Q3TP92 (CNEP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CTD nuclear envelope phosphatase 1
EC=3.1.3.16

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

Gene names

Name:	Ctdnep1
Synonyms:	Dullard

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 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. May antagonize BMP signaling By similarity.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Interacts with CNEP1R1; the complex dephosphorylates LPIN1 and LPIN2 By similarity.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Nucleus membrane; Single-pass membrane protein By similarity.
Tissue specificity	Muscle specific with lower expression in other metabolic tissues. Ref.5
Sequence similarities	Belongs to the dullard family. Contains 1 FCP1 homology domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Nucleus
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 protein localization to nucleus 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 – 244	244	CTD nuclear envelope phosphatase 1		PRO_0000297968
Regions
	Transmembrane	7 – 29	23	Helical; Potential
	Domain	57 – 224	168	FCP1 homology
Experimental info
	Sequence conflict	213	1	A → S in BAE37845. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q3TP92 [UniParc]. Last modified August 21, 2007. Version 2. Checksum: 1AD25540018F50BA	FASTA	244	28,391
	10 20 30 40 50 60 MMRTQCLLGL RTFVAFAAKL WSFFIYLLRR QIRTVIQYQT VRYDILPLSP LSRNRLAQVK 70 80 90 100 110 120 RKILVLDLDE TLIHSHHDGV LRPTVRPGTP PDFILKVVID KHPVRFFVHK RPHVDFFLEV 130 140 150 160 170 180 VSQWYELVVF TASMEIYGSA VADKLDNSRS ILKRRYYRQH CTLELGSYIK DLSVVHSDLS 190 200 210 220 230 240 SIVILDNSPG AYRSHPDNAI PIKSWFSDPS DTALLNLLPM LDALRFTADV RSVLSRNLHQ HRLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Lung.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[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.
[5]	"Nuclear envelope phosphatase-regulatory subunit 1 (formerly TMEM188) is the metazoan SPO7 ortholog and functions in the lipin activation pathway." Han S., Bahmanyar S., Zhang P., Grishin N., Oegema K., Crooke R., Graham M., Reue K., Dixon J.E., Goodman J.M. J. Biol. Chem. 287:3123-3137(2012) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK164602 mRNA. Translation: BAE37845.1. AL596185 Genomic DNA. Translation: CAI35161.1. BC018265 mRNA. Translation: AAH18265.1.
IPI	IPI00754944.
RefSeq	NP_080293.1. NM_026017.2.
UniGene	Mm.41678.
3D structure databases
ProteinModelPortal	Q3TP92.
SMR	Q3TP92. Positions 57-234.
ModBase	Search...
PTM databases
PhosphoSite	Q3TP92.
Proteomic databases
PaxDb	Q3TP92.
PRIDE	Q3TP92.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000108593; ENSMUSP00000104234; ENSMUSG00000018559.
GeneID	67181.
KEGG	mmu:67181.
UCSC	uc007jtf.1. mouse.
Organism-specific databases
CTD	23399.
MGI	MGI:1914431. Ctdnep1.
Phylogenomic databases
eggNOG	COG5190.
GeneTree	ENSGT00550000075053.
HOVERGEN	HBG098153.
InParanoid	Q3TP92.
OMA	SRNRLGQ.
Gene expression databases
Bgee	Q3TP92.
CleanEx	MM_DULLARD.
Genevestigator	Q3TP92.
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
NextBio	323816.
SOURCE	Search...

Entry information

Entry name

CNEP1_MOUSE

Accession

Primary (citable) accession number: Q3TP92
Secondary accession number(s): Q5NCW4, Q8VEL4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	August 21, 2007
Last modified:	May 1, 2013
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program