TORS_DROME
ID TORS_DROME Reviewed; 340 AA.
AC O77277; B4F5H4; B4F5H5; B4F5H6; B4F5I2; C0MLF3; C0MLF6; C0MLG2; Q8T037;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Torsin-like protein;
DE Flags: Precursor;
GN Name=Torsin; Synonyms=torp4a; ORFNames=CG3024;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-14; MET-30; SER-118;
RP LEU-125; PHE-138 AND ASN-226.
RC STRAIN=ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL229, ZBMEL377, ZBMEL384,
RC ZBMEL398, ZBMEL82, ZBMEL84, and ZBMEL95;
RX PubMed=18477586; DOI=10.1093/molbev/msn111;
RA Baines J.F., Sawyer S.A., Hartl D.L., Parsch J.;
RT "Effects of X-linkage and sex-biased gene expression on the rate of
RT adaptive protein evolution in Drosophila.";
RL Mol. Biol. Evol. 25:1639-1650(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-30; PHE-138; LYS-152;
RP ASN-163 AND ASN-226.
RC STRAIN=MEL01, MEL02, MEL11, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17,
RC MEL18, MEL19, and MEL20;
RX PubMed=19126864; DOI=10.1093/molbev/msn297;
RA Parsch J., Zhang Z., Baines J.F.;
RT "The influence of demography and weak selection on the McDonald-Kreitman
RT test: an empirical study in Drosophila.";
RL Mol. Biol. Evol. 26:691-698(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chou J., Gusella J.F.;
RT "A Drosophila homolog of human torsinA, gene responsible for primary
RT torsion dystornia.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May serve as a molecular chaperone assisting in the proper
CC folding of secreted and/or membrane proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF60321.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL39737.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA21132.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AM999060; CAQ53422.1; -; Genomic_DNA.
DR EMBL; AM999061; CAQ53423.1; -; Genomic_DNA.
DR EMBL; AM999062; CAQ53424.1; -; Genomic_DNA.
DR EMBL; AM999063; CAQ53425.1; -; Genomic_DNA.
DR EMBL; AM999064; CAQ53426.1; -; Genomic_DNA.
DR EMBL; AM999065; CAQ53427.1; -; Genomic_DNA.
DR EMBL; AM999066; CAQ53428.1; -; Genomic_DNA.
DR EMBL; AM999067; CAQ53429.1; -; Genomic_DNA.
DR EMBL; AM999068; CAQ53430.1; -; Genomic_DNA.
DR EMBL; AM999069; CAQ53431.1; -; Genomic_DNA.
DR EMBL; FM246173; CAR94099.1; -; Genomic_DNA.
DR EMBL; FM246174; CAR94100.1; -; Genomic_DNA.
DR EMBL; FM246175; CAR94101.1; -; Genomic_DNA.
DR EMBL; FM246176; CAR94102.1; -; Genomic_DNA.
DR EMBL; FM246177; CAR94103.1; -; Genomic_DNA.
DR EMBL; FM246178; CAR94104.1; -; Genomic_DNA.
DR EMBL; FM246179; CAR94105.1; -; Genomic_DNA.
DR EMBL; FM246180; CAR94106.1; -; Genomic_DNA.
DR EMBL; FM246181; CAR94107.1; -; Genomic_DNA.
DR EMBL; FM246182; CAR94108.1; -; Genomic_DNA.
DR EMBL; FM246183; CAR94109.1; -; Genomic_DNA.
DR EMBL; FM246184; CAR94110.1; -; Genomic_DNA.
DR EMBL; AF236156; AAF60321.1; ALT_INIT; mRNA.
DR EMBL; AE014298; AAF45969.2; -; Genomic_DNA.
DR EMBL; AL031766; CAA21132.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY069592; AAL39737.2; ALT_INIT; mRNA.
DR EMBL; BT003553; AAO39557.1; -; mRNA.
DR RefSeq; NP_001284866.1; NM_001297937.1.
DR RefSeq; NP_572178.1; NM_131950.4.
DR AlphaFoldDB; O77277; -.
DR SMR; O77277; -.
DR BioGRID; 57916; 6.
DR STRING; 7227.FBpp0070658; -.
DR GlyGen; O77277; 2 sites.
DR PaxDb; O77277; -.
DR DNASU; 31399; -.
DR EnsemblMetazoa; FBtr0070690; FBpp0070658; FBgn0025615.
DR EnsemblMetazoa; FBtr0345715; FBpp0311758; FBgn0025615.
DR GeneID; 31399; -.
DR KEGG; dme:Dmel_CG3024; -.
DR UCSC; CG3024-RA; d. melanogaster.
DR CTD; 31399; -.
DR FlyBase; FBgn0025615; Torsin.
DR VEuPathDB; VectorBase:FBgn0025615; -.
DR eggNOG; KOG2170; Eukaryota.
DR GeneTree; ENSGT00950000182888; -.
