IED ID | IndEnz0002005884 |
Enzyme Type ID | protease005884 |
Protein Name |
Carboxypeptidase D EC 3.4.17.22 Metallocarboxypeptidase D gp180 |
Gene Name | Cpd |
Organism | Rattus norvegicus (Rat) |
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 Rattus Rattus norvegicus (Rat) |
Enzyme Sequence | MASGWDERPPWRLESLRLLPPPPLLLLLLLLRSSAQAAHIKKAEATTTTVGGSEAAEGQFDHYYHEAALGEALEAAAAAGPPGLARLFSIGNSVEGRPLWVLRLTAGLGPPPTPAAVGLDAAGPLLPGRPQVKLVGNMHGDETVSRQVLVYLARELASGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGLGDSGPPGTSGRDNSRGRDLNRSFPDQFSTGEPPSLDEVPEVRALIDWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKTTGIYSKTSDDEVFRYLAKAYASNHPIMRTGEPHCPGDEEETFKDGITNGAHWYDVEGGMQDYNYVWANCFEITLELSCCKYPPASQLRQEWENNRESLITLIEKVHIGIKGFVKDSVTGSGLENATISVAGINHNITTGRFGDFHRLLIPGSYNLTAVSPGYMPLTINNIVVKEGPATEIDFSLQPTVMSVVPDSTEAVTTPGTVAVPNIPPGTPSSHQPIQPKDFHHHHFPDMEIFLRRFANEYPNITRLYSLGKSVESRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVRSTRIHLMPSMNPDGYEKSQEGDSISVVGRNNSNNFDLNRNFPDQFVPITDPTQPETIAVMSWVKAYPFVLSANLHGGSLVVNYPYDDNEQGVATYSKSPDDAVFQQIALSYSKENSQMFQGRPCKDMYLNEYFPHGITNGASWYNVPGGMQDWNYLQTNCFEVTIELGCVKYPFEKELPKYWEQNRRSLIQFMKQVHQGVKGFVLDATDGRGILNATLSVAEINHPVTTYKAGDYWRLLVPGTYKITASARGYNPVTKNVTVRSEGAIQVNFTLVRSSTDANNESKKGKGHSTSTDDTSDPTSKEFEALIKHLSAENGLEGFMLSSSSDLALYRYHSYKDLSEFLRGLVMNYPHITNLTTLGQSVEYRHIWSLEISNKPNISEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCLNYKKNPVVTQLVDRTRIVIVPSLNPDGRERAQEKDCTSKTGHTNARGRDLDTDFTSNASQPETKAIIENLIQKQDFSLSIALDGGSVLVTYPYDKPVQTVENKETLKHLASLYANNHPSMHMGQPSCPNNSDENIPGGVMRGAEWHSHLGSMKDYSVTYGHCPEITVYTSCCYFPSAAQLPALWAENKKSLLSMLVEVHKGVHGLVKDKTGKPISKAVIVLNEGIRVHTKEGGYFHVLLAPGVHNINAIADGYQQQHSQVFVHHDAASSVVIVFDTDNRIFGLPRELVVTVSGATMSALILTACIIWCICSIKSNRHKDGFHRLRQHHDEYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH |
Enzyme Length | 1378 |
Uniprot Accession Number | Q9JHW1 |
Absorption | |
Active Site | ACT_SITE 762; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P14384 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Releases C-terminal Arg and Lys from polypeptides.; EC=3.4.17.22; Evidence={ECO:0000250|UniProtKB:Q90240}; |
DNA Binding | |
EC Number | 3.4.17.22 |
Enzyme Function | |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (2); Chain (1); Compositional bias (2); Glycosylation (15); Lipidation (3); Metal binding (6); Modified residue (6); Motif (1); Region (7); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) |
Keywords | Alternative splicing;Carboxypeptidase;Cell membrane;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Nucleus;Palmitate;Phosphoprotein;Protease;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix;Zinc |
Interact With | |
Induction | INDUCTION: [Isoform 2]: Up-regulated by exposure to prolactin or interleukin-2. {ECO:0000269|PubMed:11181555}. |
Subcellular Location | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:11181555}. |
Modified Residue | MOD_RES 265; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:O89001; MOD_RES 270; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O89001; MOD_RES 1356; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O75976; MOD_RES 1359; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O75976; MOD_RES 1366; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 1368; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:22673903 |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..37; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 15918796; |
Motif | MOTIF 162..164; /note=Cell attachment site; /evidence=ECO:0000255 |
Gene Encoded By | |
Mass | 152,616 |
Kinetics | |
Metal Binding | METAL 139; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 142; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 257; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 564; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 567; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 671; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P19222 |
Rhea ID | |
Cross Reference Brenda | 3.4.17.22; |