TOIP2_MOUSE
ID TOIP2_MOUSE Reviewed; 502 AA.
AC Q8BYU6; Q6NY10; Q8BJP0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Torsin-1A-interacting protein 2;
GN Name=Tor1aip2; Synonyms=Ifrg15, Lull1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CD-1; TISSUE=Neural stem 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 [3]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=20457914; DOI=10.1073/pnas.0912877107;
RA Kim C.E., Perez A., Perkins G., Ellisman M.H., Dauer W.T.;
RT "A molecular mechanism underlying the neural-specific defect in torsinA
RT mutant mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9861-9866(2010).
CC -!- FUNCTION: Required for endoplasmic reticulum integrity. Regulates the
CC distribution of TOR1A between the endoplasmic reticulum and the nuclear
CC envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TOR1A and TOR1B (ATP-bound). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Nucleus envelope
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Tor1aip2;
CC IsoId=Q8BYU6-1; Sequence=Displayed;
CC Name=Ifrg15;
CC IsoId=Q9ER81-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in the spinal cord and liver (at protein
CC level). {ECO:0000269|PubMed:16364897}.
CC -!- DEVELOPMENTAL STAGE: At 16 dpc, widely expressed with higher expression
CC levels in non-neural cells and hippocampus. In the spinal cord,
CC expressed as early as 12 dpc until p21, the expression levels decrease
CC in the adulthood (at protein level). {ECO:0000269|PubMed:16364897,
CC ECO:0000269|PubMed:20457914}.
CC -!- SIMILARITY: Belongs to the TOR1AIP family. {ECO:0000305}.
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DR EMBL; AK038024; BAC29923.1; -; mRNA.
DR EMBL; AK080959; BAC38096.1; -; mRNA.
DR EMBL; BC066790; AAH66790.1; -; mRNA.
DR CCDS; CCDS15389.1; -. [Q8BYU6-1]
DR RefSeq; NP_766431.3; NM_172843.4. [Q8BYU6-1]
DR RefSeq; XP_006529650.1; XM_006529587.3. [Q8BYU6-1]
DR RefSeq; XP_006529651.1; XM_006529588.3.
DR RefSeq; XP_006529652.1; XM_006529589.3. [Q8BYU6-1]
DR RefSeq; XP_011246305.1; XM_011248003.1. [Q8BYU6-1]
DR RefSeq; XP_017176040.1; XM_017320551.1. [Q8BYU6-1]
DR RefSeq; XP_017176041.1; XM_017320552.1.
DR AlphaFoldDB; Q8BYU6; -.
DR SMR; Q8BYU6; -.
DR BioGRID; 232245; 3.
DR STRING; 10090.ENSMUSP00000107387; -.
DR GlyConnect; 2773; 1 N-Linked glycan (1 site).
DR GlyGen; Q8BYU6; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q8BYU6; -.
DR PhosphoSitePlus; Q8BYU6; -.
DR SwissPalm; Q8BYU6; -.
DR EPD; Q8BYU6; -.
DR jPOST; Q8BYU6; -.
DR PaxDb; Q8BYU6; -.
DR PeptideAtlas; Q8BYU6; -.
DR PRIDE; Q8BYU6; -.
DR ProteomicsDB; 258949; -. [Q8BYU6-1]
DR Antibodypedia; 60527; 75 antibodies from 16 providers.
DR DNASU; 240832; -.
DR Ensembl; ENSMUST00000060404; ENSMUSP00000050817; ENSMUSG00000050565. [Q8BYU6-1]
DR Ensembl; ENSMUST00000111757; ENSMUSP00000107387; ENSMUSG00000050565. [Q8BYU6-1]
DR GeneID; 240832; -.
DR UCSC; uc007dbx.2; mouse. [Q8BYU6-1]
DR CTD; 163590; -.
DR MGI; MGI:3582695; Tor1aip2.
DR VEuPathDB; HostDB:ENSMUSG00000050565; -.
DR eggNOG; ENOG502QUV7; Eukaryota.
DR GeneTree; ENSGT00390000012166; -.
DR HOGENOM; CLU_034263_1_1_1; -.
DR InParanoid; Q8BYU6; -.
DR OMA; DKTEHEN; -.
DR OrthoDB; 575658at2759; -.
DR PhylomeDB; Q8BYU6; -.
DR TreeFam; TF329438; -.
DR BioGRID-ORCS; 240832; 7 hits in 69 CRISPR screens.
DR ChiTaRS; Tor1aip2; mouse.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BYU6; protein.
DR Bgee; ENSMUSG00000050565; Expressed in placenta labyrinth and 278 other tissues.
DR ExpressionAtlas; Q8BYU6; baseline and differential.
DR Genevisible; Q8BYU6; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; ISO:MGI.
DR Gene3D; 3.40.50.12190; -; 1.
DR InterPro; IPR038599; LAP1C-like_C_sf.
DR InterPro; IPR008662; TOIP1/2.
DR PANTHER; PTHR18843; PTHR18843; 2.
DR Pfam; PF05609; LAP1C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..502
FT /note="Torsin-1A-interacting protein 2"
FT /id="PRO_0000228839"
FT TOPO_DOM 1..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..502
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..502
FT /note="Interaction with TOR1A"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 361
FT /note="S -> P (in Ref. 2; AAH66790)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="D -> G (in Ref. 2; AAH66790)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="E -> G (in Ref. 1; BAC38096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 54496 MW; 7E3290BBCCB5471A CRC64;
MSQSLKSQNT NMSDSGCRDP VGDSQNVLEN DPSINSQTQD TRVTPNNTAE AQPLQPTSDL
KEDHHEIGAR AQEHTDTGDR SESPEEPALE KPPLDKAELE SSPSSQDTEL GHHPHSEHGG
GDALDLDPNC SQSDLGGRAD AHLESSSVAS PEGAGDRGEA DEHLESSSAA PTEGAGDRGE
AGQELLAEDS TDGQSLGHSN TGPGNQDSLR RRLPVPEAGS HEEETELVKE KQEVAQDTLR
KTDKKSLWTY GSVFLGCLIV AVVLSSVNSY YSSPAQQVPQ NPALEAFLAQ FGQLKEKFPG
QSSFLWQRGR KFLQKHLNAS NPSEPATIIF TAAREGKETL KCLSYHVANA YTSSQKVTAV
SIDGAERALQ DSDTVKLLVD LELSDGFENG HKAAVVHHFE SLPAGSTLIF YKYCDHENAA
FKDVALVLTV LLEEETLEAS VSPREIEEKV RDLLWAKFTN SESPTSYSHM DSDKLSGLWS
RISHLVLPVQ PVRNIEERGC LL
