TOR1A_MACFA
ID TOR1A_MACFA Reviewed; 332 AA.
AC Q60HG2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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: Precursor;
GN Name=TOR1A; Synonyms=DYT1; ORFNames=QflA-17338;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) 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|UniProtKB:O14656}.
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
CC {ECO:0000250|UniProtKB:O14656}. Nucleus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell projection, growth cone
CC {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Cytoplasmic
CC vesicle, secretory vesicle {ECO:0000250}. Cytoplasmic vesicle,
CC secretory vesicle, synaptic vesicle {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=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. Upon oxidative stress, redistributes to
CC protusions from the cell surface (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; AB125165; BAD51953.1; -; mRNA.
DR RefSeq; NP_001272011.1; NM_001285082.1.
DR AlphaFoldDB; Q60HG2; -.
DR SMR; Q60HG2; -.
DR STRING; 9541.XP_005580705.1; -.
DR GeneID; 102124758; -.
DR CTD; 1861; -.
DR eggNOG; KOG2170; Eukaryota.
DR OrthoDB; 1453168at2759; -.
DR Proteomes; UP000233100; Unplaced.
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:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:InterPro.
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: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:0048499; P:synaptic vesicle membrane organization; 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 InterPro; IPR017378; Torsin_1/2.
DR PANTHER; PTHR10760; PTHR10760; 1.
DR PANTHER; PTHR10760:SF15; PTHR10760:SF15; 1.
DR Pfam; PF06309; Torsin; 1.
DR PIRSF; PIRSF038079; Torsin_2A; 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; Reference proteome; Signal; Synapse.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..332
FT /note="Torsin-1A"
FT /id="PRO_0000005507"
FT REGION 91..251
FT /note="Interaction with SNAPIN"
FT /evidence="ECO:0000250"
FT REGION 251..332
FT /note="Interaction with KLC1"
FT /evidence="ECO:0000250"
FT REGION 312..332
FT /note="Interaction with SYNE3"
FT /evidence="ECO:0000250"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 332 AA; 37763 MW; D2507D1CEA029349 CRC64;
MKLGRAALGL LLLAPSVVQA VEPISLGLAL AGVLTGYIYP RLYCLFAECC GQKRSLSREA
LQKDLDNKLF GQHLAKKIIL NAVFGFINNP KPKKPLTLSL HGWTGTGKNF VSKIIAENIY
EGGLNSDYVH LFVATLHFPH ASNITLYKDQ LQLWIRGNVS ACARSIFIFD EMDKMHAGLI
DAIKPFLDYY DLVDGVSYQK AIFIFLSNAG AERITDVALD FWRSGKQRED IKLKDIEHAL
SVSVFNNKNS GFWHSSLIDR NLIDYFVPFL PLEYKHLKMC IRVEMQSRGY ETNEDIVSRV
AEEMTFFPKE ERVFSDKGCK TVFTKLDYYY DD
