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Q3TP92 (CNEP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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 componentEndoplasmic reticulum
Membrane
Nucleus
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgamete generation

Inferred from mutant phenotype PubMed 23469192. Source: MGI

mesoderm development

Inferred from mutant phenotype PubMed 23469192. Source: MGI

nuclear envelope organization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 23469192. Source: MGI

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_componentNem1-Spo7 phosphatase complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear envelope

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear membrane

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 23469192. Source: MGI

   Molecular_functionprotein serine/threonine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244CTD nuclear envelope phosphatase 1
PRO_0000297968

Regions

Transmembrane7 – 2923Helical; Potential
Domain57 – 224168FCP1 homology

Experimental info

Sequence conflict2131A → S in BAE37845. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3TP92 [UniParc].

Last modified August 21, 2007. Version 2.
Checksum: 1AD25540018F50BA

FASTA24428,391
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_080293.1. NM_026017.2.
UniGeneMm.41678.

3D structure databases

ProteinModelPortalQ3TP92.
SMRQ3TP92. Positions 57-236.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ3TP92.

Proteomic databases

PaxDbQ3TP92.
PRIDEQ3TP92.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000108593; ENSMUSP00000104234; ENSMUSG00000018559.
GeneID67181.
KEGGmmu:67181.
UCSCuc007jtf.1. mouse.

Organism-specific databases

CTD23399.
MGIMGI:1914431. Ctdnep1.

Phylogenomic databases

eggNOGCOG5190.
GeneTreeENSGT00550000075053.
HOVERGENHBG098153.
InParanoidQ3TP92.
KOK17617.
OMALLGIRTF.
OrthoDBEOG7MKW6W.
PhylomeDBQ3TP92.
TreeFamTF313962.

Gene expression databases

ArrayExpressQ3TP92.
BgeeQ3TP92.
CleanExMM_DULLARD.
GenevestigatorQ3TP92.

Family and domain databases

Gene3D3.40.50.1000. 1 hit.
InterProIPR011948. Dullard_phosphatase.
IPR023214. HAD-like_dom.
IPR004274. NIF.
[Graphical view]
PfamPF03031. NIF. 1 hit.
[Graphical view]
SMARTSM00577. CPDc. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR02251. HIF-SF_euk. 1 hit.
PROSITEPS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio323816.
PROQ3TP92.
SOURCESearch...

Entry information

Entry nameCNEP1_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot