IED ID | IndEnz0002018916 |
Enzyme Type ID | protease018916 |
Protein Name |
Cytosolic carboxypeptidase 1 EC 3.4.17.- |
Gene Name | ccpp-1 F56H1.5 |
Organism | Caenorhabditis elegans |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
Enzyme Sequence | MPSDSDDVAAVKQPWSQLIVDISNFLSEHPQSKTSQALLPSCNGVWSDEEKLELIEAFGHKKQSHLTKSGVKAVLAAFEGDRTQPDVIFLCRLLHLIFSHFSSENDRKKEKYIVKCDVIATLTRITRKRIIMTLDVTDESSIDHNLDEVLWKLLHKIGLKDPRVSLKVRMGGLISPMCKLFIQKDTLPELFLPFFIKISRSPRNGQAIGRYEGFMTRLLVKIKALDASDQTSQVLLLDKHLQLLFFTMKNKRTRTQLLRENICKYLLEVLRRHLASSSNSRPTRLLSSLFGTFDKSLSAAHTEVVIGTIAILRLLSNFKKARDELKNLQVLDICSRELKEFWSDEWKTGPKSRIVDSLSALCLRCMSPLPYPLETRRFPIDFPLPTATPSTPGGHGRIRNSSSINISFDNGRSSDEDGMDEEDEAFVRDDDDEGKDDRGSDDDDGKDDDEINGALPKTTRLNPQQLAKYAPFFVENEQGTLQPTFSMIYQTNQESWRSICEKTRHVMPIHHHLPIEMFNTPTRIREKTAKTSNNMKKMIIEELDKPERSATSNQVIYDLDTAAFDGLPSPELPFVTGGGKLDTSKDLQFDSRFESGNLRMVIQVAPTHYELFLSPDVNQLRDHYQWFFFQVSNMRKSVKYTFEIVNCLKSTSLYSQGMQPVMYSMMESANGWRRVGENVCYFRNLYINENEEKKNVEEQKKKKYYYSIRFNVTFQNTGDICYIAYHYPYTYSFLNSSLSMLKKRKQENVYCREDVIGHSLAGNPIKMLTITTPASAAEIAAREVIVLSARVHPGETNASWIMQGILENLLCRQSNEMYRLRESFIFKIVPMINPDGVTNGSHRCSLAGIDLNRMWDRPNEALHPEVFATKAIIQYLCEVANKKPFAYVDIHGHSKKWDYFVYGNNASESWRADDVLDVGAAQLEEELHLALPKALEATCPSRFNASECRFNITRAKESSARVNVWRQFGVSTAYTLESTFCGFHKGQNSGYQINTSDLKEIGRDLLHSFLEMTKT |
Enzyme Length | 1015 |
Uniprot Accession Number | O76373 |
Absorption | |
Active Site | ACT_SITE 843; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00730 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.17.- |
Enzyme Function | FUNCTION: Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation of proteins such as tubulins (Probable). Via the deglutamylation of tubulin, regulates the localization and velocity of kinesin motors and the structural integrity of microtubules in sensory cilia (PubMed:21982591, PubMed:29129530). In male CEM sensory neurons, regulates the cilia release of bioactive extracellular vesicles (PubMed:29129530). Also regulates microtubule dynamics in uterine muscle cells (PubMed:24780738). {ECO:0000269|PubMed:21982591, ECO:0000269|PubMed:24780738, ECO:0000269|PubMed:29129530, ECO:0000305|PubMed:21982591, ECO:0000305|PubMed:29129530}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Compositional bias (2); Metal binding (3); Mutagenesis (1); Region (1) |
Keywords | Carboxypeptidase;Cell projection;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:21982591}. Cell projection, cilium {ECO:0000269|PubMed:21982591}. Cell projection, dendrite {ECO:0000269|PubMed:21982591}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10778742; 11381264; 16600994; 17164286; 17854888; 18407554; 19343510; 20439774; 21085631; 21177967; 21367940; 22267497; 22286215; 22347378; 22560298; 23800452; 24884423; 25487147; 33064774; 6593563; |
Motif | |
Gene Encoded By | |
Mass | 116,056 |
Kinetics | |
Metal Binding | METAL 792; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730; METAL 795; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730; METAL 891; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730 |
Rhea ID | |
Cross Reference Brenda | 3.4.17.24; |