CNEP1_RAT
ID CNEP1_RAT Reviewed; 244 AA.
AC Q3B7T6; Q5M952;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary, Placenta, and Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Serine/threonine protein phosphatase forming with CNEP1R1 an
CC active phosphatase complex that dephosphorylates and may activate LPIN1
CC and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze
CC the conversion of phosphatidic acid to diacylglycerol and control the
CC metabolism of fatty acids at different levels. May indirectly modulate
CC the lipid composition of nuclear and/or endoplasmic reticulum membranes
CC and be required for proper nuclear membrane morphology and/or dynamics.
CC May also indirectly regulate the production of lipid droplets and
CC triacylglycerol. May antagonize BMP signaling (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 CNEP1R1; the complex dephosphorylates LPIN1 and
CC LPIN2. {ECO:0000250}.
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; BU671232; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC087638; AAH87638.1; -; mRNA.
DR EMBL; BC107474; AAI07475.1; -; mRNA.
DR RefSeq; NP_001093964.1; NM_001100494.1.
DR AlphaFoldDB; Q3B7T6; -.
DR SMR; Q3B7T6; -.
DR STRING; 10116.ENSRNOP00000023379; -.
DR PaxDb; Q3B7T6; -.
DR GeneID; 287447; -.
DR KEGG; rno:287447; -.
DR UCSC; RGD:1310172; rat.
DR CTD; 23399; -.
DR RGD; 1310172; Ctdnep1.
DR VEuPathDB; HostDB:ENSRNOG00000017352; -.
DR eggNOG; KOG1605; Eukaryota.
DR HOGENOM; CLU_020262_4_3_1; -.
DR InParanoid; Q3B7T6; -.
DR OMA; IPIRSWF; -.
DR OrthoDB; 1176152at2759; -.
DR PhylomeDB; Q3B7T6; -.
DR Reactome; R-RNO-4419969; Depolymerisation of the Nuclear Lamina.
DR PRO; PR:Q3B7T6; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000017352; Expressed in skeletal muscle tissue and 20 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:0005634; C:nucleus; ISO:RGD.
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:0007276; P:gamete generation; ISO:RGD.
DR GO; GO:0007498; P:mesoderm development; ISO:RGD.
DR GO; GO:0006998; P:nuclear envelope organization; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; 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..244
FT /note="CTD nuclear envelope phosphatase 1"
FT /id="PRO_0000297969"
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"
FT CONFLICT 119
FT /note="E -> K (in Ref. 1; BU671232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 28391 MW; 1AD25540018F50BA CRC64;
MMRTQCLLGL RTFVAFAAKL WSFFIYLLRR QIRTVIQYQT VRYDILPLSP LSRNRLAQVK
RKILVLDLDE TLIHSHHDGV LRPTVRPGTP PDFILKVVID KHPVRFFVHK RPHVDFFLEV
VSQWYELVVF TASMEIYGSA VADKLDNSRS ILKRRYYRQH CTLELGSYIK DLSVVHSDLS
SIVILDNSPG AYRSHPDNAI PIKSWFSDPS DTALLNLLPM LDALRFTADV RSVLSRNLHQ
HRLW
