Q9VRG7 (CNEP1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CTD nuclear envelope phosphatase 1 homolog
EC=3.1.3.16

Alternative name(s):
Serine/threonine-protein phosphatase dullard homolog

Gene names

Name:	l(1)G0269
ORF Names:	CG1696

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	243 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Serine/threonine protein phosphatase that may dephosphorylate and activate lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at differents levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol By similarity.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the dullard family. Contains 1 FCP1 homology domain.
Sequence caution	The sequence AAM48350.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	imaginal disc-derived wing vein specification Inferred from mutant phenotype PubMed 21790556. Source: FlyBase negative regulation of BMP signaling pathway Inferred from mutant phenotype PubMed 21790556. Source: FlyBase nuclear envelope organization Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of triglyceride biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB protein dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Nem1-Spo7 phosphatase complex Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	protein serine/threonine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 243	243	CTD nuclear envelope phosphatase 1 homolog		PRO_0000297976
Regions
	Transmembrane	11 – 27	17	Helical; Potential
	Domain	56 – 223	168	FCP1 homology

Sequences

	Sequence		Length	Mass (Da)
	Q9VRG7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 1E278DD1D8DF60C6	FASTA	243	28,486
	10 20 30 40 50 60 MISLLQMKFR ALLLLLSKVW TCICFMFNRQ VRAFIQYQPV KYELFPLSPV SRHRLSLVQR 70 80 90 100 110 120 KTLVLDLDET LIHSHHNAMP RNTVKPGTPH DFTVKVTIDR NPVRFFVHKR PHVDYFLDVV 130 140 150 160 170 180 SQWYDLVVFT ASMEIYGAAV ADKLDNGRNI LRRRYYRQHC TPDYGSYTKD LSAICSDLNR 190 200 210 220 230 240 IFIIDNSPGA YRCFPNNAIP IKSWFSDPMD TALLSLLPML DALRFTNDVR SVLSRNLHLH RLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Molecular cloning and characterization of dullard: a novel gene required for neural development." Satow R., Chan T.C., Asashima M. Biochem. Biophys. Res. Commun. 295:85-91(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014298 Genomic DNA. Translation: AAF50833.1. AY094776 mRNA. Translation: AAM11129.1. AY118321 mRNA. Translation: AAM48350.1. Different initiation.
RefSeq	NP_608449.1. NM_134605.2.
UniGene	Dm.7059.
3D structure databases
HSSP	HSSP built from PDB template 1TA0 based on UniProtKB Q9GZU7.
ProteinModelPortal	Q9VRG7.
SMR	Q9VRG7. Positions 60-223.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-899760.
Proteomic databases
PaxDb	Q9VRG7.
PRIDE	Q9VRG7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0077226; FBpp0076921; FBgn0029067.
GeneID	33107.
KEGG	dme:Dmel_CG1696.
Organism-specific databases
CTD	33107.
FlyBase	FBgn0029067. l(1)G0269.
Phylogenomic databases
eggNOG	COG5190.
GeneTree	ENSGT00550000075053.
HOGENOM	HOG000002447.
InParanoid	Q9VRG7.
OMA	SRNRLGQ.
OrthoDB	EOG48KPT5.
PhylomeDB	Q9VRG7.
Gene expression databases
Bgee	Q9VRG7.
Family and domain databases
Gene3D	3.40.50.1000. 1 hit.
InterPro	IPR011948. Dullard_phosphatase. IPR023214. HAD-like_dom. IPR004274. NIF. [Graphical view]
Pfam	PF03031. NIF. 1 hit. [Graphical view]
SMART	SM00577. CPDc. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR02251. HIF-SF_euk. 1 hit.
PROSITE	PS50969. FCP1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	33107.
NextBio	781938.

Entry information

Entry name

CNEP1_DROME

Accession

Primary (citable) accession number: Q9VRG7
Secondary accession number(s): Q8MT79

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project