TOR2A_HUMAN
ID TOR2A_HUMAN Reviewed; 321 AA.
AC Q5JU69; A4FU12; A4FU13; Q3ZCN9; Q3ZCP0; Q5JU68; Q66K87; Q6UXW6; Q8NAN5;
AC Q96SL7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Torsin-2A;
DE AltName: Full=Torsin family 2 member A;
DE AltName: Full=Torsin-related protein 1;
DE Flags: Precursor;
GN Name=TOR2A; Synonyms=TORP1; ORFNames=UNQ6408/PRO21181;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-203.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Peripheral blood monocyte, and Placenta;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=B-cell;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=12910263; DOI=10.1038/nm913;
RA Shichiri M., Ishimaru S., Ota T., Nishikawa T., Isogai T., Hirata Y.;
RT "Salusins: newly identified bioactive peptides with hemodynamic and
RT mitogenic activities.";
RL Nat. Med. 9:1166-1172(2003).
CC -!- SUBUNIT: Homohexamer. Interacts with TOR1AIP1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5JU69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JU69-2; Sequence=VSP_017703, VSP_017704;
CC Name=3;
CC IsoId=Q5JU69-5; Sequence=VSP_035631, VSP_035632;
CC Name=4;
CC IsoId=Q8N2E6-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed ubiquitously, except in
CC cardiac and endothelial tissues. {ECO:0000269|PubMed:12910263}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH80527.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAI00908.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI00909.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI00910.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI00911.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={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; AY358180; AAQ88547.1; -; mRNA.
DR EMBL; AK027677; BAB55288.1; -; mRNA.
DR EMBL; AL162426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC100907; AAI00908.2; ALT_SEQ; mRNA.
DR EMBL; BC100908; AAI00909.2; ALT_SEQ; mRNA.
DR EMBL; BC100909; AAI00910.2; ALT_SEQ; mRNA.
DR EMBL; BC100910; AAI00911.2; ALT_SEQ; mRNA.
DR EMBL; BC080527; AAH80527.2; ALT_SEQ; mRNA.
DR CCDS; CCDS43879.1; -. [Q5JU69-1]
DR CCDS; CCDS48025.1; -. [Q5JU69-5]
DR CCDS; CCDS6876.1; -. [Q5JU69-2]
DR RefSeq; NP_001078816.1; NM_001085347.2. [Q5JU69-1]
DR RefSeq; NP_001127902.1; NM_001134430.2.
DR RefSeq; NP_001127903.1; NM_001134431.2. [Q5JU69-5]
DR RefSeq; NP_001238947.1; NM_001252018.1.
DR RefSeq; NP_001238950.1; NM_001252021.1.
DR RefSeq; NP_001238952.1; NM_001252023.1.
DR RefSeq; NP_569726.2; NM_130459.3. [Q5JU69-2]
DR AlphaFoldDB; Q5JU69; -.
DR SMR; Q5JU69; -.
DR BioGRID; 118167; 31.
DR DIP; DIP-59332N; -.
DR IntAct; Q5JU69; 3.
DR STRING; 9606.ENSP00000362381; -.
DR GlyConnect; 1825; 2 N-Linked glycans (1 site).
DR GlyGen; Q5JU69; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q5JU69; -.
DR PhosphoSitePlus; Q5JU69; -.
DR BioMuta; TOR2A; -.
DR DMDM; 74742272; -.
DR EPD; Q5JU69; -.
DR jPOST; Q5JU69; -.
DR MassIVE; Q5JU69; -.
DR MaxQB; Q5JU69; -.
DR PaxDb; Q5JU69; -.
DR PeptideAtlas; Q5JU69; -.
DR PRIDE; Q5JU69; -.
DR ProteomicsDB; 63257; -. [Q5JU69-1]
DR ProteomicsDB; 63258; -. [Q5JU69-2]
DR Antibodypedia; 30786; 144 antibodies from 22 providers.
DR DNASU; 27433; -.
