Detail Information for IndEnz0002005884
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;