CNEP1_DROME
ID CNEP1_DROME Reviewed; 243 AA.
AC Q9VRG7; Q8MT79;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=Dd; Synonyms=l(1)G0269; ORFNames=CG1696;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM48350.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF50833.1; -; Genomic_DNA.
DR EMBL; AY094776; AAM11129.1; -; mRNA.
DR EMBL; AY118321; AAM48350.1; ALT_INIT; mRNA.
DR RefSeq; NP_608449.1; NM_134605.3.
DR AlphaFoldDB; Q9VRG7; -.
DR SMR; Q9VRG7; -.
DR BioGRID; 59385; 14.
DR STRING; 7227.FBpp0076921; -.
DR PaxDb; Q9VRG7; -.
DR PRIDE; Q9VRG7; -.
DR DNASU; 33107; -.
DR EnsemblMetazoa; FBtr0077226; FBpp0076921; FBgn0029067.
DR GeneID; 33107; -.
DR KEGG; dme:Dmel_CG1696; -.
DR CTD; 33107; -.
DR FlyBase; FBgn0029067; Dd.
DR VEuPathDB; VectorBase:FBgn0029067; -.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240503; -.
DR InParanoid; Q9VRG7; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q9VRG7; -.
DR Reactome; R-DME-4419969; Depolymerisation of the Nuclear Lamina.
DR BioGRID-ORCS; 33107; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33107; -.
DR PRO; PR:Q9VRG7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029067; Expressed in brain and 23 other tissues.
DR ExpressionAtlas; Q9VRG7; baseline and differential.
DR Genevisible; Q9VRG7; DM.
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; IDA:FlyBase.
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:0008287; C:protein serine/threonine phosphatase complex; TAS:FlyBase.
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; IMP:FlyBase.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:FlyBase.
DR GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR GO; GO:0101025; P:nuclear membrane biogenesis; IEP:FlyBase.
DR GO; GO:1903740; P:positive regulation of phosphatidate phosphatase activity; IGI:FlyBase.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:FlyBase.
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 2: Evidence at transcript level;
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_0000297976"
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; 28486 MW; 1E278DD1D8DF60C6 CRC64;
MISLLQMKFR ALLLLLSKVW TCICFMFNRQ VRAFIQYQPV KYELFPLSPV SRHRLSLVQR
KTLVLDLDET LIHSHHNAMP RNTVKPGTPH DFTVKVTIDR NPVRFFVHKR PHVDYFLDVV
SQWYDLVVFT ASMEIYGAAV ADKLDNGRNI LRRRYYRQHC TPDYGSYTKD LSAICSDLNR
IFIIDNSPGA YRCFPNNAIP IKSWFSDPMD TALLSLLPML DALRFTNDVR SVLSRNLHLH
RLW
