G5EBX9 · PPE_CAEEL
- ProteinSerine/threonine-protein phosphatase with EF-hands pef-1
- Genepef-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids707 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probably acts as a protein phosphatase.
Catalytic activity
- H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Cofactor
Note: Binds 2 manganese ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 256 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 258 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 285 | Mn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 285 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 317 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Active site | 318 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 369 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 465 | Mn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 642 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 644 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 646 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 648 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 653 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 682 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 684 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 686 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 693 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cilium | |
Cellular Component | cytosol | |
Cellular Component | dendrite | |
Cellular Component | neuronal cell body | |
Cellular Component | nucleus | |
Cellular Component | perikaryon | |
Cellular Component | plasma membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | iron ion binding | |
Molecular Function | manganese ion binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | protein serine/threonine phosphatase activity | |
Biological Process | detection of stimulus involved in sensory perception |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein phosphatase with EF-hands pef-1
- EC number
- Short namesCePPEF
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionG5EBX9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 2 | Loss of palmitoylation and myristoylation resulting in loss of association with the cell membrane. Severe loss of axonal, dendritic and cilia localization in AWC, AWB and BAG neurons. | ||||
Sequence: G → A | ||||||
Mutagenesis | 3 | Loss of palmitoylation resulting in loss of association with the cell membrane. Moderate loss of axonal, dendritic and cilia localization in AWC, AWB and BAG neurons. | ||||
Sequence: C → S |
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000436235 | 2-707 | Serine/threonine-protein phosphatase with EF-hands pef-1 | |||
Sequence: GCGPSSGRQNPSTELKKSTRATTTTTSSSQRNNYNDNNQNTSSSSGNKKESSSSSKQHSSKKSKKSNSKKNRSPSPQPQLTIKSAILIQKWYRRCEARLEARRRATWQIFTALEYAGEQDQLKLYDFFADVIRAMAEENGKGGVENGRNSPLMSALSHYAKPSLMDSEGETVKKMLEDTSPTNVDIDRNYKGPTLSLPLDKPQVAKMIEAFKVNKVLHPKYVLMILHEARKIFKAMPSVSRISTSISNQVTICGDLHGKFDDLCIILYKNGYPSVDNPYIFNGDFVDRGGQSIEVLCVLFALVIVDPMSIYLNRGNHEDHIMNLRYGFIKELSTKYKDLSTPITRLLEDVFSWLPIATIIDRDIFVVHGGISDQTEVSKLDKIPRHRFQSVLRPPVNKGMESEKENSAVNVDEWKQMLDIMWSDPKQNKGCWPNVFRGGGSYFGADITASFLEKHGFRLLVRSHECKFEGYEFSHNNTCLTVFSASNYYETGSNRGAYVKFIGKSKQPHFVQYMASKTHRKSTLRERLGVVEESAVKELKEKLSSFHTDLQKEFEIMDIEKSGKLPILKWSDCVERITGLNLPWIALAPKVATLSEDGKYVMYKEDRRIAQVGGTHAQEKDIVESLYRHKSTLETLFRFMDKDNSGQVSMKEFIDACEVLGKYTKRPLQTDYISQIAESIDFNKDGFIDLNELLEAFRLVDRPLLR | ||||||
Lipidation | 3 | S-palmitoyl cysteine | ||||
Sequence: C |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expression is restricted to neurons. Expressed in AWB, AWC, AVA, AVB, AVX, BAG and URX neurons and in one tail neuron (at protein level).
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-54 | Polar residues | ||||
Sequence: MGCGPSSGRQNPSTELKKSTRATTTTTSSSQRNNYNDNNQNTSSSSGNKKESSS | ||||||
Region | 1-82 | Disordered | ||||
Sequence: MGCGPSSGRQNPSTELKKSTRATTTTTSSSQRNNYNDNNQNTSSSSGNKKESSSSSKQHSSKKSKKSNSKKNRSPSPQPQLT | ||||||
Domain | 81-103 | IQ | ||||
Sequence: LTIKSAILIQKWYRRCEARLEAR | ||||||
Region | 205-518 | Catalytic | ||||
Sequence: VAKMIEAFKVNKVLHPKYVLMILHEARKIFKAMPSVSRISTSISNQVTICGDLHGKFDDLCIILYKNGYPSVDNPYIFNGDFVDRGGQSIEVLCVLFALVIVDPMSIYLNRGNHEDHIMNLRYGFIKELSTKYKDLSTPITRLLEDVFSWLPIATIIDRDIFVVHGGISDQTEVSKLDKIPRHRFQSVLRPPVNKGMESEKENSAVNVDEWKQMLDIMWSDPKQNKGCWPNVFRGGGSYFGADITASFLEKHGFRLLVRSHECKFEGYEFSHNNTCLTVFSASNYYETGSNRGAYVKFIGKSKQPHFVQYMASK | ||||||
Domain | 546-581 | EF-hand 1 | ||||
Sequence: SFHTDLQKEFEIMDIEKSGKLPILKWSDCVERITGL | ||||||
Domain | 629-664 | EF-hand 2 | ||||
Sequence: RHKSTLETLFRFMDKDNSGQVSMKEFIDACEVLGKY | ||||||
Domain | 669-704 | EF-hand 3 | ||||
Sequence: LQTDYISQIAESIDFNKDGFIDLNELLEAFRLVDRP |
Sequence similarities
Belongs to the PPP phosphatase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
G5EBX9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Namea
- Length707
- Mass (Da)80,330
- Last updated2011-12-14 v1
- Checksum1943CE218D0A7EF7
G5EBX9-2
- Nameb
- Differences from canonical
- 1-135: Missing
G5EBX9-3
- Namec
- Differences from canonical
- 17-81: Missing
Features
Showing features for compositional bias, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF023454 EMBL· GenBank· DDBJ | AAB82794.1 EMBL· GenBank· DDBJ | mRNA | ||
BX284603 EMBL· GenBank· DDBJ | CCD69949.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284603 EMBL· GenBank· DDBJ | CCD69950.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284603 EMBL· GenBank· DDBJ | CCD69954.1 EMBL· GenBank· DDBJ | Genomic DNA |