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 27-MAR-2024, entry version 85. 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; 46245.Q29I63; -. DR EnsemblMetazoa; FBtr0275234; FBpp0273672; FBgn0074267. DR GeneID; 4815779; -. DR KEGG; dpo:4815779; -. DR eggNOG; KOG1605; Eukaryota. DR HOGENOM; CLU_020262_4_3_1; -. DR InParanoid; Q29I63; -. DR OMA; RIWGFFM; -. DR PhylomeDB; Q29I63; -. DR Proteomes; UP000001819; Chromosome X. DR Bgee; FBgn0074267; Expressed in female reproductive system and 2 other cell types or tissues. DR ExpressionAtlas; Q29I63; baseline. 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: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 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..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 //