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Q8JIL9 (CNEP1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine protein phosphatase that may dephosphorylate and activate lipins. 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. Induces neuronal differentiation by antagonizing BMP signaling. Acts both by dephosphorylating BMPR1A and by promoting BMPR2 proteasomal degradation. Ref.1 Ref.3

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Subunit structure

Interacts with bmpr1a, bmpr1b and bmpr2. Ref.3

Subcellular location

Membrane; Single-pass membrane protein Potential. Cytoplasmperinuclear region Ref.3.

Developmental stage

Expressed from egg to stage 35. Expression is restricted to the neural region as gastrulation proceeds, and is subsequently localized to neural tissues, branchial arches and pronephroi at the tail-bud stages. Ref.1

Sequence similarities

Belongs to the dullard family.

Contains 1 FCP1 homology domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCytoplasm
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Hydrolase
Protein phosphatase
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

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_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

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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_0000297972

Regions

Transmembrane7 – 2923Helical; Potential
Domain58 – 225168FCP1 homology

Experimental info

Mutagenesis671D → E: Strongly reduces phosphatase activity. Ref.3
Mutagenesis691D → E: Strongly reduces phosphatase activity. Ref.3
Sequence conflict541N → S in AAH82639. Ref.2
Sequence conflict1501G → A in AAH82639. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8JIL9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 57E95520F55D26CC

FASTA24428,169
        10         20         30         40         50         60 
MMRTPGLLGL RGFVAFAAKL WSFVLYLLRR QFRTIIQYQT VRYDVLPLSP ASRNRLSQVK 

        70         80         90        100        110        120 
RKVLVLDLDE TLIHSHHDGV LRPTVRPGTP PDFILKVVID KHPVRFFVHK RPHVDFFLEV 

       130        140        150        160        170        180 
VSQWYELVVF TASMEIYGSA VADKLDNNKG VLRRRFYRQH CTLELGSYIK DLSVVHSDLS 

       190        200        210        220        230        240 
SVVILDNSPG AYRSHPDNAI PIKSWFSDPS DTALLNLLPM LDALRFTADV RSVLSRNLHQ 


HRLW 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, FUNCTION.
Tissue: Embryo.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"Dullard promotes degradation and dephosphorylation of BMP receptors and is required for neural induction."
Satow R., Kurisaki A., Chan T.C., Hamazaki T.S., Asashima M.
Dev. Cell 11:763-774(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-67 AND ASP-69, INTERACTION WITH BMPR1A; BMPR1B AND BMPR2, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB084264 mRNA. Translation: BAB92973.1.
BC082639 mRNA. Translation: AAH82639.1.
RefSeqNP_001084192.1. NM_001090723.1.
NP_001090256.1. NM_001096787.1.
UniGeneXl.5594.
Xl.76057.

3D structure databases

ProteinModelPortalQ8JIL9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399358.
779162.
KEGGxla:399358.
xla:779162.

Organism-specific databases

CTD399358.
779162.
XenbaseXB-GENE-6254032. ctdnep1.

Phylogenomic databases

HOVERGENHBG098153.
KOK17617.

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...

Entry information

Entry nameCNEP1_XENLA
AccessionPrimary (citable) accession number: Q8JIL9
Secondary accession number(s): Q640I6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 55 of the entry and version 1 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