ID   CNEPA_DANRE             Reviewed;         245 AA.
AC   Q5U395;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=CTD nuclear envelope phosphatase 1A;
DE            EC=3.1.3.16;
DE   AltName: Full=Serine/threonine-protein phosphatase dullard-A;
GN   Name=ctdnep1a; Synonyms=dullard;
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; BC085649; AAH85649.1; -; mRNA.
DR   RefSeq; NP_001007310.1; NM_001007309.1.
DR   AlphaFoldDB; Q5U395; -.
DR   SMR; Q5U395; -.
DR   STRING; 7955.ENSDARP00000036009; -.
DR   PaxDb; 7955-ENSDARP00000036009; -.
DR   GeneID; 492343; -.
DR   KEGG; dre:492343; -.
DR   AGR; ZFIN:ZDB-GENE-041114-177; -.
DR   CTD; 492343; -.
DR   ZFIN; ZDB-GENE-041114-177; ctdnep1a.
DR   eggNOG; KOG1605; Eukaryota.
DR   HOGENOM; CLU_020262_4_3_1; -.
DR   InParanoid; Q5U395; -.
DR   OMA; RIWGFFM; -.
DR   OrthoDB; 5473812at2759; -.
DR   PhylomeDB; Q5U395; -.
DR   TreeFam; TF313962; -.
DR   Reactome; R-DRE-4419969; Depolymerization of the Nuclear Lamina.
DR   PRO; PR:Q5U395; -.
DR   Proteomes; UP000000437; Alternate scaffold 5.
DR   Proteomes; UP000000437; Chromosome 5.
DR   Bgee; ENSDARG00000016519; Expressed in cleaving embryo and 28 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
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:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
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   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR011948; Dullard_phosphatase.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR   PANTHER; PTHR12210:SF70; CTD NUCLEAR ENVELOPE PHOSPHATASE 1; 1.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 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 1A"
FT                   /id="PRO_0000297970"
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;  28507 MW;  E98068959A2CCE2A CRC64;
     MLKTRQCLLG IRTFLGVTSR IWSFFLYILR KHLRTIIQYQ TVRYDILPLS PISRNRLNAV
     KRKILVLDLD ETLIHSHHDG VLRPTVRPGT PPDFILKVVI DKHPVRFFVH KRPHVDFFLE
     VVSQWYELVV FTASMEIYGS AVADKLDNNR GILKRRYYRQ HCTLDLGSYI KDLSVVHSDL
     SSIVILDNSP GAYRSHPDNA IPIKSWFSDP SDTALLNLLP MLDALRFTSD VRSVLSRNLH
     QHRLW
//