TOIP1_RAT
ID TOIP1_RAT Reviewed; 583 AA.
AC Q5PQX1; Q62741; Q62754;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Torsin-1A-interacting protein 1;
DE AltName: Full=Lamina-associated polypeptide 1B;
DE Short=LAP1B;
DE AltName: Full=Lamina-associated polypeptide 1C;
DE Short=LAP1C;
GN Name=Tor1aip1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA69914.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAA69914.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAA69914.1};
RX PubMed=7721789; DOI=10.1074/jbc.270.15.8822;
RA Martin L., Crimaudo C., Gerace L.;
RT "cDNA cloning and characterization of lamina-associated polypeptide 1C
RT (LAP1C), an integral protein of the inner nuclear membrane.";
RL J. Biol. Chem. 270:8822-8828(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 PROTEIN SEQUENCE OF 32-39 AND 152-160, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
RA Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
RA Watanabe Y., Furukawa K., Horigome T.;
RT "Proteome analysis of a rat liver nuclear insoluble protein fraction and
RT localization of a novel protein, ISP36, to compartments in the
RT interchromatin space.";
RL FEBS J. 272:4327-4338(2005).
RN [4]
RP INTERACTION WITH ATP1B4.
RX PubMed=14656723; DOI=10.1152/ajpcell.00358.2003;
RA Zhao H., Pestov N.B., Korneenko T.V., Shakhparonov M.I., Modyanov N.N.;
RT "Accumulation of beta (m), a structural member of X,K-ATPase beta-subunit
RT family, in nuclear envelopes of perinatal myocytes.";
RL Am. J. Physiol. 286:C757-C767(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-142; SER-157; SER-231
RP AND SER-242, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SUBUNIT: Interacts with ATP1B4. Interacts with TOR1A (ATP-bound).
CC Interacts with TOR1B, TOR2A and TOR3A. Interacts with VIM.
CC {ECO:0000269|PubMed:14656723}.
CC -!- INTERACTION:
CC Q5PQX1; P62138: Ppp1ca; NbExp=2; IntAct=EBI-15644430, EBI-357231;
CC Q5PQX1; P63088: Ppp1cc; NbExp=2; IntAct=EBI-15644430, EBI-80049;
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:16128803, ECO:0000269|PubMed:7721789}; Single-pass
CC membrane protein {ECO:0000269|PubMed:16128803,
CC ECO:0000269|PubMed:7721789}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5PQX1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:7721789};
CC IsoId=Q5PQX1-2; Sequence=VSP_051777, VSP_051778;
CC Name=3 {ECO:0000269|PubMed:7721789};
CC IsoId=Q5PQX1-3; Sequence=VSP_051776;
CC -!- SIMILARITY: Belongs to the TOR1AIP family. {ECO:0000305}.
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DR EMBL; U19614; AAA69914.1; -; mRNA.
DR EMBL; U20286; AAA69915.1; -; mRNA.
DR EMBL; BC086987; AAH86987.1; -; mRNA.
DR PIR; A56391; A56391.
DR PIR; I61730; I61730.
DR RefSeq; NP_659560.2; NM_145092.2. [Q5PQX1-1]
DR AlphaFoldDB; Q5PQX1; -.
DR SMR; Q5PQX1; -.
DR DIP; DIP-60963N; -.
DR IntAct; Q5PQX1; 7.
DR STRING; 10116.ENSRNOP00000005280; -.
DR GlyGen; Q5PQX1; 1 site.
DR iPTMnet; Q5PQX1; -.
DR PhosphoSitePlus; Q5PQX1; -.
DR PaxDb; Q5PQX1; -.
DR PRIDE; Q5PQX1; -.
DR Ensembl; ENSRNOT00000005280; ENSRNOP00000005280; ENSRNOG00000003946. [Q5PQX1-1]
DR GeneID; 246314; -.
DR KEGG; rno:246314; -.
DR UCSC; RGD:628851; rat. [Q5PQX1-1]
DR CTD; 26092; -.
DR RGD; 628851; Tor1aip1.
DR eggNOG; ENOG502QUV7; Eukaryota.
DR GeneTree; ENSGT00390000012166; -.
DR HOGENOM; CLU_034263_0_1_1; -.
DR InParanoid; Q5PQX1; -.
DR OMA; FSEEGDT; -.
DR OrthoDB; 575658at2759; -.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:Q5PQX1; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003946; Expressed in testis and 19 other tissues.
DR Genevisible; Q5PQX1; RN.
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:RGD.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IBA:GO_Central.
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:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0005521; F:lamin binding; IDA:RGD.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0071763; P:nuclear membrane organization; ISO:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; ISO:RGD.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
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; Direct protein sequencing; Glycoprotein;
KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..583
FT /note="Torsin-1A-interacting protein 1"
FT /id="PRO_0000084355"
FT TOPO_DOM 1..339
FT /note="Nuclear"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:7721789"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..583
FT /note="Perinuclear space"
FT /evidence="ECO:0000255"
FT REGION 23..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..583
FT /note="Interaction with TOR1A"
FT /evidence="ECO:0000250"
FT COILED 360..388
FT /evidence="ECO:0000255"
FT COMPBIAS 45..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 309
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5JTV8"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7721789"
FT /id="VSP_051776"
FT VAR_SEQ 220..246
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7721789"
FT /id="VSP_051777"
FT VAR_SEQ 362..412
FT /note="TTAVQEFQNQMKQLQSKYQSQDEKLWKRGTTFLEKHLNSSLPRPQPAILLL
FT -> I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7721789"
FT /id="VSP_051778"
SQ SEQUENCE 583 AA; 65649 MW; 827FC3FA8CBDE3D8 CRC64;
MAGERWRAEG LGEGWAIYVT PRAPIREGRR RLATQNGDGS DAPAYETHPS RHGRREVRFS
EEPPEVYGDF EPRAAKERSP GERRTPPEKF RSDSAKEEVR ESAYNLRSRQ RRQRGPQEAE
EMKTRRSTRL EQHSQQAQQQ LSPATSGRGL RDAQSLSEDR GEDEPSSQPV TSQTVSKKTV
RTPETSVMSE DPISNLCRPP LRSPRPDASI VQHINPFEEG ETEDDLESSY SDVTIRIRSR
DSVESRDEAA VAAGHHPDSL WGLPHSRGDF TAHENQPSLL PTGCQKNPQE WVEQAVRMRT
RMAYNNIQKS DFGNQSPSTS RQQAAVQPPD ESSVKIKWWL LILVAALAMG IYWFFHTPVV
ETTAVQEFQN QMKQLQSKYQ SQDEKLWKRG TTFLEKHLNS SLPRPQPAIL LLTAAQDAAE
VLKCLSEQIA DAYSSFRSVR AIRIDGAGKA AQDSDLVKHE VDQELTDGFR NGQNAAVVHR
FESLPAGSTL IFYKYCDHEN AAFKDVALVL TVLLEEQTLE ASLGLKEIEE KVRDFLKVKF
TSSDTANSYN HMDPDKLNGL WSRISHLVLP VQPENALKAG SCL
