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   27-MAR-2024, entry version 136.
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).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=35852146; DOI=10.7554/elife.75513;
RA   Mauro M.S., Celma G., Zimyanin V., Magaj M.M., Gibson K.H., Redemann S.,
RA   Bahmanyar S.;
RT   "Ndc1 drives nuclear pore complex assembly independent of membrane
RT   biogenesis to promote nuclear formation and growth.";
RL   Elife 11:0-0(2022).
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, PubMed:35852146). Contributes to closure of nuclear
CC       envelope (NE) holes and prevents excess nuclear membranes after meiosis
CC       and mitosis, possibly through spatial regulation of lipin
CC       (PubMed:32271860). May limit the production of endoplasmic reticulum
CC       (ER) sheets proximal to the NE to prevent the ER membranes that feed
CC       into NE openings from invading the nuclear interior and thereby
CC       restrict nuclear transport to nuclear pore complexes (NPCs)
CC       (PubMed:32271860). May also indirectly regulate the production of lipid
CC       droplets and triacylglycerol (PubMed:22134922).
CC       {ECO:0000269|PubMed:22134922, ECO:0000269|PubMed:32271860,
CC       ECO:0000269|PubMed:35852146}.
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). Increase in embryo
CC       nuclear size (PubMed:35852146). Twinned nuclei after mitosis
CC       (PubMed:32271860). Simultaneous knockdown of chmp-7 or lem-2 leads to
CC       enhanced nuclear sealing defects (PubMed:32271860).
CC       {ECO:0000269|PubMed:32271860, ECO:0000269|PubMed:35852146}.
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.1; -.
DR   EPD; Q20432; -.
DR   PaxDb; 6239-F45E12-1b; -.
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   AGR; WB:WBGene00018474; -.
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; RIWGFFM; -.
DR   OrthoDB; 5473812at2759; -.
DR   PhylomeDB; Q20432; -.
DR   Reactome; R-CEL-4419969; Depolymerization of the Nuclear Lamina.
DR   PRO; PR:Q20432; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00018474; Expressed in adult organism and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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: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   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR011948; Dullard_phosphatase.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR   PANTHER; PTHR12210:SF70; CTD NUCLEAR ENVELOPE PHOSPHATASE 1; 1.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 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
//