Q5BKX5 · ACTMP_HUMAN
- ProteinActin maturation protease
- GeneACTMAP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids351 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cleaves N-terminal acetylated methionine of immature cytoplasmic beta- and gamma-actins ACTB and ACTG1 after translation (PubMed:36173861).
Cleaves N-terminal acetylated cysteine of muscle alpha-actins ACTA1, ACTC1 and ACTA2 after canonical removal of N-terminal methionine (By similarity).
Catalytic activity
Actin maturation protease
H2O + N-terminal N(alpha)-acetyl-L-methionyl-L-aspartyl-[protein] = N(alpha)-acetyl-L-methionine + N-terminal L-aspartyl-[protein]This reaction proceeds in the forward direction.Actin maturation protease
H2O + N-terminal N(alpha)-acetyl-L-methionyl-L-glutamyl-[protein] = N(alpha)-acetyl-L-methionine + N-terminal L-glutamyl-[protein]This reaction proceeds in the forward direction.Actin maturation protease
H2O + N-terminal N(alpha)-acetyl-L-cysteinyl-L-aspartyl-[protein] = N-acetyl-L-cysteine + N-terminal L-aspartyl-[protein]This reaction proceeds in the forward direction.Actin maturation protease
H2O + N-terminal N(alpha)-acetyl-L-cysteinyl-L-glutamyl-[protein] = N-acetyl-L-cysteine + N-terminal L-glutamyl-[protein]This reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 132 | |||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | cysteine-type aminopeptidase activity | |
Molecular Function | initiator methionyl aminopeptidase activity | |
Biological Process | protein processing |
Keywords
- Molecular function
Enzyme and pathway databases
Responsible for the noncanonical excision of the acetylated methionine of actin molecules after translation.
Names & Taxonomy
Protein names
- Recommended nameActin maturation protease
- EC number
- Alternative names
Gene names
- Community suggested namesACTMAP; C19orf54; actin maturation protease.
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5BKX5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 132 | Catalytically inactive, disrupts N-terminal cleavage of immature actin. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 420 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000297659 | 1-351 | UniProt | Actin maturation protease | |||
Sequence: MTSPCSPPLKPPISPPKTPVPQASSIPSPPLPPSPLDFSALPSPPWSQQTPVPPPLPLPPPPAATGPAPRHVFGLEKSQLLKEAFDKAGPVPKGREDVKRLLKLHKDRFRGDLRWILFCADLPSLIQEGPQCGLVALWMAGTLLSPPSGVPLERLIRVATERGYTAQGEMFSVADMGRLAQEVLGCQAKLLSGGLGGPNRDLVLQHLVTGHPLLIPYDEDFNHEPCQRKGHKAHWAVSAGVLLGVRAVPSLGYTEDPELPGLFHPVLGTPCQPPSLPEEGSPGAVYLLSKQGKSWHYQLWDYDQVRESNLQLTDFSPSRATDGRVYVVPVGGVRAGLCGQALLLTPQDCSH | |||||||
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 316 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 316 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with PFN1 (PubMed:36173861).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-67 | Pro residues | ||||
Sequence: MTSPCSPPLKPPISPPKTPVPQASSIPSPPLPPSPLDFSALPSPPWSQQTPVPPPLPLPPPPAATGP | ||||||
Region | 1-70 | Disordered | ||||
Sequence: MTSPCSPPLKPPISPPKTPVPQASSIPSPPLPPSPLDFSALPSPPWSQQTPVPPPLPLPPPPAATGPAPR | ||||||
Region | 124-244 | Peptidase C39-like | ||||
Sequence: SLIQEGPQCGLVALWMAGTLLSPPSGVPLERLIRVATERGYTAQGEMFSVADMGRLAQEVLGCQAKLLSGGLGGPNRDLVLQHLVTGHPLLIPYDEDFNHEPCQRKGHKAHWAVSAGVLLG |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q5BKX5-1
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.
- Name1
- Length351
- Mass (Da)37,779
- Last updated2010-10-05 v2
- ChecksumB1CE78515DC3A553
Q5BKX5-2
- Name2
- Differences from canonical
- 1-216: MTSPCSPPLKPPISPPKTPVPQASSIPSPPLPPSPLDFSALPSPPWSQQTPVPPPLPLPPPPAATGPAPRHVFGLEKSQLLKEAFDKAGPVPKGREDVKRLLKLHKDRFRGDLRWILFCADLPSLIQEGPQCGLVALWMAGTLLSPPSGVPLERLIRVATERGYTAQGEMFSVADMGRLAQEVLGCQAKLLSGGLGGPNRDLVLQHLVTGHPLLIP → MRAGGLVDGRYSPVAPQWRPPGETHTGGHGKRLHGPGRDVLSTS
- 305-351: VRESNLQLTDFSPSRATDGRVYVVPVGGVRAGLCGQALLLTPQDCSH → GPPLSSH
Q5BKX5-3
- Name3
- Differences from canonical
- 1-216: MTSPCSPPLKPPISPPKTPVPQASSIPSPPLPPSPLDFSALPSPPWSQQTPVPPPLPLPPPPAATGPAPRHVFGLEKSQLLKEAFDKAGPVPKGREDVKRLLKLHKDRFRGDLRWILFCADLPSLIQEGPQCGLVALWMAGTLLSPPSGVPLERLIRVATERGYTAQGEMFSVADMGRLAQEVLGCQAKLLSGGLGGPNRDLVLQHLVTGHPLLIP → MRAGGLVDGRYSPVAPQWRPPGETHTGGHGKRLHGPGRDVLSTS
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-67 | Pro residues | ||||
Sequence: MTSPCSPPLKPPISPPKTPVPQASSIPSPPLPPSPLDFSALPSPPWSQQTPVPPPLPLPPPPAATGP | ||||||
Alternative sequence | VSP_039884 | 1-216 | in isoform 2 and isoform 3 | |||
Sequence: MTSPCSPPLKPPISPPKTPVPQASSIPSPPLPPSPLDFSALPSPPWSQQTPVPPPLPLPPPPAATGPAPRHVFGLEKSQLLKEAFDKAGPVPKGREDVKRLLKLHKDRFRGDLRWILFCADLPSLIQEGPQCGLVALWMAGTLLSPPSGVPLERLIRVATERGYTAQGEMFSVADMGRLAQEVLGCQAKLLSGGLGGPNRDLVLQHLVTGHPLLIP → MRAGGLVDGRYSPVAPQWRPPGETHTGGHGKRLHGPGRDVLSTS | ||||||
Sequence conflict | 70 | in Ref. 3; BC020262 | ||||
Sequence: R → P | ||||||
Alternative sequence | VSP_039885 | 305-351 | in isoform 2 | |||
Sequence: VRESNLQLTDFSPSRATDGRVYVVPVGGVRAGLCGQALLLTPQDCSH → GPPLSSH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK298068 EMBL· GenBank· DDBJ | BAG60359.1 EMBL· GenBank· DDBJ | mRNA | ||
AC020945 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC020262 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC090894 EMBL· GenBank· DDBJ | AAH90894.1 EMBL· GenBank· DDBJ | mRNA |