ID TOR3A_HUMAN Reviewed; 397 AA. AC Q9H497; B4DSY0; B7ZB65; Q5M7Y7; Q8WVA7; Q8WWM2; Q9H495; Q9H6E7; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 154. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Lymphoma; 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] (ISOFORMS 1 AND 3), AND VARIANT RP LEU-13. RC TISSUE=Kidney epithelium, Pancreas, and Stomach; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-13. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP LEU-13. RC TISSUE=Cervix, Eye, and Muscle; 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 [6] RP SUBCELLULAR LOCATION, GLYCOSYLATION, SUBUNIT, AND MUTAGENESIS OF GLU-236. RX PubMed=20015956; DOI=10.1093/hmg/ddp557; RA Jungwirth M., Dear M.L., Brown P., Holbrook K., Goodchild R.; RT "Relative tissue expression of homologous torsinB correlates with the RT neuronal specific importance of DYT1 dystonia-associated torsinA."; RL Hum. Mol. Genet. 19:888-900(2010). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- SUBUNIT: May not form homohexamers. {ECO:0000269|PubMed:20015956}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum lumen. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=ADIR1; CC IsoId=Q9H497-1; Sequence=Displayed; CC Name=2; Synonyms=ADIR2; CC IsoId=Q9H497-2; Sequence=VSP_017666, VSP_017667; CC Name=3; CC IsoId=Q9H497-3; Sequence=VSP_017665; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in CC stomach, salivary glands and lymph nodes. Isoform 2 is expressed in CC placenta. {ECO:0000269|PubMed:11863361}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20015956}. CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ299403; CAC13973.1; -; mRNA. DR EMBL; AJ299441; CAC14461.1; -; mRNA. DR EMBL; AJ318044; CAC88129.1; -; Genomic_DNA. DR EMBL; AJ318045; CAC88129.1; JOINED; Genomic_DNA. DR EMBL; AJ318046; CAC88129.1; JOINED; Genomic_DNA. DR EMBL; AJ318047; CAC88129.1; JOINED; Genomic_DNA. DR EMBL; AJ318048; CAC88129.1; JOINED; Genomic_DNA. DR EMBL; AJ318049; CAC88129.1; JOINED; Genomic_DNA. DR EMBL; AJ318044; CAC88130.1; -; Genomic_DNA. DR EMBL; AJ318045; CAC88130.1; JOINED; Genomic_DNA. DR EMBL; AJ318046; CAC88130.1; JOINED; Genomic_DNA. DR EMBL; AJ318047; CAC88130.1; JOINED; Genomic_DNA. DR EMBL; AJ318048; CAC88130.1; JOINED; Genomic_DNA. DR EMBL; AJ318050; CAC88130.1; JOINED; Genomic_DNA. DR EMBL; AK025998; BAB15312.1; -; mRNA. DR EMBL; CR457354; CAG33635.1; -; mRNA. DR EMBL; AK299966; BAG61792.1; -; mRNA. DR EMBL; AK316530; BAH14901.1; -; mRNA. DR EMBL; AL139132; CAH70928.1; -; Genomic_DNA. DR EMBL; AL139132; CAH70929.1; -; Genomic_DNA. DR EMBL; BC001085; AAH01085.1; -; mRNA. DR EMBL; BC007571; AAH07571.1; -; mRNA. DR EMBL; BC011746; AAH11746.1; -; mRNA. DR EMBL; BC018292; AAH18292.1; -; mRNA. DR EMBL; BC088368; AAH88368.1; -; mRNA. DR CCDS; CCDS1329.1; -. [Q9H497-1] DR RefSeq; NP_071766.2; NM_022371.3. [Q9H497-1] DR AlphaFoldDB; Q9H497; -. DR SMR; Q9H497; -. DR BioGRID; 122112; 130. DR DIP; DIP-59333N; -. DR IntAct; Q9H497; 17. DR MINT; Q9H497; -. DR STRING; 9606.ENSP00000356599; -. DR GlyCosmos; Q9H497; 1 site, No reported glycans. DR GlyGen; Q9H497; 2 sites. DR iPTMnet; Q9H497; -. DR PhosphoSitePlus; Q9H497; -. DR BioMuta; TOR3A; -. DR DMDM; 74752636; -. DR EPD; Q9H497; -. DR jPOST; Q9H497; -. DR MassIVE; Q9H497; -. DR MaxQB; Q9H497; -. DR PaxDb; 9606-ENSP00000356599; -. DR PeptideAtlas; Q9H497; -. DR ProteomicsDB; 