ID E7FDJ9_DANRE Unreviewed; 355 AA.
AC E7FDJ9; A0A8N7UUP2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Torsin {ECO:0000256|PIRNR:PIRNR038079};
GN Name=tor1l2 {ECO:0000313|Ensembl:ENSDARP00000110024,
GN ECO:0000313|RefSeq:XP_684868.5, ECO:0000313|ZFIN:ZDB-GENE-121107-3};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000110024};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000110024}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000110024};
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000110024, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000110024};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_684868.5}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_684868.5};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001836};
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. {ECO:0000256|ARBA:ARBA00025909}.
CC -!- SUBCELLULAR LOCATION: Cell projection, growth cone
CC {ECO:0000256|ARBA:ARBA00004624}. Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004156}. Endoplasmic reticulum lumen
CC {ECO:0000256|PIRNR:PIRNR038079}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000256|ARBA:ARBA00006235, ECO:0000256|PIRNR:PIRNR038079}.
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DR EMBL; AL954146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_684868.5; XM_679776.7.
DR STRING; 7955.ENSDARP00000110024; -.
DR Ensembl; ENSDART00000126892; ENSDARP00000110024; ENSDARG00000090741.
DR Ensembl; ENSDART00000126892.3; ENSDARP00000110024.2; ENSDARG00000090741.3.
DR GeneID; 556854; -.
DR AGR; ZFIN:ZDB-GENE-121107-3; -.
DR CTD; 556854; -.
DR ZFIN; ZDB-GENE-121107-3; tor1l2.
DR HOGENOM; CLU_053537_1_0_1; -.
DR OMA; ESKHVQI; -.
DR OrthoDB; 4023449at2759; -.
DR Reactome; R-DRE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Proteomes; UP000000437; Chromosome 23.
DR Bgee; ENSDARG00000090741; Expressed in zone of skin and 2 other cell types or tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019894; F:kinesin binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0071763; P:nuclear membrane organization; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; IBA:GO_Central.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049337; TOR1A_C.
DR InterPro; IPR010448; Torsin.
DR InterPro; IPR017378; Torsin_1/2.
DR PANTHER; PTHR10760; TORSIN; 1.
DR PANTHER; PTHR10760:SF15; TORSIN-1A; 1.
DR Pfam; PF21376; TOR1A_C; 1.
DR Pfam; PF06309; Torsin; 1.
DR PIRSF; PIRSF038079; Torsin_2A; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR038079-1};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR038079};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR038079-1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 295..349
FT /note="Torsin-1A C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21376"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038079-1"
SQ SEQUENCE 355 AA; 40910 MW; 354D3DC0C3BF3831 CRC64;
MYAVCHVSLL LKECTLPETK HKKKPESFAL TMKVQRILTA LLLVSNITSS SCFLEAFTDA
LKHSAVYKFF ERDDLLVFDP KRLEKDLNDF LFGQHIASNV ILKSVSSFMT DSKPNKPLVL
SLHGTTGTGK NHVTKILARN IYKKGEESKH VQIYVSEYNF PDRGKVDLYT AQLRQWIYGN
VSSFPRSMFI FDEMDKMQPQ LIDVLKPFLD YSLVNGVSFH NAIFIFLSNA GGKVIADLAL
DFWREGKNRE DLWMNSRELE IKISTNVYND KNCGFLHTSI IDEHLIDHFI PFLPLELKHV
RQCVLAEMKH LNITKDDELA DEVARDMPYF PEEERIFAVK GCKSVRQKLV LHVDE
//
