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   24-JAN-2024, entry version 125.
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   GlyCosmos; Q5PQX1; 1 site, No reported glycans.
DR   GlyGen; Q5PQX1; 1 site.
DR   iPTMnet; Q5PQX1; -.
DR   PhosphoSitePlus; Q5PQX1; -.
DR   PaxDb; 10116-ENSRNOP00000005280; -.
DR   Ensembl; ENSRNOT00000005280.7; ENSRNOP00000005280.4; ENSRNOG00000003946.9. [Q5PQX1-1]
DR   GeneID; 246314; -.
DR   KEGG; rno:246314; -.
DR   UCSC; RGD:628851; rat. [Q5PQX1-1]
DR   AGR; RGD:628851; -.
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; NASFVKM; -.
DR   OrthoDB; 2913800at2759; -.
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 cell types or tissues.
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: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   InterPro; IPR046753; TOIP1/2_C.
DR   InterPro; IPR046754; TOIP1/2_N.
DR   PANTHER; PTHR18843; TORSIN-1A-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR18843:SF6; TORSIN-1A-INTERACTING PROTEIN 1; 1.
DR   Pfam; PF05609; LAP1_C; 1.
DR   Pfam; PF20443; LAP1_N; 1.
DR   Genevisible; Q5PQX1; RN.
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
//