TOIP2_HUMAN
ID TOIP2_HUMAN Reviewed; 470 AA.
AC Q8NFQ8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Torsin-1A-interacting protein 2;
DE AltName: Full=Lumenal domain-like LAP1;
GN Name=TOR1AIP2; Synonyms=IFRG15, LULL1;
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].
RC TISSUE=Brain;
RA Guo J.H., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 TORSIN-A, AND SUBCELLULAR LOCATION.
RX PubMed=15767459; DOI=10.1083/jcb.200411026;
RA Goodchild R.E., Dauer W.T.;
RT "The AAA+ protein torsinA interacts with a conserved domain present in LAP1
RT and a novel ER protein.";
RL J. Cell Biol. 168:855-862(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-163, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19339278; DOI=10.1091/mbc.e09-01-0094;
RA Vander Heyden A.B., Naismith T.V., Snapp E.L., Hodzic D., Hanson P.I.;
RT "LULL1 retargets TorsinA to the nuclear envelope revealing an activity that
RT is impaired by the DYT1 dystonia mutation.";
RL Mol. Biol. Cell 20:2661-2672(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-120 AND THR-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION AS ATPASE ACTIVATOR, AND INTERACTION WITH TOR1A.
RX PubMed=23569223; DOI=10.1073/pnas.1300676110;
RA Zhao C., Brown R.S., Chase A.R., Eisele M.R., Schlieker C.;
RT "Regulation of Torsin ATPases by LAP1 and LULL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1545-1554(2013).
RN [13]
RP FUNCTION IN ENDOPLASMIC RETICULUM INTEGRITY, INTERACTION WITH TOR1B, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24275647; DOI=10.1074/jbc.m113.515791;
RA Rose A.E., Zhao C., Turner E.M., Steyer A.M., Schlieker C.;
RT "Arresting a Torsin ATPase reshapes the endoplasmic reticulum.";
RL J. Biol. Chem. 289:552-564(2014).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 233-470 IN COMPLEX WITH TOR1A.
RX PubMed=27490483; DOI=10.7554/elife.17983;
RA Demircioglu F.E., Sosa B.A., Ingram J., Ploegh H.L., Schwartz T.U.;
RT "Structures of TorsinA and its disease-mutant complexed with an activator
RT reveal the molecular basis for primary dystonia.";
RL Elife 5:0-0(2016).
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.
CC {ECO:0000269|PubMed:19339278, ECO:0000269|PubMed:23569223,
CC ECO:0000269|PubMed:24275647}.
CC -!- SUBUNIT: Interacts with TOR1A and TOR1B (ATP-bound).
CC {ECO:0000269|PubMed:15767459, ECO:0000269|PubMed:23569223,
CC ECO:0000269|PubMed:24275647, ECO:0000269|PubMed:27490483}.
CC -!- INTERACTION:
CC Q8NFQ8; O14656: TOR1A; NbExp=3; IntAct=EBI-524567, EBI-524257;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC membrane protein. Nucleus membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=TOR1AIP2;
CC IsoId=Q8NFQ8-1; Sequence=Displayed;
CC Name=IFRG15;
CC IsoId=Q9H496-1; Sequence=External;
CC -!- SIMILARITY: Belongs to the TOR1AIP family. {ECO:0000305}.
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DR EMBL; AF464140; AAM50514.1; -; mRNA.
DR EMBL; AL359853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC101532; AAI01533.1; -; mRNA.
DR EMBL; BC112225; AAI12226.1; -; mRNA.
DR CCDS; CCDS1334.1; -. [Q8NFQ8-1]
DR RefSeq; NP_001186189.1; NM_001199260.1. [Q8NFQ8-1]
DR RefSeq; NP_659471.1; NM_145034.4. [Q8NFQ8-1]
DR RefSeq; XP_005244996.1; XM_005244939.4.
DR RefSeq; XP_016855963.1; XM_017000474.1.
DR RefSeq; XP_016855964.1; XM_017000475.1.
DR PDB; 5J1S; X-ray; 1.40 A; B=233-470.
DR PDB; 5J1T; X-ray; 1.40 A; B=233-470.
DR PDBsum; 5J1S; -.
DR PDBsum; 5J1T; -.
DR AlphaFoldDB; Q8NFQ8; -.
DR SMR; Q8NFQ8; -.
DR BioGRID; 127870; 238.
DR IntAct; Q8NFQ8; 68.
DR MINT; Q8NFQ8; -.
DR STRING; 9606.ENSP00000356584; -.
DR GlyConnect; 1823; 2 N-Linked glycans (1 site).
DR GlyGen; Q8NFQ8; 4 sites, 3 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q8NFQ8; -.
DR MetOSite; Q8NFQ8; -.
DR PhosphoSitePlus; Q8NFQ8; -.
DR SwissPalm; Q8NFQ8; -.
DR BioMuta; TOR1AIP2; -.
DR DMDM; 74751288; -.