DR Ensembl; ENST00000373281.8; ENSP00000362378.5; ENSG00000160404.18. [Q5JU69-2]
DR Ensembl; ENST00000373284.10; ENSP00000362381.5; ENSG00000160404.18. [Q5JU69-1]
DR Ensembl; ENST00000463256.5; ENSP00000485648.1; ENSG00000160404.18. [Q5JU69-5]
DR Ensembl; ENST00000463577.2; ENSP00000485268.1; ENSG00000160404.18. [Q5JU69-5]
DR Ensembl; ENST00000493439.1; ENSP00000485360.1; ENSG00000160404.18. [Q5JU69-5]
DR Ensembl; ENST00000496460.5; ENSP00000485544.1; ENSG00000160404.18. [Q5JU69-5]
DR GeneID; 27433; -.
DR KEGG; hsa:27433; -.
DR MANE-Select; ENST00000373284.10; ENSP00000362381.5; NM_001085347.3; NP_001078816.2.
DR UCSC; uc004brs.5; human. [Q5JU69-1]
DR CTD; 27433; -.
DR DisGeNET; 27433; -.
DR GeneCards; TOR2A; -.
DR HGNC; HGNC:11996; TOR2A.
DR HPA; ENSG00000160404; Low tissue specificity.
DR MIM; 608052; gene.
DR neXtProt; NX_Q5JU69; -.
DR OpenTargets; ENSG00000160404; -.
DR PharmGKB; PA36677; -.
DR VEuPathDB; HostDB:ENSG00000160404; -.
DR eggNOG; KOG2170; Eukaryota.
DR GeneTree; ENSGT00950000182888; -.
DR HOGENOM; CLU_053537_0_0_1; -.
DR InParanoid; Q5JU69; -.
DR OMA; HQFSPIV; -.
DR OrthoDB; 611758at2759; -.
DR PhylomeDB; Q5JU69; -.
DR TreeFam; TF314941; -.
DR PathwayCommons; Q5JU69; -.
DR SignaLink; Q5JU69; -.
DR BioGRID-ORCS; 27433; 167 hits in 1088 CRISPR screens.
DR ChiTaRS; TOR2A; human.
DR GeneWiki; TOR2A; -.
DR GenomeRNAi; 27433; -.
DR Pharos; Q5JU69; Tbio.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5JU69; protein.
DR Bgee; ENSG00000160404; Expressed in oocyte and 108 other tissues.
DR ExpressionAtlas; Q5JU69; baseline and differential.
DR Genevisible; Q5JU69; HS.
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; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010448; Torsin.
DR InterPro; IPR017378; Torsin_1/2.
DR PANTHER; PTHR10760; PTHR10760; 1.
DR Pfam; PF06309; Torsin; 1.
DR PIRSF; PIRSF038079; Torsin_2A; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Endoplasmic reticulum; Glycoprotein;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..321
FT /note="Torsin-2A"
FT /id="PRO_0000228829"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 51..72
FT /note="GLECDLAQHLAGQHLAKALVVK -> EGSEELGPREPHCLWPLPLPLR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035631"
FT VAR_SEQ 73..321
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035632"
FT VAR_SEQ 198..253
FT /note="SNTGGKQINQVALEAWRSRRDREEILLQELEPVISRAVLDNPHHGFSNSGIM
FT EERL -> RWGPALQWAQWGGHFSEVQLYSLSLCSQQNPVPHGLSWAFPVPSATLRDDI
FT VIPPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017703"
FT VAR_SEQ 254..321
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017704"
FT VARIANT 203
FT /note="K -> E (in dbSNP:rs538066)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_055661"
FT CONFLICT Q5JU69-2:208
FT /note="W -> C (in Ref. 2; BAB55288)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35714 MW; 93F4DACF3CA0EA02 CRC64;
MAAATRGCRP WGSLLGLLGL VSAAAAAWDL ASLRCTLGAF CECDFRPDLP GLECDLAQHL
AGQHLAKALV VKALKAFVRD PAPTKPLVLS LHGWTGTGKS YVSSLLAHYL FQGGLRSPRV
HHFSPVLHFP HPSHIERYKK DLKSWVQGNL TACGRSLFLF DEMDKMPPGL MEVLRPFLGS
SWVVYGTNYR KAIFIFISNT GGKQINQVAL EAWRSRRDRE EILLQELEPV ISRAVLDNPH
HGFSNSGIME ERLLDAVVPF LPLQRHHVRH CVLNELAQLG LEPRDEVVQA VLDSTTFFPE
DEQLFSSNGC KTVASRIAFF L
