Q1RMV9 (CNEP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 46.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: CTD nuclear envelope phosphatase 1 EC=3.1.3.16 Alternative name(s): Serine/threonine-protein phosphatase dullard | ||||
| Gene names |
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| Organism | Bos taurus (Bovine) [Reference proteome] | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 244 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at differents levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling By similarity. |
| Catalytic activity | A phosphoprotein + H2O = a protein + phosphate. |
| Subunit structure | Interacts with CNEP1R1; the complex dephosphorylates LPIN1 and LPIN2 By similarity. |
| Subcellular location | Endoplasmic reticulum membrane; Single-pass membrane protein By similarity. Nucleus membrane; Single-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the dullard family. Contains 1 FCP1 homology domain. |
Ontologies
Sequence annotation (Features)
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Uterus. |
Cross-references
Sequence databases | |
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| EMBL GenBank DDBJ | BC114677 mRNA. Translation: AAI14678.1. |
| IPI | IPI00688950. |
| RefSeq | NP_001039491.1. NM_001046026.1. |
| UniGene | Bt.27121. |
3D structure databases | |
| ProteinModelPortal | Q1RMV9. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9913.ENSBTAP00000025896. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000025896; ENSBTAP00000025896; ENSBTAG00000019443. |
| GeneID | 509192. |
| KEGG | bta:509192. |
Organism-specific databases | |
| CTD | 23399. |
Phylogenomic databases | |
| eggNOG | COG5190. |
| GeneTree | ENSGT00550000075053. |
| HOVERGEN | HBG098153. |
| InParanoid | Q1RMV9. |
| OMA | SRNRLGQ. |
| OrthoDB | EOG4J6RRP. |
Family and domain databases | |
| Gene3D | 3.40.50.1000. 1 hit. |
| InterPro | IPR011948. Dullard_phosphatase. IPR023214. HAD-like_dom. IPR004274. NIF. [Graphical view] |
| Pfam | PF03031. NIF. 1 hit. [Graphical view] |
| SMART | SM00577. CPDc. 1 hit. [Graphical view] |
| SUPFAM | SSF56784. HAD-like_dom. 1 hit. |
| TIGRFAMs | TIGR02251. HIF-SF_euk. 1 hit. |
| PROSITE | PS50969. FCP1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20868866. |
Entry information
| Entry name | CNEP1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q1RMV9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