DR EPD; Q8NFQ8; -.
DR jPOST; Q8NFQ8; -.
DR MassIVE; Q8NFQ8; -.
DR PaxDb; Q8NFQ8; -.
DR PeptideAtlas; Q8NFQ8; -.
DR PRIDE; Q8NFQ8; -.
DR ProteomicsDB; 73337; -. [Q8NFQ8-1]
DR ABCD; Q8NFQ8; 1 sequenced antibody.
DR Antibodypedia; 60527; 75 antibodies from 16 providers.
DR DNASU; 163590; -.
DR Ensembl; ENST00000367612.7; ENSP00000356584.3; ENSG00000169905.13. [Q8NFQ8-1]
DR Ensembl; ENST00000609928.6; ENSP00000477486.1; ENSG00000169905.13. [Q8NFQ8-1]
DR GeneID; 163590; -.
DR KEGG; hsa:163590; -.
DR MANE-Select; ENST00000609928.6; ENSP00000477486.1; NM_001199260.2; NP_001186189.1.
DR UCSC; uc001gnk.4; human. [Q8NFQ8-1]
DR CTD; 163590; -.
DR DisGeNET; 163590; -.
DR GeneCards; TOR1AIP2; -.
DR HGNC; HGNC:24055; TOR1AIP2.
DR HPA; ENSG00000169905; Low tissue specificity.
DR MalaCards; TOR1AIP2; -.
DR MIM; 614513; gene.
DR neXtProt; NX_Q8NFQ8; -.
DR OpenTargets; ENSG00000169905; -.
DR PharmGKB; PA142670716; -.
DR VEuPathDB; HostDB:ENSG00000169905; -.
DR eggNOG; ENOG502QUV7; Eukaryota.
DR GeneTree; ENSGT00390000012166; -.
DR HOGENOM; CLU_034263_1_1_1; -.
DR InParanoid; Q8NFQ8; -.
DR OMA; DKTEHEN; -.
DR OrthoDB; 575658at2759; -.
DR PhylomeDB; Q8NFQ8; -.
DR TreeFam; TF329438; -.
DR PathwayCommons; Q8NFQ8; -.
DR SignaLink; Q8NFQ8; -.
DR BioGRID-ORCS; 163590; 74 hits in 1090 CRISPR screens.
DR ChiTaRS; TOR1AIP2; human.
DR GenomeRNAi; 163590; -.
DR Pharos; Q8NFQ8; Tbio.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NFQ8; protein.
DR Bgee; ENSG00000169905; Expressed in adrenal tissue and 205 other tissues.
DR ExpressionAtlas; Q8NFQ8; baseline and differential.
DR Genevisible; Q8NFQ8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001671; F:ATPase activator activity; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:UniProtKB.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IDA:CACAO.
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 3D-structure; Acetylation; Alternative splicing; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..470
FT /note="Torsin-1A-interacting protein 2"
FT /id="PRO_0000228838"
FT TOPO_DOM 2..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..470
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..470
FT /note="Interaction with TOR1A"
FT /evidence="ECO:0000269|PubMed:23569223"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 250..265
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 271..285
FT /evidence="ECO:0007829|PDB:5J1S"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 305..319
FT /evidence="ECO:0007829|PDB:5J1S"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:5J1S"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 340..356
FT /evidence="ECO:0007829|PDB:5J1S"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 377..382
FT /evidence="ECO:0007829|PDB:5J1S"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:5J1S"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:5J1S"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 411..426
FT /evidence="ECO:0007829|PDB:5J1S"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:5J1T"
FT HELIX 440..450
FT /evidence="ECO:0007829|PDB:5J1S"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5J1S"
FT HELIX 461..466
FT /evidence="ECO:0007829|PDB:5J1S"
SQ SEQUENCE 470 AA; 51263 MW; 275CB5E28B7D4338 CRC64;
MADSGLREPQ EDSQKDLEND PSVNSQAQET TIIASNAEEA EILHSACGLS KDHQEVETEG
PESADTGDKS ESPDEANVGK HPKDKTEDEN KQSFLDGGKG HHLPSENLGK EPLDPDPSHS
PSDKVGRADA HLGSSSVALP KEASDGTGAS QEPPTTDSQE AQSPGHSSAG QEGEDTLRRR
LLAPEAGSHP QQTQKLEEIK ENAQDTMRQI NKKGFWSYGP VILVVLVVAV VASSVNSYYS
SPAQQVPKNP ALEAFLAQFS QLEDKFPGQS SFLWQRGRKF LQKHLNASNP TEPATIIFTA
AREGRETLKC LSHHVADAYT SSQKVSPIQI DGAGRTWQDS DTVKLLVDLE LSYGFENGQK
AAVVHHFESF PAGSTLIFYK YCDHENAAFK DVALVLTVLL EEETLEASVG PRETEEKVRD
LLWAKFTNSD TPTSFNHMDS DKLSGLWSRI SHLVLPVQPV SSIEEQGCLF
