the cytoskeleton with the nuclear envelope, this
CC mechanism seems to be crucial for the control of nuclear polarity, cell
CC movement and, specifically in neurons, nuclear envelope integrity.
CC Participates in the cellular trafficking and may regulate the
CC subcellular location of multipass membrane proteins such as the
CC dopamine transporter SLC6A3, leading to the modulation of dopamine
CC neurotransmission. In the endoplasmic reticulum, plays a role in the
CC quality control of protein folding by increasing clearance of misfolded
CC proteins such as SGCE variants or holding them in an intermediate state
CC for proper refolding. May have a redundant function with TOR1B in non-
CC neural tissues (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC -!- SUBUNIT: Homohexamer. Interacts with TOR1B; the interaction may be
CC specific of neural tissues. Interacts (ATP-bound) with TOR1AIP1 and
CC TOR1AIP2; the interactions induce ATPase activity. Interacts with
CC KLHL14; preferentially when ATP-free. Interacts with KLC1 (via TPR
CC repeats); the interaction associates TOR1A with the kinesin oligomeric
CC complex. Interacts with COPS4; the interaction associates TOR1A with
CC the CSN complex. Interacts with SNAPIN; the interaction is direct and
CC associates SNAPIN with the CSN complex. Interacts with STON2. Interacts
CC (ATP-bound) with SYNE3 (via KASH domain); the interaction is required
CC for SYNE3 nuclear envelope localization. Interacts with VIM; the
CC interaction associates TOR1A with the cytoskeleton. Interacts with
CC PLEC. Interacts (ATP-bound) with SLC6A3; regulates SLC6A3 transport to
CC the plasma membrane (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC Nucleus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cytoplasmic
CC vesicle membrane {ECO:0000250}. Synapse, synaptosome {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Mainly located in the lumen
CC of the endoplasmic reticulum.Peripherally associated with the inner
CC face of the ER membrane, probably mediated by the interaction with
CC TOR1AIP1. The association with nucleus membrane is mediated by the
CC interaction with TOR1AIP2 (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ298842; CAC12784.1; -; mRNA.
DR AlphaFoldDB; Q9ERA9; -.
DR SMR; Q9ERA9; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; ISS:UniProtKB.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISS:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR GO; GO:0071763; P:nuclear membrane organization; ISS:UniProtKB.
DR GO; GO:0006996; P:organelle organization; ISS:UniProtKB.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISS:UniProtKB.
DR GO; GO:0000338; P:protein deneddylation; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0051584; P:regulation of dopamine uptake involved in synaptic transmission; ISS:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0048489; P:synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010448; Torsin.
DR InterPro; IPR030549; Torsin-1A.
DR PANTHER; PTHR10760; PTHR10760; 1.
DR PANTHER; PTHR10760:SF15; PTHR10760:SF15; 1.
DR Pfam; PF06309; Torsin; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell projection; Chaperone; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleus; Synapse; Synaptosome.
FT CHAIN <1..>273
FT /note="Torsin-1A"
FT /id="PRO_0000191242"
FT REGION 45..205
FT /note="Interaction with SNAPIN"
FT /evidence="ECO:0000250"
FT BINDING 56..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 273
SQ SEQUENCE 273 AA; 31217 MW; AC0E96EED256018E CRC64;
AECCGQKRSL SREALQKDLD DKLFGQHLAK KVILNAVSGF LSNPKPKKPL TLSLHGWTGT
GKNFASKIIA ENIYEGGLNS DYVHLFVATL HFPHASNVTL YKDQLQMWIR GNVSACARSI
FIFDEMDKMH AGLIDAIKPF LDYYDVVDEV SYQKAIFIFL SNAGAERITD VALDFWKSGK
QREEIKLRDM EHALAVSVFN NKNSGFWHSS LIDRNLIDYF VPFLPLEYKH LKMCIRVEMQ
SRGYEVDEDI ISKVAEEMTF FPKEERVFSD KGC
