CTD nuclear envelope phosphatase 1 - Xenopus laevis (African clawed frog)

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Q8JIL9 (CNEP1_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 50. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	244 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H₂O = a protein + phosphate.
Subunit structure	Interacts with bmpr1a, bmpr1b and bmpr2. Ref.3
Subcellular location	Membrane; Single-pass membrane protein Potential. Cytoplasm › perinuclear 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 process	Differentiation Neurogenesis
Cellular component	Cytoplasm Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Developmental protein Hydrolase Protein phosphatase
Gene Ontology (GO)
Biological_process	cell 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_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 perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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_0000297972

Regions

Transmembrane

7 – 29

Helical; Potential

Domain

58 – 225

168

FCP1 homology

Experimental info

Mutagenesis

D → E: Strongly reduces phosphatase activity. Ref.3

Mutagenesis

D → E: Strongly reduces phosphatase activity. Ref.3

Sequence conflict

N → S in AAH82639. Ref.2

Sequence conflict

150

G → A in AAH82639. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q8JIL9 [UniParc].

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

244

28,169

        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

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References

	« Hide 'large scale' referencesShow '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.
RefSeq	NP_001084192.1. NM_001090723.1. NP_001090256.1. NM_001096787.1.
UniGene	Xl.5594. Xl.76057.
3D structure databases
HSSP	HSSP built from PDB template 1TA0 based on UniProtKB Q9GZU7.
ProteinModelPortal	Q8JIL9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	399358. 779162.
KEGG	xla:399358. xla:779162.
Organism-specific databases
CTD	399358. 779162.
Xenbase	XB-GENE-6254032. ctdnep1.
Phylogenomic databases
HOVERGEN	HBG098153.
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_XENLA

Accession

Primary (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 3, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents