TOIP1_MOUSE
ID TOIP1_MOUSE Reviewed; 595 AA.
AC Q921T2; E9QLK1; Q1EQW1; Q3U7A4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Torsin-1A-interacting protein 1;
DE AltName: Full=Lamina-associated polypeptide 1B;
DE Short=LAP1B;
GN Name=Tor1aip1;
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] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Komoto S., Takasaki Y., Ando S.;
RT "cDNA cloning of mouse lamina-associated polypeptide 1B.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-520 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-151, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, 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 [9]
RP FUNCTION IN NUCLEAR ENVELOPE INTEGRITY, INTERACTION WITH TOR1A; TOR1B;
RP TOR2A AND TOR3A, DISRUPTION PHENOTYPE, AND 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 nuclear membrane integrity. Induces TOR1A and
CC TOR1B ATPase activity and is required for their location on the nuclear
CC membrane. Binds to A- and B-type lamins. Possible role in membrane
CC attachment and assembly of the nuclear lamina.
CC {ECO:0000269|PubMed:20457914}.
CC -!- SUBUNIT: Interacts with ATP1B4. Interacts with TOR1A (ATP-bound).
CC Interacts with TOR1B, TOR2A and TOR3A. Interacts with VIM.
CC {ECO:0000269|PubMed:20457914}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q921T2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q921T2-2; Sequence=VSP_042953;
CC Name=3;
CC IsoId=Q921T2-3; Sequence=VSP_042952;
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 high expression
CC levels in hippocampus and low levels in heart. 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 -!- DISRUPTION PHENOTYPE: Mutant mice exhibit perinatal mortality,
CC typically dying on the last prenatal or first postnatal day. All
CC tissues tested exhibit nuclear membrane abnormalities with membranous
CC vesicle-appearing structures observed in the perinuclear space of
CC neurons. {ECO:0000269|PubMed:20457914}.
CC -!- SIMILARITY: Belongs to the TOR1AIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE31466.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB251963; BAE94915.1; -; mRNA.
DR EMBL; AC159964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010841; AAH10841.1; -; mRNA.
DR EMBL; AK152751; BAE31466.1; ALT_INIT; mRNA.
DR CCDS; CCDS15387.1; -. [Q921T2-3]
DR CCDS; CCDS48402.1; -. [Q921T2-2]
DR RefSeq; NP_001153490.1; NM_001160018.1. [Q921T2-2]
DR RefSeq; NP_001153491.1; NM_001160019.1.
DR RefSeq; NP_659040.2; NM_144791.2. [Q921T2-3]
DR AlphaFoldDB; Q921T2; -.
DR SMR; Q921T2; -.
DR BioGRID; 228970; 36.
DR DIP; DIP-56693N; -.
DR IntAct; Q921T2; 35.
DR GlyConnect; 2772; 3 N-Linked glycans (1 site).
DR GlyGen; Q921T2; 1 site, 3 N-linked glycans (1 site).
DR iPTMnet; Q921T2; -.
DR PhosphoSitePlus; Q921T2; -.
DR SwissPalm; Q921T2; -.
DR EPD; Q921T2; -.
DR jPOST; Q921T2; -.
DR MaxQB; Q921T2; -.
DR PaxDb; Q921T2; -.
DR PeptideAtlas; Q921T2; -.
DR PRIDE; Q921T2; -.
DR ProteomicsDB; 259488; -. [Q921T2-1]
DR ProteomicsDB; 259489; -. [Q921T2-2]
DR ProteomicsDB; 259490; -. [Q921T2-3]
DR Antibodypedia; 34423; 118 antibodies from 27 providers.
DR Ensembl; ENSMUST00000027738; ENSMUSP00000027738; ENSMUSG00000026466. [Q921T2-3]
DR Ensembl; ENSMUST00000097527; ENSMUSP00000095134; ENSMUSG00000026466. [Q921T2-2]
DR GeneID; 208263; -.
DR KEGG; mmu:208263; -.
