ID   CNEP1_CAEBR             Reviewed;         246 AA.
AC   Q61C05; A8XH54;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 89.
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 2;
GN   Name=cnep-1; Synonyms=scpl-2; ORFNames=CBG13136;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Serine/threonine protein phosphatase that may dephosphorylate
CC       and activate lipin-like phosphatases. Lipins are phosphatidate
CC       phosphatases that catalyze the conversion of phosphatidic acid to
CC       diacylglycerol and control the metabolism of fatty acids at different
CC       levels. May indirectly modulate the lipid composition of nuclear and/or
CC       endoplasmic reticulum membranes and be required for proper nuclear
CC       membrane morphology and/or dynamics. May also indirectly regulate the
CC       production of lipid droplets and triacylglycerol (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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the dullard family. {ECO:0000305}.
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DR   EMBL; HE601401; CAP31978.3; -; Genomic_DNA.
DR   RefSeq; XP_002646742.1; XM_002646696.1.
DR   AlphaFoldDB; Q61C05; -.
DR   SMR; Q61C05; -.
DR   STRING; 6238.Q61C05; -.
DR   GeneID; 8588741; -.
DR   KEGG; cbr:CBG_13136; -.
DR   CTD; 8588741; -.
DR   WormBase; CBG13136; CBP28570; WBGene00033948; Cbr-cnep-1.
DR   eggNOG; KOG1605; Eukaryota.
DR   HOGENOM; CLU_020262_4_3_1; -.
DR   InParanoid; Q61C05; -.
DR   OMA; RIWGFFM; -.
DR   OrthoDB; 5473812at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
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; ISS:UniProtKB.
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:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
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   Hydrolase; Membrane; Protein phosphatase; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..246
FT                   /note="CTD nuclear envelope phosphatase 1 homolog"
FT                   /id="PRO_0000297974"
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"
SQ   SEQUENCE   246 AA;  28419 MW;  793ED6CE6513D471 CRC64;
     MTSFAQTVFY VLAGLFNVFL LYFRKTNRAY CKYQVVKYHS NIPMSPLTTH RLLTVKRKIL
     VLDLDETLIH SHHDGVLRQT VKPGTPSDFT IRVVIDRHPV KFSVHERPHV DYFLTVVSQW
     YELVVFTASM EVYGSSVADK LDRGRGILKR RYFRQHCTME VGGYTKDLSA IHPDLSSICI
     LDNSPGAYRK FPHNAIPIPS WFSDPNDTCL LNLLPFLDAL RFTSDVRSVL SRNMQVLPET
     QTVQYY
//