CNEP1_XENLA
ID CNEP1_XENLA Reviewed; 244 AA.
AC Q8JIL9; Q640I6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=CTD nuclear envelope phosphatase 1;
DE EC=3.1.3.16;
DE AltName: Full=Serine/threonine-protein phosphatase dullard;
GN Name=ctdnep1; Synonyms=dullard;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND FUNCTION.
RC TISSUE=Embryo;
RX 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 required
RT 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; BMPR1B
RP 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 and is
RT required for neural induction.";
RL Dev. Cell 11:763-774(2006).
CC -!- FUNCTION: Serine/threonine protein phosphatase that may dephosphorylate
CC and activate lipins. Lipins are phosphatidate phosphatases that
CC catalyze the conversion of phosphatidic acid to diacylglycerol and
CC control the metabolism of fatty acids at different levels. May
CC indirectly modulate the lipid composition of nuclear and/or endoplasmic
CC reticulum membranes and be required for proper nuclear membrane
CC morphology and/or dynamics. May also indirectly regulate the production
CC of lipid droplets and triacylglycerol (By similarity). Induces neuronal
CC differentiation by antagonizing BMP signaling. Acts both by
CC dephosphorylating BMPR1A and by promoting BMPR2 proteasomal
CC degradation. {ECO:0000250, ECO:0000269|PubMed:12083771,
CC ECO:0000269|PubMed:17141153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Interacts with bmpr1a, bmpr1b and bmpr2.
CC {ECO:0000269|PubMed:17141153}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:17141153}.
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. {ECO:0000269|PubMed:12083771}.
CC -!- SIMILARITY: Belongs to the dullard family. {ECO:0000305}.
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DR EMBL; AB084264; BAB92973.1; -; mRNA.
DR EMBL; BC082639; AAH82639.1; -; mRNA.
DR RefSeq; NP_001084192.1; NM_001090723.1.
DR RefSeq; NP_001090256.1; NM_001096787.1.
DR AlphaFoldDB; Q8JIL9; -.
DR SMR; Q8JIL9; -.
DR DNASU; 779162; -.
DR GeneID; 399358; -.
DR GeneID; 779162; -.
DR KEGG; xla:399358; -.
DR KEGG; xla:779162; -.
DR CTD; 399358; -.
DR CTD; 779162; -.
DR Xenbase; XB-GENE-6254032; ctdnep1.L.
DR Xenbase; XB-GENE-5939350; ctdnep1.S.
DR OMA; IPIRSWF; -.
DR OrthoDB; 1176152at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 399358; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071595; C:Nem1-Spo7 phosphatase complex; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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 GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; SSF56784; 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; Membrane;
KW Neurogenesis; Protein phosphatase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..244
FT /note="CTD nuclear envelope phosphatase 1"
FT /id="PRO_0000297972"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 58..225
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT MUTAGEN 67
FT /note="D->E: Strongly reduces phosphatase activity."
FT /evidence="ECO:0000269|PubMed:17141153"
FT MUTAGEN 69
FT /note="D->E: Strongly reduces phosphatase activity."
FT /evidence="ECO:0000269|PubMed:17141153"
FT CONFLICT 54
FT /note="N -> S (in Ref. 2; AAH82639)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="G -> A (in Ref. 2; AAH82639)"
FT /evidence="ECO:0000305"
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
