CNEP1_CAEEL
ID CNEP1_CAEEL Reviewed; 246 AA.
AC Q20432; H1ZUW4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=CTD nuclear envelope phosphatase 1 homolog;
DE Short=CTDNEP1;
DE EC=3.1.3.16;
DE AltName: Full=Serine/threonine-protein phosphatase dullard homolog;
DE AltName: Full=Small C-terminal domain phosphatase-like phosphatase 21;
GN Name=cnep-1; Synonyms=scpl-2; ORFNames=F45E12.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
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 [3]
RP FUNCTION.
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).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=32271860; DOI=10.1083/jcb.201908179;
RA Penfield L., Shankar R., Szentgyoergyi E., Laffitte A., Mauro M.S.,
RA Audhya A., Mueller-Reichert T., Bahmanyar S.;
RT "Regulated lipid synthesis and LEM2/CHMP7 jointly control nuclear envelope
RT closure.";
RL J. Cell Biol. 219:0-0(2020).
CC -!- FUNCTION: Serine/threonine protein phosphatase that may dephosphorylate
CC and activate lipin-like phosphatases (PubMed:22134922). Lipins are
CC phosphatidate phosphatases that catalyze the conversion of phosphatidic
CC acid to diacylglycerol and control the metabolism of fatty acids at
CC different levels (PubMed:22134922). May indirectly modulate the lipid
CC composition of nuclear and/or endoplasmic reticulum membranes and be
CC required for proper nuclear membrane morphology and/or dynamics
CC (PubMed:22134922). Contributes to closure of nuclear envelope (NE)
CC holes and prevents excess nuclear membranes after meiosis and mitosis,
CC possibly through spatial regulation of lipin (PubMed:32271860). May
CC limit the production of endoplasmic reticulum (ER) sheets proximal to
CC the NE to prevent the ER membranes that feed into NE openings from
CC invading the nuclear interior and thereby restrict nuclear transport to
CC nuclear pore complexes (NPCs) (PubMed:32271860). May also indirectly
CC regulate the production of lipid droplets and triacylglycerol
CC (PubMed:22134922). {ECO:0000269|PubMed:22134922,
CC ECO:0000269|PubMed:32271860}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:32271860}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q20432-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q20432-2; Sequence=VSP_056100;
CC -!- DISRUPTION PHENOTYPE: Excess of internal nuclear membranes in oocyte-
CC derived pronuclei that are nearly or completely bisecting the nucleus
CC in embryos during nuclear closure (PubMed:32271860). Increased
CC phosphatidylinositol (PI) production and ectopic ER sheets
CC (PubMed:32271860). Nuclei contain openings through which imported
CC proteins passively diffuse (PubMed:32271860). Twinned nuclei after
CC mitosis (PubMed:32271860). Simultaneous knockdown of chmp-7 or lem-2
CC leads to enhanced nuclear sealing defects (PubMed:32271860).
CC {ECO:0000269|PubMed:32271860}.
CC -!- SIMILARITY: Belongs to the dullard family. {ECO:0000305}.
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DR EMBL; FO080734; CCD66263.1; -; Genomic_DNA.
DR EMBL; FO080734; CCF23398.1; -; Genomic_DNA.
DR PIR; T16371; T16371.
DR RefSeq; NP_001254123.1; NM_001267194.1. [Q20432-2]
DR RefSeq; NP_001254124.1; NM_001267195.1.
DR AlphaFoldDB; Q20432; -.
DR SMR; Q20432; -.
DR BioGRID; 50561; 1.
DR STRING; 6239.F45E12.1b; -.
DR EPD; Q20432; -.
DR PaxDb; Q20432; -.
DR PeptideAtlas; Q20432; -.
DR EnsemblMetazoa; F45E12.1a.1; F45E12.1a.1; WBGene00018474. [Q20432-1]
DR EnsemblMetazoa; F45E12.1a.2; F45E12.1a.2; WBGene00018474. [Q20432-1]
DR EnsemblMetazoa; F45E12.1b.1; F45E12.1b.1; WBGene00018474. [Q20432-2]
DR GeneID; 185802; -.
DR KEGG; cel:CELE_F45E12.1; -.
DR UCSC; F45E12.1; c. elegans. [Q20432-1]
DR CTD; 185802; -.
DR WormBase; F45E12.1a; CE02737; WBGene00018474; cnep-1. [Q20432-1]
DR WormBase; F45E12.1b; CE46930; WBGene00018474; cnep-1. [Q20432-2]
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240503; -.
DR HOGENOM; CLU_020262_4_3_1; -.
DR InParanoid; Q20432; -.
DR OMA; IPIRSWF; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q20432; -.
DR Reactome; R-CEL-4419969; Depolymerisation of the Nuclear Lamina.
DR PRO; PR:Q20432; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00018474; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0071595; C:Nem1-Spo7 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
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:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR GO; GO:0031468; P:nuclear membrane reassembly; IMP:UniProtKB.
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:0051783; P:regulation of nuclear division; IMP:WormBase.
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 3: Inferred from homology;
KW Alternative splicing; Hydrolase; Membrane; Nucleus; Protein phosphatase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..246
FT /note="CTD nuclear envelope phosphatase 1 homolog"
FT /id="PRO_0000297975"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 53..220
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT VAR_SEQ 1
FT /note="M -> MYVPNRQFGGGNPESHRRRDQKQASLVLRTM (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_056100"
SQ SEQUENCE 246 AA; 28414 MW; 7D60A06A050EA3EA CRC64;
MTTIAQSVFC FLAGFFNFFL LYFRKTSRAY CKYQVVKYHS NIPMSPLTTH RLLTVKRKIL
VLDLDETLIH SHHDGVLRQT VKPGTPSDFT IRVVIDRHPV KFSVHERPHV DYFLSVVSQW
YELVVFTASM EVYGTSVADR LDRGRGILKR RYFRQHCTME VGGYTKDLSA IHPDLSSICI
LDNSPGAYRK FPHNAIPIPS WFSDPNDTCL LNLLPFLDAL RFTSDVRSVL SRNMQALPET
QSVQYY
