ID   CNEPB_DANRE             Reviewed;         245 AA.
AC   Q5U3T3;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=CTD nuclear envelope phosphatase 1B;
DE            EC=3.1.3.16;
DE   AltName: Full=Dullard-like protein;
DE   AltName: Full=Serine/threonine-protein phosphatase dullard-B;
GN   Name=ctdnep1b; Synonyms=dullardl;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (NOV-2004) 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. May antagonize BMP signaling (By
CC       similarity). {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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}. Nucleus membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dullard family. {ECO:0000305}.
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DR   EMBL; BC085403; AAH85403.1; -; mRNA.
DR   AlphaFoldDB; Q5U3T3; -.
DR   SMR; Q5U3T3; -.
DR   STRING; 7955.ENSDARP00000103636; -.
DR   PaxDb; Q5U3T3; -.
DR   ZFIN; ZDB-GENE-041114-152; ctdnep1b.
DR   eggNOG; KOG1605; Eukaryota.
DR   InParanoid; Q5U3T3; -.
DR   PhylomeDB; Q5U3T3; -.
DR   Reactome; R-DRE-4419969; Depolymerisation of the Nuclear Lamina.
DR   PRO; PR:Q5U3T3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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: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:0060322; P:head development; IMP:ZFIN.
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   Endoplasmic reticulum; Hydrolase; Membrane; Nucleus; Protein phosphatase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..245
FT                   /note="CTD nuclear envelope phosphatase 1B"
FT                   /id="PRO_0000297971"
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"
SQ   SEQUENCE   245 AA;  28504 MW;  3EE081D5A3BA78DF CRC64;
     MLKTRQCLLG VRTFHGVTSR IWSFFLYILR KHIRTIIQYQ TVRYDILSLS PISRNRLNNV
     KRKILVLDLD ETLIHSHHDG VLRPTVRPGT PPDFILKVVI DKHPVRFFVH KRPHVDFFLE
     VVSQWYELVV FTASMEIYGS AVADKLDNNK AILKRRYYRQ HCTLDSGSYI KDLSVVHDDL
     SSVVILDNSP GAYRSHPDNA IPIKSWFSDP SDTALLNLLP MLDALRFPAD VRSVLSRNLH
     QHRLW