| IED ID | IndEnz0002018918 |
| Enzyme Type ID | protease018918 |
| Protein Name |
Cytosolic carboxypeptidase 1 EC 3.4.17.- EC 3.4.17.24 ATP/GTP-binding protein 1 Nervous system nuclear protein induced by axotomy protein 1 Protein deglutamylase CCP1 |
| Gene Name | Agtpbp1 Ccp1 Nna1 |
| Organism | Mus musculus (Mouse) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MSKLKVVGEKSLTNSSRVVGLLAQLEKINTDSTESDTARYVTSKILHLAQSQEKTRREMTTKGSTGMEVLLSTLENTKDLQTVLNILSILIELVSSGGGRRASFLVAKGGSQILLQLLMNASKDSPPHEEVMVQTHSILAKIGPKDKKFGVKARVNGALTVTLNLVKQHFQNYRLVLPCLQLLRVYSTNSVNSVSLGKNGVVELMFKIIGPFSKKNSGLMKVALDTLAALLKSKTNARRAVDRGYVQVLLTIYVDWHRHDNRHRNMLIRKGILQSLKSVTNIKLGRKAFIDANGMKILYNTSQECLAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSSFHFQLPIIPVTGPVAQLYSLPPEVDDVVDESDDNDDIDLEVENELENEDDLDQSFKNDDIETDINKLRPQQVPGRTIEELKMYEHLFPELVDDFQDYELISKEPKPFVFEGKARGPIVVPTAGEEVPGNSGSVKKGVVMKERASPKGEEAKEDPKGHDRTLPQQLGGQSRVAPSAHSFNNDLVKALDRITLQNVPSQVASGLNAGMRKDFGLPLTVLSCTKACPHVAKCGSTLFEGRTVHLGKLCCTGVETEDDEDTESHSSTEQAPSVEASDGPTLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHIPPPFKEPILERPYGVQRTKIAQDIERLIHQNDIIDRVVYDLDNPTYTTPEEGDTLKFNSKFESGNLRKVIQIRKSEYDLILNSDINSNHYHQWFYFEVSGMRPGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALNARPWWIRMGTDICYYKNHFSRSSVAAGGQKGKSYYTITFTVNFPHKDDVCYFAYHYPYTYSTLQMHLQKLESAHNPQQIYFRKDVLCETLSGNICPLVTITAMPESNYYEHICQFRTRPYIFLSARVHPGETNASWVMKGTLEYLMSNSPTAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQSPNPELHPTIYHAKGLLQYLAAVKRLPLVYCDYHGHSRKKNVFMYGCSIKETVWHTHDNSASCDIVEDMGYRTLPKILSHIAPAFCMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGRYKGLQIGTRELEEMGAKFCVGLLRLKRLTSSLEYNLPSNLLDFENDLIESSCKVTSPTTYVLDEDEPRFLEEVDYSAESNDELDVELAENTGDYEPSAQEEALSDSEVSRTHLI |
| Enzyme Length | 1218 |
| Uniprot Accession Number | Q641K1 |
| Absorption | |
| Active Site | ACT_SITE 962; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P00730 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623; Evidence={ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:22170066, ECO:0000269|PubMed:25103237, ECO:0000269|PubMed:29593216, ECO:0000269|PubMed:30420557};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000305|PubMed:21074048, ECO:0000305|PubMed:22170066, ECO:0000305|PubMed:25103237, ECO:0000305|PubMed:29593216, ECO:0000305|PubMed:30420557}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:22170066};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000305|PubMed:21074048, ECO:0000305|PubMed:22170066}; |
| DNA Binding | |
| EC Number | 3.4.17.-; 3.4.17.24 |
| Enzyme Function | FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins (PubMed:21074048, PubMed:22170066, PubMed:25103237, PubMed:30420557, PubMed:29593216). Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin (PubMed:22170066, PubMed:25103237, PubMed:30420557). Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate (PubMed:21074048). Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of alpha-tubulin as well as non-tubulin proteins such as MYLK (PubMed:21074048, PubMed:22170066). Involved in KLF4 deglutamylation which promotes KLF4 proteasome-mediated degradation, thereby negatively regulating cell pluripotency maintenance and embryogenesis (PubMed:29593216). {ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:22170066, ECO:0000269|PubMed:25103237, ECO:0000269|PubMed:29593216, ECO:0000269|PubMed:30420557}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (7); Chain (1); Compositional bias (1); Erroneous initiation (1); Metal binding (3); Modified residue (1); Mutagenesis (9); Natural variant (1); Region (3); Sequence conflict (10) |
| Keywords | Alternative splicing;Carboxypeptidase;Cytoplasm;Disease variant;Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Neurodegeneration;Nucleus;Phosphoprotein;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | INDUCTION: By axonal regeneration. {ECO:0000269|PubMed:11083920, ECO:0000269|PubMed:11884758}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPW5}. Cytoplasm, cytosol {ECO:0000269|PubMed:11083920}. Nucleus {ECO:0000269|PubMed:11083920}. Mitochondrion {ECO:0000269|PubMed:20620870}. Note=Localizes in both the cytoplasm and nuclei of interphase and dividing cells. {ECO:0000250|UniProtKB:Q9UPW5}. |
| Modified Residue | MOD_RES 1160; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UPW5 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10102304; 10197920; 10493779; 1061118; 10613519; 10630211; 10800965; 11217851; 11279275; 11529272; 11826084; 11853768; 1196386; 11984816; 12466851; 12479378; 12787313; 12787314; 1282111; 12866125; 1446244; 14610273; 1483388; 15051164; 15582153; 1565842; 1590945; 1623950; 16332269; 16356646; 16499884; 16602821; 16634962; 16943433; 16978877; 17244818; 17349613; 17663432; 1781951; 18799693; 18930027; 19200061; 19931625; 20061535; 200636; 2027034; 20484972; 2077109; 21052544; 21110128; 2123001; 21267068; 21700704; 21824473; 22133893; 2230805; 22835831; 2293612; 23047288; 23121602; 23219973; 23593366; 24791901; 25332286; 25416787; 26029065; 26433022; 26452267; 26819763; 26829768; 2707487; 2726749; 27333203; 27831556; 28104815; 28794449; 2901364; 29449678; 29474907; 2994831; 30225910; 30337352; 30420556; 30905767; 31932508; 32109557; 32290105; 32718435; 33004692; 3456566; 34637898; 3587363; 3619071; 3678603; 3988985; 3988986; 593342; 6144362; 7153374; 7153375; 7188319; 7479945; 7563251; 7666163; 7690917; 7891151; 7932867; 8013566; 8100981; 8132866; 8177535; 8194390; 8230318; 8326827; 8361659; 8381926; 8395631; 8541477; 8564845; 8575786; 8689037; 8738138; 8786457; 8830098; 8872304; 8910533; 9051257; 9171167; 9184992; 9259491; 9369330; 9501871; 9831049; 9878189; 9926858; |
| Motif | |
| Gene Encoded By | |
| Mass | 137,197 |
| Kinetics | |
| Metal Binding | METAL 912; /note=Zinc; /evidence=ECO:0000305; METAL 915; /note=Zinc; /evidence=ECO:0000305; METAL 1009; /note=Zinc; /evidence=ECO:0000250|UniProtKB:P00730 |
| Rhea ID | RHEA:60004; RHEA:60005; RHEA:63792; RHEA:63793 |
| Cross Reference Brenda | 3.4.17.24; |