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Reviewed, UniProtKB/Swiss-Prot Q8JIL9 (DULRD_XENLA)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Serine/threonine-protein phosphatase dullard
    EC=3.1.3.16
Gene names
Name: dullard
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Serine/threonine phosphatase which may be required for proper nuclear membrane morphology By similarity. Induces neuronal differentiation by antagonizing BMP signaling. Acts both by dephosphorylating BMPR1A and by promoting BMPR2 proteasomal degradation.

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. Cytoplasmperinuclear region.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244Serine/threonine-protein phosphatase dullard
PRO_0000297972

Regions

Transmembrane7 – 2923 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
Q8JIL9-1 [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: 12083771] [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: 17141153] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-67 AND ASP-69, INTERACTION WITH BMPR1A; BMPR1B AND BMPR2, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

AB084264 mRNA. Translation: BAB92973.1.
BC082639 mRNA. Translation: AAH82639.1.
RefSeqNP_001084192.1.
NP_001090256.1.
UniGeneXl.5594
Xl.76057

3D structure databases

ModBaseSearch...

Genome annotation databases

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

Organism-specific databases

XenbaseXB-FEAT-5939295. dullard.

Phylogenomic databases

HOVERGENQ8JIL9.

Enzyme and pathway databases

BRENDA3.1.3.16. 648.

Family and domain databases

InterProIPR011948. Dullard.
IPR004274. NIF.
[Graphical view]
PfamPF03031. NIF. 1 hit.
[Graphical view]
SMARTSM00577. CPDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR02251. HIF-SF_euk. 1 hit.
PROSITEPS50969. FCP1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDULRD_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: June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectXenopus annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents