TOR3A_MOUSE
ID TOR3A_MOUSE Reviewed; 385 AA.
AC Q9ER38; Q3T9Q6; Q3TDA9; Q3U5X1; Q3U8F2; Q9CR17; Q9CU67;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Torsin-3A;
DE AltName: Full=ATP-dependent interferon-responsive protein;
DE AltName: Full=Torsin family 3 member A;
DE Flags: Precursor;
GN Name=Tor3a; Synonyms=Adir;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND VARIANT HIS-94.
RC TISSUE=Oropharynx, and Spleen;
RX PubMed=11863361; DOI=10.1006/geno.2002.6709;
RA Dron M., Meritet J.F., Dandoy-Dron F., Meyniel J.P., Maury C., Tovey M.G.;
RT "Molecular cloning of ADIR, a novel interferon responsive gene encoding a
RT protein related to the torsins.";
RL Genomics 79:315-325(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Pancreas, Spleen, Thymus, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH TOR1AIP1, AND DEVELOPMENTAL STAGE.
RX PubMed=16364897; DOI=10.1016/j.neuron.2005.11.010;
RA Goodchild R.E., Kim C.E., Dauer W.T.;
RT "Loss of the dystonia-associated protein torsinA selectively disrupts the
RT neuronal nuclear envelope.";
RL Neuron 48:923-932(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBUNIT: Interacts with TOR1AIP1. {ECO:0000269|PubMed:16364897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum lumen
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: At 16 dpc, widely expressed with very low levels
CC in heart, liver and neural tissues. {ECO:0000269|PubMed:16364897}.
CC -!- INDUCTION: By interferon-alpha and interferon-gamma, in spleen and
CC liver. {ECO:0000269|PubMed:11863361}.
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; AJ299404; CAC13978.1; -; mRNA.
DR EMBL; AK007814; BAB25279.1; -; mRNA.
DR EMBL; AK009693; BAB26443.1; -; mRNA.
DR EMBL; AK017908; BAB30998.1; -; mRNA.
DR EMBL; AK151048; BAE30065.1; -; mRNA.
DR EMBL; AK152243; BAE31066.1; -; mRNA.
DR EMBL; AK152358; BAE31149.1; -; mRNA.
DR EMBL; AK152484; BAE31256.1; -; mRNA.
DR EMBL; AK153391; BAE31955.1; -; mRNA.
DR EMBL; AK170296; BAE41695.1; -; mRNA.
DR EMBL; AK172355; BAE42964.1; -; mRNA.
DR EMBL; BC071216; AAH71216.1; -; mRNA.
DR CCDS; CCDS15394.1; -.
DR RefSeq; NP_075630.2; NM_023141.2.
DR AlphaFoldDB; Q9ER38; -.
DR SMR; Q9ER38; -.
DR BioGRID; 206012; 4.
DR STRING; 10090.ENSMUSP00000078572; -.
DR GlyConnect; 2775; 2 N-Linked glycans (1 site).
DR GlyGen; Q9ER38; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9ER38; -.
DR PhosphoSitePlus; Q9ER38; -.
DR EPD; Q9ER38; -.
DR MaxQB; Q9ER38; -.
DR PaxDb; Q9ER38; -.
DR PeptideAtlas; Q9ER38; -.
DR PRIDE; Q9ER38; -.
DR ProteomicsDB; 260653; -.
DR Antibodypedia; 20580; 141 antibodies from 23 providers.
DR DNASU; 30935; -.
DR Ensembl; ENSMUST00000079625; ENSMUSP00000078572; ENSMUSG00000060519.
DR Ensembl; ENSMUST00000122242; ENSMUSP00000113984; ENSMUSG00000060519.
DR Ensembl; ENSMUST00000188964; ENSMUSP00000140079; ENSMUSG00000060519.
DR GeneID; 30935; -.
DR KEGG; mmu:30935; -.
DR UCSC; uc007dcn.2; mouse.
DR CTD; 64222; -.
DR MGI; MGI:1353652; Tor3a.
DR VEuPathDB; HostDB:ENSMUSG00000060519; -.
DR eggNOG; KOG2170; Eukaryota.
DR GeneTree; ENSGT00950000182888; -.
DR HOGENOM; CLU_053537_0_0_1; -.
DR InParanoid; Q9ER38; -.
DR OMA; EIAQMMV; -.
DR OrthoDB; 1453168at2759; -.
DR PhylomeDB; Q9ER38; -.
DR TreeFam; TF314941; -.
DR BioGRID-ORCS; 30935; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Tor3a; mouse.
DR PRO; PR:Q9ER38; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9ER38; protein.
DR Bgee; ENSMUSG00000060519; Expressed in mucous cell of stomach and 211 other tissues.
DR ExpressionAtlas; Q9ER38; baseline and differential.
DR Genevisible; Q9ER38; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:MGI.
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; 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; IPR030552; Torsin-3A.
DR PANTHER; PTHR10760; PTHR10760; 1.
DR PANTHER; PTHR10760:SF3; PTHR10760:SF3; 1.
DR Pfam; PF06309; Torsin; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Glycoprotein;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..385
FT /note="Torsin-3A"
FT /id="PRO_0000228148"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 94
FT /note="R -> H"
FT /evidence="ECO:0000269|PubMed:11863361"
FT CONFLICT 8
FT /note="L -> R (in Ref. 2; BAB30998)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="K -> R (in Ref. 2; BAE41695)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="K -> T (in Ref. 1; CAC13978 and 2; BAE42964/
FT BAE41695)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="D -> N (in Ref. 2; BAB30998)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="R -> C (in Ref. 1; CAC13978)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="L -> V (in Ref. 1; CAC13978 and 2; BAE42964/
FT BAE41695)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="D -> G (in Ref. 2; BAE31955/BAE30065)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="C -> R (in Ref. 1; CAC13978)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="P -> PRK (in Ref. 2; BAB30998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 43814 MW; 320754A2C292B292 CRC64;
MFLGALWLLL LLPLRPPGAQ GQEADEPTPW PSVKGLKEQL RKAGALSKRY WELFSCTLWP
DHCEDQETPV PPLGWSLPLW GRRSLDVLTA WLCRFQDCCS GGGDCRISNN LTGLESDLRV
RLHGQHLASK LVLRAVKGYL EMPQVGKALA LSFHGWSGTG KNFLARILMD NLYRDGMRSD
CVKMFISTFH FPHPKYVDTY KEELQRQMQE TQWRCHQSTF VFDEAEKLHP GLLELLEPYL
EPRSPEARGV EAPRAIFLFL SNLGGSVINE VVLSLLKAGW SREEITTQHL EVPLQAEIME
AADSSFGSSG LLKKHLIDHF IPFLPLEYCH VRLCVRDAFL GQDLPYTEET LDEIAKMMTY
VPEEERLFSS QGCKSISQRI NLFLP
