CNEP1_MOUSE
ID CNEP1_MOUSE Reviewed; 244 AA.
AC Q3TP92; Q5NCW4; Q8VEL4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=CTD nuclear envelope phosphatase 1;
DE EC=3.1.3.16;
DE AltName: Full=Serine/threonine-protein phosphatase dullard;
GN Name=Ctdnep1; Synonyms=Dullard;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [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].
RC STRAIN=FVB/N; 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 IDENTIFICATION.
RX PubMed=12083771; DOI=10.1016/s0006-291x(02)00641-1;
RA Satow R., Chan T.C., Asashima M.;
RT "Molecular cloning and characterization of dullard: a novel gene required
RT for neural development.";
RL Biochem. Biophys. Res. Commun. 295:85-91(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=22134922; DOI=10.1074/jbc.m111.324350;
RA Han S., Bahmanyar S., Zhang P., Grishin N., Oegema K., Crooke R.,
RA Graham M., Reue K., Dixon J.E., Goodman J.M.;
RT "Nuclear envelope phosphatase-regulatory subunit 1 (formerly TMEM188) is
RT the metazoan SPO7 ortholog and functions in the lipin activation pathway.";
RL J. Biol. Chem. 287:3123-3137(2012).
CC -!- FUNCTION: Serine/threonine protein phosphatase forming with CNEP1R1 an
CC active phosphatase complex that dephosphorylates and may activate LPIN1
CC and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze
CC the conversion of phosphatidic acid to diacylglycerol and control the
CC metabolism of fatty acids at different levels. May indirectly modulate
CC the lipid composition of nuclear and/or endoplasmic reticulum membranes
CC and be required for proper nuclear membrane morphology and/or dynamics.
CC May also indirectly regulate the production of lipid droplets and
CC triacylglycerol. May antagonize BMP signaling (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Interacts with CNEP1R1; the complex dephosphorylates LPIN1 and
CC LPIN2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Nucleus membrane
CC {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Muscle specific with lower expression in other
CC metabolic tissues. {ECO:0000269|PubMed:22134922}.
CC -!- SIMILARITY: Belongs to the dullard family. {ECO:0000305}.
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DR EMBL; AK164602; BAE37845.1; -; mRNA.
DR EMBL; AL596185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018265; AAH18265.1; -; mRNA.
DR CCDS; CCDS24927.1; -.
DR RefSeq; NP_080293.1; NM_026017.2.
DR AlphaFoldDB; Q3TP92; -.
DR SMR; Q3TP92; -.
DR BioGRID; 211999; 3.
DR STRING; 10090.ENSMUSP00000104234; -.
DR iPTMnet; Q3TP92; -.
DR PhosphoSitePlus; Q3TP92; -.
DR EPD; Q3TP92; -.
DR MaxQB; Q3TP92; -.
DR PaxDb; Q3TP92; -.
DR PeptideAtlas; Q3TP92; -.
DR PRIDE; Q3TP92; -.
DR ProteomicsDB; 283867; -.
DR Antibodypedia; 23976; 149 antibodies from 23 providers.
DR Ensembl; ENSMUST00000108593; ENSMUSP00000104234; ENSMUSG00000018559.
DR GeneID; 67181; -.
DR KEGG; mmu:67181; -.
DR UCSC; uc007jtf.1; mouse.
DR CTD; 23399; -.
DR MGI; MGI:1914431; Ctdnep1.
DR VEuPathDB; HostDB:ENSMUSG00000018559; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240503; -.
DR HOGENOM; CLU_020262_4_3_1; -.
DR InParanoid; Q3TP92; -.
DR OMA; IPIRSWF; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q3TP92; -.
DR TreeFam; TF313962; -.
DR Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
DR BioGRID-ORCS; 67181; 10 hits in 74 CRISPR screens.
DR ChiTaRS; Ctdnep1; mouse.
DR PRO; PR:Q3TP92; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3TP92; protein.
DR Bgee; ENSMUSG00000018559; Expressed in hindlimb stylopod muscle and 246 other tissues.
DR ExpressionAtlas; Q3TP92; baseline and differential.
DR Genevisible; Q3TP92; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0071595; C:Nem1-Spo7 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0007276; P:gamete generation; IMP:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Nucleus; Protein phosphatase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..244
FT /note="CTD nuclear envelope phosphatase 1"
FT /id="PRO_0000297968"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 57..224
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT CONFLICT 213
FT /note="A -> S (in Ref. 1; BAE37845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 28391 MW; 1AD25540018F50BA CRC64;
MMRTQCLLGL RTFVAFAAKL WSFFIYLLRR QIRTVIQYQT VRYDILPLSP LSRNRLAQVK
RKILVLDLDE TLIHSHHDGV LRPTVRPGTP PDFILKVVID KHPVRFFVHK RPHVDFFLEV
VSQWYELVVF TASMEIYGSA VADKLDNSRS ILKRRYYRQH CTLELGSYIK DLSVVHSDLS
SIVILDNSPG AYRSHPDNAI PIKSWFSDPS DTALLNLLPM LDALRFTADV RSVLSRNLHQ
HRLW