DR UCSC; uc007dbu.2; mouse. [Q921T2-3]
DR UCSC; uc007dbw.2; mouse. [Q921T2-2]
DR CTD; 26092; -.
DR MGI; MGI:3582693; Tor1aip1.
DR VEuPathDB; HostDB:ENSMUSG00000026466; -.
DR eggNOG; ENOG502QUV7; Eukaryota.
DR GeneTree; ENSGT00390000012166; -.
DR HOGENOM; CLU_034263_0_1_1; -.
DR InParanoid; Q921T2; -.
DR OMA; FSEEGDT; -.
DR OrthoDB; 575658at2759; -.
DR TreeFam; TF329438; -.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR BioGRID-ORCS; 208263; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tor1aip1; mouse.
DR PRO; PR:Q921T2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q921T2; protein.
DR Bgee; ENSMUSG00000026466; Expressed in spermatid and 241 other tissues.
DR ExpressionAtlas; Q921T2; baseline and differential.
DR Genevisible; Q921T2; MM.
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; IDA:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0005521; F:lamin binding; ISO:MGI.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0071763; P:nuclear membrane organization; IMP:MGI.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IMP:MGI.
DR Gene3D; 3.40.50.12190; -; 1.
DR InterPro; IPR038599; LAP1C-like_C_sf.
DR InterPro; IPR008662; TOIP1/2.
DR PANTHER; PTHR18843; PTHR18843; 1.
DR Pfam; PF05609; LAP1C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Glycoprotein; Isopeptide bond; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..595
FT /note="Torsin-1A-interacting protein 1"
FT /id="PRO_0000228836"
FT TOPO_DOM 1..351
FT /note="Nuclear"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..595
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..595
FT /note="Interaction with TOR1A"
FT /evidence="ECO:0000250"
FT COILED 373..400
FT /evidence="ECO:0000255"
FT COMPBIAS 48..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQX1"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQX1"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQX1"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 321
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT VAR_SEQ 260..335
FT /note="DEATPAAGNHPDSLRGLPHNQDFPAHENQPLLLTSGCQENPQEWVDRAVRMR
FT SRMAYNNIQKSNFGNQSPSTSRPQ -> E (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042952"
FT VAR_SEQ 261..279
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_042953"
FT CONFLICT 108
FT /note="S -> A (in Ref. 4; BAE31466)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="D -> N (in Ref. 1; BAE94915 and 3; AAH10841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 66781 MW; 8456CF717594ED53 CRC64;
MAGERWQAEG PGEGWAIYVT PRAPIREGRR RLDPRNGDSS DAPAYGAHPS RRGRREVRFS
EEPAEVYGDF EPRAAKERSP GGRRTPPEKF RPASAGEEVR ESAYNLRSRP RRQRRAQEAE
EMKTRRSARL EQHSQQPQLS PATSGRGLRD SPSSSEDREE DEPSSRPVTS QTASKKTLRT
PEASVMNEDP ISNLCRPPLR SPRLDSTYQT NGNTKTNERE ATIVQQVNFF EEGETEDDLE
SSYSDITIRA RSSDSLESRD EATPAAGNHP DSLRGLPHNQ DFPAHENQPL LLTSGCQENP
QEWVDRAVRM RSRMAYNNIQ KSNFGNQSPS TSRPQSAIHH PNEPSVKIKW WLLGLVAILA
VGLFWFFHTP AVETTAVQEF QNQMKQLQSK YQSQNEKLWK RGTTFLEKHL NSSLPRPQPA
ILLLTAAQDA AEVLKCLSEQ IADAYSSFRS VRAIRIDGAG KAAQDSDLVK HEVDQELTDG
FKNGQNAAVV HRFESLPAGS TLIFYKYCDH ENAAFKDVAL VLTVLLEEKT LEASLGLKEI
EEKVRDFLKV KFTSSSTASS YNHMDPDKLN GLWSRISHLV LPVQPENTLK AGSCL
