ID   DULRD_XENLA             Reviewed;         244 AA.
AC   Q8JIL9; Q640I6;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Serine/threonine-protein phosphatase dullard;
DE            EC=3.1.3.16;
GN   Name=dullard;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND FUNCTION.
RC   TISSUE=Embryo;
RX   MEDLINE=22078992; PubMed=12083771; DOI=10.1016/S0006-291X(02)00641-1;
RA   Satow R., Chan T.C., Asashima M.;
RT   "Molecular cloning and characterization of dullard: a novel gene
RT   required for neural development.";
RL   Biochem. Biophys. Res. Commun. 295:85-91(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, MUTAGENESIS OF ASP-67 AND ASP-69, INTERACTION WITH BMPR1A;
RP   BMPR1B AND BMPR2, AND SUBCELLULAR LOCATION.
RX   PubMed=17141153; DOI=10.1016/j.devcel.2006.10.001;
RA   Satow R., Kurisaki A., Chan T.C., Hamazaki T.S., Asashima M.;
RT   "Dullard promotes degradation and dephosphorylation of BMP receptors
RT   and is required for neural induction.";
RL   Dev. Cell 11:763-774(2006).
CC   -!- FUNCTION: Serine/threonine phosphatase which may be required for
CC       proper nuclear membrane morphology (By similarity). Induces
CC       neuronal differentiation by antagonizing BMP signaling. Acts both
CC       by dephosphorylating BMPR1A and by promoting BMPR2 proteasomal
CC       degradation.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBUNIT: Interacts with bmpr1a, bmpr1b and bmpr2.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential). Cytoplasm, perinuclear region.
CC   -!- DEVELOPMENTAL STAGE: Expressed from egg to stage 35. Expression is
CC       restricted to the neural region as gastrulation proceeds, and is
CC       subsequently localized to neural tissues, branchial arches and
CC       pronephroi at the tail-bud stages.
CC   -!- SIMILARITY: Belongs to the dullard family.
CC   -!- SIMILARITY: Contains 1 FCP1 homology domain.
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DR   EMBL; AB084264; BAB92973.1; -; mRNA.
DR   EMBL; BC082639; AAH82639.1; -; mRNA.
DR   RefSeq; NP_001084192.1; -.
DR   RefSeq; NP_001090256.1; -.
DR   UniGene; Xl.5594; -.
DR   UniGene; Xl.76057; -.
DR   GeneID; 399358; -.
DR   GeneID; 779162; -.
DR   KEGG; xla:399358; -.
DR   KEGG; xla:779162; -.
DR   Xenbase; XB-FEAT-5939295; dullard.
DR   HOVERGEN; Q8JIL9; -.
DR   BRENDA; 3.1.3.16; 648.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR   InterPro; IPR011948; Dullard.
DR   InterPro; IPR004274; NIF.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   TIGRFAMs; TIGR02251; HIF-SF_euk; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Differentiation; Hydrolase;
KW   Membrane; Neurogenesis; Protein phosphatase; Transmembrane.
FT   CHAIN         1    244       Serine/threonine-protein phosphatase
FT                                dullard.
FT                                /FTId=PRO_0000297972.
FT   TRANSMEM      7     29       Potential.
FT   DOMAIN       58    225       FCP1 homology.
FT   MUTAGEN      67     67       D->E: Strongly reduces phosphatase
FT                                activity.
FT   MUTAGEN      69     69       D->E: Strongly reduces phosphatase
FT                                activity.
FT   CONFLICT     54     54       N -> S (in Ref. 2; AAH82639).
FT   CONFLICT    150    150       G -> A (in Ref. 2; AAH82639).
SQ   SEQUENCE   244 AA;  28169 MW;  57E95520F55D26CC CRC64;
     MMRTPGLLGL RGFVAFAAKL WSFVLYLLRR QFRTIIQYQT VRYDVLPLSP ASRNRLSQVK
     RKVLVLDLDE TLIHSHHDGV LRPTVRPGTP PDFILKVVID KHPVRFFVHK RPHVDFFLEV
     VSQWYELVVF TASMEIYGSA VADKLDNNKG VLRRRFYRQH CTLELGSYIK DLSVVHSDLS
     SVVILDNSPG AYRSHPDNAI PIKSWFSDPS DTALLNLLPM LDALRFTADV RSVLSRNLHQ
     HRLW
//