ID   CNEP1_XENTR             Reviewed;         244 AA.
AC   Q28HW9;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
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; ORFNames=TEgg035l07.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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. Induces neuronal differentiation
CC       by antagonizing BMP signaling. Acts both by dephosphorylating BMPR1A
CC       and by promoting BMPR2 proteasomal degradation (By similarity).
CC       {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dullard family. {ECO:0000305}.
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DR   EMBL; CR760700; CAJ82232.1; -; mRNA.
DR   RefSeq; NP_001017177.1; NM_001017177.2.
DR   AlphaFoldDB; Q28HW9; -.
DR   SMR; Q28HW9; -.
DR   STRING; 8364.ENSXETP00000014538; -.
DR   PaxDb; Q28HW9; -.
DR   GeneID; 549931; -.
DR   KEGG; xtr:549931; -.
DR   CTD; 23399; -.
DR   Xenbase; XB-GENE-5939296; ctdnep1.
DR   eggNOG; KOG1605; Eukaryota.
DR   HOGENOM; CLU_020262_6_0_1; -.
DR   InParanoid; Q28HW9; -.
DR   OrthoDB; 1176152at2759; -.
DR   Reactome; R-XTR-4419969; Depolymerisation of the Nuclear Lamina.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
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:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
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   2: Evidence at transcript 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_0000297973"
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          57..224
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
SQ   SEQUENCE   244 AA;  28149 MW;  92C5AD45DEB2BD73 CRC64;
     MMRTPGLLGL RGFVAFAAKL WSFVLYLLRR QVRTIIQYQT VRYDVLPLSP ASRNRLSQVK
     RKVLVLDLDE TLIHSHHDGV LRPTVRPGTP PDFILKVVID KHPVRFFVHK RPHVDFFLEV
     VSQWYELVVF TASMEIYGSA VADKLDNNRG VLRRRFYRQH CTLELGSYIK DLSVVHSDLS
     SVVILDNSPG AYRSHPDNAI PIKSWFSDPS DTALLNLLPM LDALRFTADV RSVLSRNLHQ
     HRLW