ID A0A3Q3N8P7_9TELE Unreviewed; 1051 AA.
AC A0A3Q3N8P7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Torsin-1A {ECO:0000256|ARBA:ARBA00013611};
DE AltName: Full=Dystonia 1 protein {ECO:0000256|ARBA:ARBA00033320};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000028584.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000028584.2}
RP IDENTIFICATION.
RG Ensembl;
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}. 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}.
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DR AlphaFoldDB; A0A3Q3N8P7; -.
DR STRING; 205130.ENSMAMP00000028584; -.
DR Ensembl; ENSMAMT00000029326.2; ENSMAMP00000028584.2; ENSMAMG00000019247.2.
DR GeneTree; ENSGT00950000182888; -.
DR InParanoid; A0A3Q3N8P7; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049337; TOR1A_C.
DR InterPro; IPR010448; Torsin.
DR PANTHER; PTHR10760; TORSIN; 1.
DR PANTHER; PTHR10760:SF15; TORSIN-1A; 1.
DR Pfam; PF21376; TOR1A_C; 4.
DR Pfam; PF06309; Torsin; 3.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261640}.
FT DOMAIN 145..288
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 480..623
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 815..958
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 1051 AA; 119749 MW; FE61F8255C5F4EEF CRC64;
MKARGQKSDQ NKAHKLAKDL EYFPKFWEAS STRGCKTVEA RLEFYTMSTS DGNCSVTMST
SNKYNALKQM NKESKSSVVV KSLDPINYEW QQIFNSHESC DSKWISFNAE GLRADVESKL
IGQHIASSII LKAVEGFMSD TNPQKPLVLS LHGPSGTGKN FVSKLIAGNI YKEGMDSSFV
HIFISTYHFP HQGHVDLYKT QLQQWIKDKI THCERSMFIF DEMDKMHPGL TDSIMPYLGY
HNKLDGVSYR KAIFIFLSNA GGEIITETAL KFWKEGKDRE EIELKDLETL ISATAFNNNN
SGFWHSSLID RHLVDFFVPF LPLQYGHVII CAMATMKARG QKPDQNKAHK LAKDLEYFPK
FWEVFSARGC KTVEARLEFY MMSTSDGNCS VTMSTSNKYN ALKQMNKESK SSVVVKSVDP
INYEWQQIFN SHESCDSKWI SFNAEGLRAD LESKLIGQHI ASSIILKAVE GFMSDTNPQK
PLVLSLHGPS GTGKNFVSKL IAGNIYKEGM DSSFVHIFIS TYHFPHQGHV DLYKTQLQQW
IKDKITHCEH SMFIFDEMDK CPPGLMDSIM PYLGYHNKLD GVSYRKAIFI FLSNAGGEII
TETALKFWKE GKDREEIELK DLETLISATA FNNNNSGFWH SSLIDRNLVD FFVPFLPLQY
GHVIICAMAT MKARGQKPDQ NKAHKLAKDL EYFPKFWEVF SARGCKTVEA RLEFYMMSTS
DGNCSVTMST SNKYNALKQM NKESKSSVVV KSLDPINYEW QQIFNSHESC DSKWISFNAE
GLRADVESKL IGQHIASSII LKAVEGFMSD DNPQKPLVLS LHGPSGTGKN FVSKLIAGNI
YKKGMDSSFV KVFTSTFHFP HKENIDRYKT QLQQWIKDKI THCERSMFIF DEMDKMHPGL
TDSIMPYLGY HNKLDGVSYR KAIFIFLSNA GGEIITETAL KFWKEGKDRE EIELKDLETL
ISATAFNNNN SGFWHSSLID RHLVDFFVPF LPLEYRHVVI CAIAAMKARG QKPDQNKAIK
LAEDLDFFPK FERAFSVRGC KTVEARLEFY T
//