| IED ID | IndEnz0002004150 |
| Enzyme Type ID | protease004150 |
| Protein Name |
Serine beta-lactamase-like protein LACTB, mitochondrial EC 3.4.-.- |
| Gene Name | LACTB MRPL56 UNQ843/PRO1781 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MYRLMSAVTARAAAPGGLASSCGRRGVHQRAGLPPLGHGWVGGLGLGLGLALGVKLAGGLRGAAPAQSPAAPDPEASPLAEPPQEQSLAPWSPQTPAPPCSRCFARAIESSRDLLHRIKDEVGAPGIVVGVSVDGKEVWSEGLGYADVENRVPCKPETVMRIASISKSLTMVALAKLWEAGKLDLDIPVQHYVPEFPEKEYEGEKVSVTTRLLISHLSGIRHYEKDIKKVKEEKAYKALKMMKENVAFEQEKEGKSNEKNDFTKFKTEQENEAKCRNSKPGKKKNDFEQGELYLREKFENSIESLRLFKNDPLFFKPGSQFLYSTFGYTLLAAIVERASGCKYLDYMQKIFHDLDMLTTVQEENEPVIYNRARFYVYNKKKRLVNTPYVDNSYKWAGGGFLSTVGDLLKFGNAMLYGYQVGLFKNSNENLLPGYLKPETMVMMWTPVPNTEMSWDKEGKYAMAWGVVERKQTYGSCRKQRHYASHTGGAVGASSVLLVLPEELDTETINNKVPPRGIIVSIICNMQSVGLNSTALKIALEFDKDRSD |
| Enzyme Length | 547 |
| Uniprot Accession Number | P83111 |
| Absorption | |
| Active Site | ACT_SITE 164; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:P15555 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Mitochondrial serine protease that acts as a regulator of mitochondrial lipid metabolism (PubMed:28329758). Acts by decreasing protein levels of PISD, a mitochondrial enzyme that converts phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn), thereby affecting mitochondrial lipid metabolism (PubMed:28329758). It is unclear whether it acts directly by mediating proteolysis of PISD or by mediating proteolysis of another lipid metabolism protein (PubMed:28329758). Acts as a tumor suppressor that has the ability to inhibit proliferation of multiple types of breast cancer cells: probably by promoting decreased levels of PISD, thereby affecting mitochondrial lipid metabolism (PubMed:28329758). {ECO:0000269|PubMed:28329758}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Modified residue (4); Natural variant (1); Region (1); Sequence conflict (1); Transit peptide (1) |
| Keywords | Acetylation;Alternative splicing;Hydrolase;Lipid metabolism;Mitochondrion;Protease;Reference proteome;Transit peptide;Tumor suppressor |
| Interact With | |
| Induction | INDUCTION: Down-regulated in a number of cancer cells. {ECO:0000269|PubMed:28329758}. |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11551941, ECO:0000269|PubMed:19858488, ECO:0000269|PubMed:28329758}. |
| Modified Residue | MOD_RES 283; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9EP89; MOD_RES 284; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9EP89; MOD_RES 297; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9EP89; MOD_RES 342; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12164938; 18538381; 20877624; 21182203; 21182205; 25609649; 26496610; 26603571; 28835318; 29899406; 33152401; 33507917; 33675985; 34362477; |
| Motif | |
| Gene Encoded By | |
| Mass | 60,694 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |