ID   NEPR1_PONAB             Reviewed;         125 AA.
AC   Q5R7J7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Nuclear envelope phosphatase-regulatory subunit 1;
DE   AltName: Full=Transmembrane protein 188;
GN   Name=CNEP1R1; Synonyms=TMEM188;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms with the serine/threonine protein phosphatase CTDNEP1
CC       an active complex which dephosphorylates and may activate LPIN1 and
CC       LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the
CC       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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CTDNEP1; the complex dephosphorylates LPIN1 and
CC       LPIN2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Filamentous pattern in the cytoplasm. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CNEP1R1 family. {ECO:0000305}.
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DR   EMBL; CR860118; CAH92263.1; -; mRNA.
DR   RefSeq; NP_001126325.1; NM_001132853.1.
DR   AlphaFoldDB; Q5R7J7; -.
DR   STRING; 9601.ENSPPYP00000008284; -.
DR   Ensembl; ENSPPYT00000041694; ENSPPYP00000045029; ENSPPYG00000007335.
DR   GeneID; 100173306; -.
DR   KEGG; pon:100173306; -.
DR   CTD; 255919; -.
DR   eggNOG; KOG4606; Eukaryota.
DR   GeneTree; ENSGT00390000008576; -.
DR   HOGENOM; CLU_138149_1_0_1; -.
DR   InParanoid; Q5R7J7; -.
DR   OMA; DQTVCED; -.
DR   TreeFam; TF313179; -.
DR   Proteomes; UP000001595; Chromosome 16.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0031965; C:nuclear membrane; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR   InterPro; IPR019168; NEP1-R1.
DR   PANTHER; PTHR20996; PTHR20996; 1.
DR   Pfam; PF09771; Tmemb_18A; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Lipid metabolism; Membrane; Nucleus;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..125
FT                   /note="Nuclear envelope phosphatase-regulatory subunit 1"
FT                   /id="PRO_0000286617"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N9A8"
SQ   SEQUENCE   125 AA;  14267 MW;  546EB9BEFE8EA593 CRC64;
     MNSLEQAEDL KAFERRLTEY IHCLQPATGR WRMLLIVVSV CTATGAWNWL IDPETQKVSF
     FTSLWNHPFF TISCITLIGL FFAGIHKRVV APSIIAARCR TVLAEYNMSC DDTGKLILKP
     RPHVQ