Q29I63 (CNEP1_DROPS) 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:	GA14238

Organism

Drosophila pseudoobscura pseudoobscura (Fruit fly) [Reference proteome]

Taxonomic identifier

46245 [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 › obscura group › pseudoobscura subgroup › Drosophila pseudoobscura

Protein attributes

Sequence length	243 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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.

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	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_0000297977
Regions
	Transmembrane	11 – 27	17	Helical; Potential
	Domain	56 – 223	168	FCP1 homology

Sequences

	Sequence		Length	Mass (Da)
	Q29I63 [UniParc]. Last modified April 4, 2006. Version 1. Checksum: 28FBC1B51E9FE2CE	FASTA	243	28,467
	10 20 30 40 50 60 MISLLQMKFH 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

[1]

"Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution." Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L. , Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., Weinstock G.M., Gibbs R.A. Genome Res. 15:1-18(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MV2-25 / Tucson 14011-0121.94.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH379063 Genomic DNA. Translation: EAL32790.1.
RefSeq	XP_001355731.1. XM_001355695.2.
3D structure databases
ProteinModelPortal	Q29I63.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0275234; FBpp0273672; FBgn0074267.
GeneID	4815779.
KEGG	dpo:Dpse_GA14238.
Organism-specific databases
FlyBase	FBgn0074267. Dpse\GA14238.
Phylogenomic databases
eggNOG	COG5190.
InParanoid	Q29I63.
OMA	SRNRLGQ.
OrthoDB	EOG48KPT5.
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...

Entry information

Entry name

CNEP1_DROPS

Accession

Primary (citable) accession number: Q29I63

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	April 4, 2006
Last modified:	April 3, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project