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UniProtKB/Swiss-Prot entry Q8JIL9


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DULRD_XENLA
Primary accession number Q8JIL9
Secondary accession number Q640I6
Integrated into Swiss-Prot on August 21, 2007
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 22)
Name and origin of the protein
Protein name Serine/threonine-protein phosphatase dullard
Synonym EC 3.1.3.16
Gene name
Name: dullard
From
Xenopus laevis (African clawed frog) [TaxID: 8355] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND FUNCTION.
TISSUE=Embryo;
DOI=10.1016/S0006-291X(02)00641-1; PubMed=12083771 [NCBI, ExPASy, EBI, Israel, Japan]
Satow R., Chan T.C., Asashima M.;
"Molecular cloning and characterization of dullard: a novel gene required for neural development.";
Biochem. Biophys. Res. Commun. 295:85-91(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, MUTAGENESIS OF ASP-67 AND ASP-69, INTERACTION WITH BMPR1A; BMPR1B AND BMPR2, AND SUBCELLULAR LOCATION.
DOI=10.1016/j.devcel.2006.10.001; PubMed=17141153 [NCBI, ExPASy, EBI, Israel, Japan]
Satow R., Kurisaki A., Chan T.C., Hamazaki T.S., Asashima M.;
"Dullard promotes degradation and dephosphorylation of BMP receptors and is required for neural induction.";
Dev. Cell 11:763-774(2006).
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: Interacts with bmpr1a, bmpr1b and bmpr2.
  • SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (Potential). Cytoplasm, perinuclear 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.
  • SIMILARITY: Belongs to the dullard family.
  • SIMILARITY: Contains 1 FCP1 homology domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB084264; BAB92973.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC082639; AAH82639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001084192.1; -.
NP_001090256.1; -.
UniGene Xl.5594
3D structure databases
ModBase Q8JIL9.
Organism-specific databases
Xenbase XB-FEAT-5939295; dullard.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005635; Cellular component: nuclear envelope (inferred from sequence or structural similarity from UniProtKB).
GO:0004722; Molecular function: protein serine/threonine phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0030154; Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
GO:0007399; Biological process: nervous system development (inferred from electronic annotation from UniProtKB-KW).
GO:0006998; Biological process: nuclear envelope organization (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011948; Dullard.
IPR004274; NIF.
Graphical view of domain structure.
Pfam PF03031; NIF; 1.
Pfam graphical view of domain structure.
SMART SM00577; CPDc; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR02251; HIF-SF_euk; 1.
PROSITE PS50969; FCP1; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8JIL9.
Genome annotation databases
GeneID 399358; -.
779162; -.
KEGG xla:399358; -.
xla:779162; -.
Phylogenomic databases
HOVERGEN Q8JIL9; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Developmental protein; Differentiation; Hydrolase; Membrane; Neurogenesis; Protein phosphatase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   244  244     Serine/threonine-protein phosphatase dullard. PRO_0000297972
TRANSMEM   7    29  23     Potential. 
DOMAIN   58   225  168     FCP1 homology. 
MUTAGEN   67    67        D->E: Strongly reduces phosphatase activity. 
MUTAGEN   69    69        D->E: Strongly reduces phosphatase activity. 
CONFLICT   54    54        N -> S (in Ref. 2; AAH82639). 
CONFLICT   150   150        G -> A (in Ref. 2; AAH82639). 
Sequence information
Length: 244 AA [This is the length of the unprocessed precursor] Molecular weight: 28169 Da [This is the MW of the unprocessed precursor] CRC64: 57E95520F55D26CC [This is a checksum on the sequence]
        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 

Q8JIL9 in FASTA format

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