CNEP1_DROPS
ID CNEP1_DROPS Reviewed; 243 AA.
AC Q29I63;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=CTD nuclear envelope phosphatase 1 homolog;
DE EC=3.1.3.16;
DE AltName: Full=Serine/threonine-protein phosphatase dullard homolog;
GN Name=l(1)G0269; ORFNames=GA14238;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH379063; EAL32790.1; -; Genomic_DNA.
DR RefSeq; XP_001355731.1; XM_001355695.3.
DR AlphaFoldDB; Q29I63; -.
DR SMR; Q29I63; -.
DR STRING; 7237.FBpp0273672; -.
DR EnsemblMetazoa; FBtr0275234; FBpp0273672; FBgn0074267.
DR GeneID; 4815779; -.
DR KEGG; dpo:Dpse_GA14238; -.
DR eggNOG; KOG1605; Eukaryota.
DR HOGENOM; CLU_020262_4_3_1; -.
DR InParanoid; Q29I63; -.
DR OMA; IPIRSWF; -.
DR PhylomeDB; Q29I63; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0074267; Expressed in female reproductive system and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblMetazoa.
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:0007474; P:imaginal disc-derived wing vein specification; IEA:EnsemblMetazoa.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR GO; GO:0101025; P:nuclear membrane biogenesis; IEA:EnsemblMetazoa.
DR GO; GO:1903740; P:positive regulation of phosphatidate phosphatase activity; IEA:EnsemblMetazoa.
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..243
FT /note="CTD nuclear envelope phosphatase 1 homolog"
FT /id="PRO_0000297977"
FT TRANSMEM 11..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 56..223
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
SQ SEQUENCE 243 AA; 28467 MW; 28FBC1B51E9FE2CE CRC64;
MISLLQMKFH ALLLLLSKVW TCICFMFNRQ VRAFIQYQPV KYELFPLSPV SRHRLSLVQR
KTLVLDLDET LIHSHHNAMP RNTVKPGTPH DFTVKVTIDR NPVRFFVHKR PHVDYFLDVV
SQWYDLVVFT ASMEIYGAAV ADKLDNGRNI LRRRYYRQHC TPDYGSYTKD LSAICSDLNR
IFIIDNSPGA YRCFPNNAIP IKSWFSDPMD TALLSLLPML DALRFTNDVR SVLSRNLHLH
RLW
