IED ID | IndEnz0005001093 |
Enzyme Type ID | lipase001093 |
Protein Name |
Arylacetamide deacetylase-like 2 EC 3.1.1.- |
Gene Name | AADACL2 |
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 | MGLKALCLGLLCVLFVSHFYTPMPDNIEESWKIMALDAIAKTCTFTAMCFENMRIMRYEEFISMIFRLDYTQPLSDEYITVTDTTFVDIPVRLYLPKRKSETRRRAVIYFHGGGFCFGSSKQRAFDFLNRWTANTLDAVVVGVDYRLAPQHHFPAQFEDGLAAVKFFLLEKILTKYGVDPTRICIAGDSSGGNLATAVTQQVQNDAEIKHKIKMQVLLYPGLQITDSYLPSHRENEHGIVLTRDVAIKLVSLYFTKDEALPWAMRRNQHMPLESRHLFKFVNWSILLPEKYRKDYVYTEPILGGLSYSLPGLTDSRALPLLANDSQLQNLPLTYILTCQHDLLRDDGLMYVTRLRNVGVQVVHEHIEDGIHGALSFMTSPFYLRLGLRIRDMYVSWLDKNL |
Enzyme Length | 401 |
Uniprot Accession Number | Q6P093 |
Absorption | |
Active Site | ACT_SITE 189; /evidence="ECO:0000250|UniProtKB:Q8BLF1, ECO:0000255|PROSITE-ProRule:PRU10038"; ACT_SITE 341; /evidence="ECO:0000250|UniProtKB:Q8BLF1"; ACT_SITE 371; /evidence="ECO:0000250|UniProtKB:Q8BLF1" |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.1.1.- |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Alternative sequence (2); Chain (1); Disulfide bond (1); Erroneous initiation (1); Motif (1); Natural variant (2); Sequence caution (1); Sequence conflict (1); Signal peptide (1) |
Keywords | Alternative splicing;Disulfide bond;Hydrolase;Reference proteome;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 111..113; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3 |
Gene Encoded By | |
Mass | 46,099 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |