CNEPA_DANRE
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 03-AUG-2022, entry version 109.
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; Q5U395; -.
DR Ensembl; ENSDART00000029889; ENSDARP00000036009; ENSDARG00000016519.
DR Ensembl; ENSDART00000174856; ENSDARP00000143755; ENSDARG00000115280.
DR GeneID; 492343; -.
DR KEGG; dre:492343; -.
DR CTD; 492343; -.
DR ZFIN; ZDB-GENE-041114-177; ctdnep1a.
DR eggNOG; KOG1605; Eukaryota.
DR GeneTree; ENSGT01040000240503; -.
DR HOGENOM; CLU_020262_4_3_1; -.
DR InParanoid; Q5U395; -.
DR OMA; IPIRSWF; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q5U395; -.
DR TreeFam; TF313962; -.
DR PRO; PR:Q5U395; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000016519; Expressed in cleaving embryo and 28 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: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: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 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