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Torsin-1A-interacting protein 1 (Lamina-associated polypeptide 1B) (LAP1B) (Lamina-associated polypeptide 1C) (LAP1C)

 TOIP1_RAT               Reviewed;         583 AA.
Q5PQX1; Q62741; Q62754;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 1.
12-SEP-2018, entry version 103.
RecName: Full=Torsin-1A-interacting protein 1;
AltName: Full=Lamina-associated polypeptide 1B;
Short=LAP1B;
AltName: Full=Lamina-associated polypeptide 1C;
Short=LAP1C;
Name=Tor1aip1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000305, ECO:0000312|EMBL:AAA69914.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND SUBCELLULAR
LOCATION.
STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAA69914.1};
TISSUE=Liver {ECO:0000312|EMBL:AAA69914.1};
PubMed=7721789; DOI=10.1074/jbc.270.15.8822;
Martin L., Crimaudo C., Gerace L.;
"cDNA cloning and characterization of lamina-associated polypeptide 1C
(LAP1C), an integral protein of the inner nuclear membrane.";
J. Biol. Chem. 270:8822-8828(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 32-39 AND 152-160, AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
Watanabe Y., Furukawa K., Horigome T.;
"Proteome analysis of a rat liver nuclear insoluble protein fraction
and localization of a novel protein, ISP36, to compartments in the
interchromatin space.";
FEBS J. 272:4327-4338(2005).
[4]
INTERACTION WITH ATP1B4.
PubMed=14656723; DOI=10.1152/ajpcell.00358.2003;
Zhao H., Pestov N.B., Korneenko T.V., Shakhparonov M.I.,
Modyanov N.N.;
"Accumulation of beta (m), a structural member of X,K-ATPase beta-
subunit family, in nuclear envelopes of perinatal myocytes.";
Am. J. Physiol. 286:C757-C767(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-142; SER-157;
SER-231 AND SER-242, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Required for nuclear membrane integrity. Induces TOR1A
and TOR1B ATPase activity and is required for their location on
the nuclear membrane. Binds to A- and B-type lamins. Possible role
in membrane attachment and assembly of the nuclear lamina.
-!- SUBUNIT: Interacts with ATP1B4. Interacts with TOR1A (ATP-bound).
Interacts with TOR1B, TOR2A and TOR3A. Interacts with VIM.
{ECO:0000269|PubMed:14656723}.
-!- SUBCELLULAR LOCATION: Nucleus inner membrane
{ECO:0000269|PubMed:16128803, ECO:0000269|PubMed:7721789}; Single-
pass membrane protein {ECO:0000269|PubMed:16128803,
ECO:0000269|PubMed:7721789}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q5PQX1-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:7721789};
IsoId=Q5PQX1-2; Sequence=VSP_051777, VSP_051778;
Name=3 {ECO:0000269|PubMed:7721789};
IsoId=Q5PQX1-3; Sequence=VSP_051776;
-!- SIMILARITY: Belongs to the TOR1AIP family. {ECO:0000305}.
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EMBL; U19614; AAA69914.1; -; mRNA.
EMBL; U20286; AAA69915.1; -; mRNA.
EMBL; BC086987; AAH86987.1; -; mRNA.
PIR; A56391; A56391.
PIR; I61730; I61730.
RefSeq; NP_659560.2; NM_145092.2. [Q5PQX1-1]
UniGene; Rn.11373; -.
SMR; Q5PQX1; -.
DIP; DIP-60963N; -.
IntAct; Q5PQX1; 1.
STRING; 10116.ENSRNOP00000005280; -.
iPTMnet; Q5PQX1; -.
PhosphoSitePlus; Q5PQX1; -.
PaxDb; Q5PQX1; -.
PRIDE; Q5PQX1; -.
Ensembl; ENSRNOT00000005280; ENSRNOP00000005280; ENSRNOG00000003946. [Q5PQX1-1]
Ensembl; ENSRNOT00000005296; ENSRNOP00000005296; ENSRNOG00000003946. [Q5PQX1-1]
GeneID; 246314; -.
KEGG; rno:246314; -.
UCSC; RGD:628851; rat. [Q5PQX1-1]
CTD; 26092; -.
RGD; 628851; Tor1aip1.
eggNOG; ENOG410IJUB; Eukaryota.
eggNOG; ENOG4111IZJ; LUCA.
GeneTree; ENSGT00390000012166; -.
HOGENOM; HOG000015293; -.
HOVERGEN; HBG083152; -.
InParanoid; Q5PQX1; -.
OMA; FQNQMKQ; -.
PRO; PR:Q5PQX1; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000003946; Expressed in 9 organ(s), highest expression level in testis.
Genevisible; Q5PQX1; RN.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005635; C:nuclear envelope; IDA:RGD.
GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
GO; GO:0005521; F:lamin binding; IDA:RGD.
GO; GO:0071763; P:nuclear membrane organization; IEA:Ensembl.
GO; GO:0032781; P:positive regulation of ATPase activity; ISS:UniProtKB.
GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
Gene3D; 3.40.50.12190; -; 1.
InterPro; IPR008662; Lamina-ass_polypeptide_CLAP1C.
InterPro; IPR038599; LAP1C-like_C_sf.
PANTHER; PTHR18843; PTHR18843; 1.
Pfam; PF05609; LAP1C; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome;
Direct protein sequencing; Glycoprotein; Isopeptide bond; Membrane;
Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 583 Torsin-1A-interacting protein 1.
/FTId=PRO_0000084355.
TOPO_DOM 1 339 Nuclear. {ECO:0000255,
ECO:0000303|PubMed:7721789}.
TRANSMEM 340 360 Helical. {ECO:0000255}.
TOPO_DOM 361 583 Perinuclear space. {ECO:0000255}.
REGION 356 583 Interaction with TOR1A. {ECO:0000250}.
COILED 360 388 {ECO:0000255}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000250|UniProtKB:Q5JTV8}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000250|UniProtKB:Q5JTV8}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 189 189 Phosphoserine.
{ECO:0000250|UniProtKB:Q5JTV8}.
MOD_RES 222 222 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5JTV8}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000250|UniProtKB:Q5JTV8}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000250|UniProtKB:Q5JTV8}.
CARBOHYD 399 399 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 309 309 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q5JTV8}.
VAR_SEQ 1 121 Missing (in isoform 3).
{ECO:0000303|PubMed:7721789}.
/FTId=VSP_051776.
VAR_SEQ 220 246 Missing (in isoform 2).
{ECO:0000303|PubMed:7721789}.
/FTId=VSP_051777.
VAR_SEQ 362 412 TTAVQEFQNQMKQLQSKYQSQDEKLWKRGTTFLEKHLNSSL
PRPQPAILLL -> I (in isoform 2).
{ECO:0000303|PubMed:7721789}.
/FTId=VSP_051778.
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


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