CNEP1_CAEBR
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 03-AUG-2022, entry version 83.
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.CBG13136; -.
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; IPIRSWF; -.
DR OrthoDB; 1176152at2759; -.
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: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; 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: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:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; 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 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