80801; -. [Q9H497-1] DR ProteomicsDB; 80802; -. [Q9H497-2] DR ProteomicsDB; 80803; -. [Q9H497-3] DR Pumba; Q9H497; -. DR Antibodypedia; 20580; 158 antibodies from 24 providers. DR DNASU; 64222; -. DR Ensembl; ENST00000352445.10; ENSP00000335351.6; ENSG00000186283.14. [Q9H497-2] DR Ensembl; ENST00000367627.8; ENSP00000356599.3; ENSG00000186283.14. [Q9H497-1] DR GeneID; 64222; -. DR KEGG; hsa:64222; -. DR MANE-Select; ENST00000367627.8; ENSP00000356599.3; NM_022371.4; NP_071766.2. DR UCSC; uc001gmd.4; human. [Q9H497-1] DR AGR; HGNC:11997; -. DR CTD; 64222; -. DR DisGeNET; 64222; -. DR GeneCards; TOR3A; -. DR HGNC; HGNC:11997; TOR3A. DR HPA; ENSG00000186283; Low tissue specificity. DR MIM; 607555; gene. DR neXtProt; NX_Q9H497; -. DR OpenTargets; ENSG00000186283; -. DR PharmGKB; PA36678; -. DR VEuPathDB; HostDB:ENSG00000186283; -. DR eggNOG; KOG2170; Eukaryota. DR GeneTree; ENSGT00950000182888; -. DR HOGENOM; CLU_053537_0_0_1; -. DR InParanoid; Q9H497; -. DR OMA; VARMMVF; -. DR OrthoDB; 5087at2759; -. DR PhylomeDB; Q9H497; -. DR TreeFam; TF314941; -. DR PathwayCommons; Q9H497; -. DR SignaLink; Q9H497; -. DR BioGRID-ORCS; 64222; 26 hits in 1161 CRISPR screens. DR ChiTaRS; TOR3A; human. DR GenomeRNAi; 64222; -. DR Pharos; Q9H497; Tbio. DR PRO; PR:Q9H497; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9H497; Protein. DR Bgee; ENSG00000186283; Expressed in oocyte and 189 other cell types or tissues. DR ExpressionAtlas; Q9H497; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. 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; IDA:UniProtKB. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR049337; TOR1A_C. DR InterPro; IPR010448; Torsin. DR PANTHER; PTHR10760; TORSIN; 1. DR PANTHER; PTHR10760:SF3; TORSIN-3A; 1. DR Pfam; PF21376; TOR1A_C; 1. DR Pfam; PF06309; Torsin; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q9H497; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cytoplasm; Endoplasmic reticulum; KW Glycoprotein; Nucleotide-binding; Reference proteome; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..397 FT /note="Torsin-3A" FT /id="PRO_0000228147" FT BINDING 167..174 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT CARBOHYD 122 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..216 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_017665" FT VAR_SEQ 315..336 FT /note="DNGFGHSRLVKENLIDYFIPFL -> GFSFLTTRWPHLDLPTSSVAPT (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:11863361" FT /id="VSP_017666" FT VAR_SEQ 337..397 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11863361" FT /id="VSP_017667" FT VARIANT 13 FT /note="F -> L (in dbSNP:rs2296377)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_025697" FT MUTAGEN 236 FT /note="E->Q: No effect on subcellular location." FT /evidence="ECO:0000269|PubMed:20015956" FT CONFLICT 272 FT /note="L -> P (in Ref. 5; AAH18292)" FT /evidence="ECO:0000305" SQ SEQUENCE 397 AA; 46199 MW; 459CD18EA22709FE CRC64; MLRGPWRQLW LFFLLLLPGA PEPRGASRPW EGTDEPGSAW AWPGFQRLQE QLRAAGALSK RYWTLFSCQV WPDDCDEDEE AATGPLGWRL PLLGQRYLDL LTTWYCSFKD CCPRGDCRIS NNFTGLEWDL NVRLHGQHLV QQLVLRTVRG YLETPQPEKA LALSFHGWSG TGKNFVARML VENLYRDGLM SDCVRMFIAT FHFPHPKYVD LYKEQLMSQI RETQQLCHQT LFIFDEAEKL HPGLLEVLGP HLERRAPEGH RAESPWTIFL FLSNLRGDII NEVVLKLLKA GWSREEITME HLEPHLQAEI VETIDNGFGH SRLVKENLID YFIPFLPLEY RHVRLCARDA FLSQELLYKE ETLDEIAQMM VYVPKEEQLF SSQGCKSISQ RINYFLS //