DR HOGENOM; CLU_053537_0_0_1; -.
DR InParanoid; O77277; -.
DR OMA; CCDDRSI; -.
DR OrthoDB; 1453168at2759; -.
DR PhylomeDB; O77277; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR BioGRID-ORCS; 31399; 2 hits in 3 CRISPR screens.
DR GenomeRNAi; 31399; -.
DR PRO; PR:O77277; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0025615; Expressed in embryonic/larval hemocyte (Drosophila) and 27 other tissues.
DR ExpressionAtlas; O77277; baseline and differential.
DR Genevisible; O77277; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:FlyBase.
DR GO; GO:0106083; C:nuclear membrane protein complex; IGI:FlyBase.
DR GO; GO:0005524; F:ATP binding; ISM:FlyBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:FlyBase.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:FlyBase.
DR GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:InterPro.
DR GO; GO:0008057; P:eye pigment granule organization; IMP:FlyBase.
DR GO; GO:0007504; P:larval fat body development; IMP:FlyBase.
DR GO; GO:0046467; P:membrane lipid biosynthetic process; IMP:FlyBase.
DR GO; GO:1903741; P:negative regulation of phosphatidate phosphatase activity; IMP:FlyBase.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:FlyBase.
DR GO; GO:0140591; P:nuclear envelope budding; IMP:FlyBase.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:FlyBase.
DR GO; GO:0043104; P:positive regulation of GTP cyclohydrolase I activity; IMP:FlyBase.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; IMP:FlyBase.
DR GO; GO:0010883; P:regulation of lipid storage; IMP:FlyBase.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:FlyBase.
DR GO; GO:0099050; P:vesicle scission; IMP:FlyBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010448; Torsin.
DR InterPro; IPR030553; Torsin-like.
DR InterPro; IPR017378; Torsin_1/2.
DR PANTHER; PTHR10760; PTHR10760; 1.
DR PANTHER; PTHR10760:SF2; PTHR10760:SF2; 1.
DR Pfam; PF06309; Torsin; 1.
DR PIRSF; PIRSF038079; Torsin_2A; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..340
FT /note="Torsin-like protein"
FT /id="PRO_0000005512"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 14
FT /note="V -> G (in strain: ZBMEL384)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT VARIANT 30
FT /note="I -> M (in strain: MEL14 and ZBMEL384)"
FT /evidence="ECO:0000269|PubMed:18477586,
FT ECO:0000269|PubMed:19126864"
FT VARIANT 118
FT /note="A -> S (in strain: ZBMEL82, ZBMEL95, ZBMEL131,
FT ZBMEL145, ZBMEL157, ZBMEL229, ZBMEL377 and ZBMEL398)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT VARIANT 125
FT /note="M -> L (in strain: ZBMEL82, ZBMEL95, ZBMEL131,
FT ZBMEL145, ZBMEL157, ZBMEL229, ZBMEL377 and ZBMEL398)"
FT /evidence="ECO:0000269|PubMed:18477586"
FT VARIANT 138
FT /note="Y -> F (in strain: MEL14, ZBMEL82, ZBMEL95,
FT ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL229, ZBMEL377 and
FT ZBMEL398)"
FT /evidence="ECO:0000269|PubMed:18477586,
FT ECO:0000269|PubMed:19126864"
FT VARIANT 152
FT /note="N -> K (in strain: MEL20)"
FT /evidence="ECO:0000269|PubMed:19126864"
FT VARIANT 163
FT /note="D -> N (in strain: MEL11 and MEL13)"
FT /evidence="ECO:0000269|PubMed:19126864"
FT VARIANT 226
FT /note="S -> N (in strain: MEL14, ZBMEL82, ZBMEL131,
FT ZBMEL145, ZBMEL157, ZBMEL229, ZBMEL377, ZBMEL384 and
FT ZBMEL398)"
FT /evidence="ECO:0000269|PubMed:18477586,
FT ECO:0000269|PubMed:19126864"
SQ SEQUENCE 340 AA; 38170 MW; 942F05D3C2ACE7A8 CRC64;
MMSFPRMLSL CLSVLVILPL PLQSVDPLTI GAVGAVALGA YFKEHTYCRF AECCDDRNIP
ARIDELERSL ERTLIGQHIV RQHIVPALKA HIASGNKSRK PLVISFHGQP GTGKNFVAEQ
IADAMYLKGS RSNYVTKYLG QADFPKESEV SNYRVKINNA VRDTLRSCPR SLFIFDEVDK
MPSGVFDQLT SLVDYNAFVD GTDNTKAIFI FLSNTAGSHI ASHLGSVMKN GRLREDTRLS
DFEPLLRKAA YNMDGGMKKT TMIESHVIDH FIPFLPMEKA HVIKCLEAEL LRWRRDPKQA
NNQKIIEDII NSSISYDRTH SLFAISGCKT LEKKVAMAIY
