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DescriptionRecName: Full=Nuclear envelope phosphatase-regulatory subunit 1; AltName: Full=Transmembrane protein 188;
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MyHits synonymsNEPR1_BOVIN , Q3ZBP2 , 546EB9BEFE8EA593
match map segment
ipfam:Tmemb_18A  
Legends: 1, N-acetylmethionine. {ECO:0000250|UniProtKB:Q8N9A8}; 2, TRANSMEM Helical. {ECO:0000255}.
ID   NEPR1_BOVIN             Reviewed;         125 AA.
AC   Q3ZBP2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   02-NOV-2016, entry version 69.
DE   RecName: Full=Nuclear envelope phosphatase-regulatory subunit 1;
DE   AltName: Full=Transmembrane protein 188;
GN   Name=CNEP1R1; Synonyms=TMEM188;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms with the serine/threonine protein phosphatase
CC       CTDNEP1 an active complex which dephosphorylates and may activate
CC       LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases
CC       that catalyze the conversion of phosphatidic acid to
CC       diacylglycerol and control the metabolism of fatty acids at
CC       differents levels. May indirectly modulate the lipid composition
CC       of nuclear and/or endoplasmic reticulum membranes and be required
CC       for proper nuclear membrane morphology and/or dynamics. May also
CC       indirectly regulate the production of lipid droplets and
CC       triacylglycerol (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CTDNEP1; the complex dephosphorylates
CC       LPIN1 and 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}.
DR   EMBL; BC103188; AAI03189.1; -; mRNA.
DR   RefSeq; NP_001029475.1; NM_001034303.2.
DR   UniGene; Bt.65363; -.
DR   ProteinModelPortal; Q3ZBP2; -.
DR   STRING; 9913.ENSBTAP00000044208; -.
DR   PaxDb; Q3ZBP2; -.
DR   Ensembl; ENSBTAT00000046962; ENSBTAP00000044208; ENSBTAG00000033078.
DR   GeneID; 507593; -.
DR   KEGG; bta:507593; -.
DR   CTD; 255919; -.
DR   eggNOG; KOG4606; Eukaryota.
DR   eggNOG; ENOG4111N81; LUCA.
DR   GeneTree; ENSGT00390000008576; -.
DR   HOGENOM; HOG000285924; -.
DR   HOVERGEN; HBG107287; -.
DR   InParanoid; Q3ZBP2; -.
DR   OMA; WIHPVFT; -.
DR   OrthoDB; EOG091G19Y2; -.
DR   TreeFam; TF313179; -.
DR   Reactome; R-BTA-4419969; Depolymerisation of the Nuclear Lamina.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000033078; -.
DR   GO; GO:0005737; C:cytoplasm; 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: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   Pfam; PF09771; Tmemb_18A; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; Cytoplasm; Lipid metabolism; Membrane;
KW   Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN         1    125       Nuclear envelope phosphatase-regulatory
FT                                subunit 1.
FT                                /FTId=PRO_0000286614.
FT   TRANSMEM     33     53       Helical. {ECO:0000255}.
FT   TRANSMEM     65     85       Helical. {ECO:0000255}.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000250|UniProtKB:Q8N9A8}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         6    122       ipfam:Tmemb_18A [T]
SQ   SEQUENCE   125 AA;  14267 MW;  546EB9BEFE8EA593 CRC64;
     MNSLEQAEDL KAFERRLTEY IHCLQPATGR WRMLLIVVSV CTATGAWNWL IDPETQKVSF
     FTSLWNHPFF TISCITLIGL FFAGIHKRVV APSIIAARCR TVLAEYNMSC DDTGKLILKP
     RPHVQ
//