Detail Information for IndEnz0002018939
IED ID IndEnz0002018939
Enzyme Type ID protease018939
Protein Name Carboxypeptidase D
EC 3.4.17.22
Metallocarboxypeptidase D
gp180
Gene Name Cpd
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 MASGRDERPPWRLGRLRLLPPPPLLLLLLLLRSSAQAAHIKKAEATTTTVGGSEAAEGQFDHYYHEAALGEALEAAAAAGPPGLARLFSIGSSVEGRPLWVLRLTAGLGPPPTAAAGLDAAGPLLPGRPQVKLVGNMHGDETVSRQVLVYLARELASGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGLGDSGPPGTSGRDNSRGRDLNRSFPDQFSTGEPPSLDEVPEVRALIDWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKTTGLYSKTSDDEVFRYLAKAYASNHPIMKTGEPHCPGDEDETFKDGITNGAHWYDVEGGMQDYNYVWANCFEITLELSCCKYPPASQLRQEWENNRESLITLIEKVHIGIKGFVKDSVTGSGLENATISVAGINHNITTGRFGDFHRLLVPGTYNLTALSTGYMPLTINNIMVKEGPATEMDFSLRPTVMSVMPGSTEAVTTPGTVAVPNIPPGTPSSHQPIQPKDFHHHHFPDMEIFLRRFANEYPNITRLYSLGKSVESRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVRSTRIHLMPSMNPDGYEKSQEGDSISVVGRNNSNNFDLNRNFPDQFVPITEPTQPETIAVMSWVKAYPFVLSANLHGGSLVVNYPYDDNEQGVATYSKSPDDAVFQQIALSYSKENSQMFQGRPCKDMYLNEYFPHGITNGASWYNVPGGMQDWNYLQTNCFEVTIELGCVKYPFENELPKYWEQNRRSLIQFMKQVHQGVKGFVLDATDGRGILNATLSVAEINHPVTTYKAGDYWRLLVPGTYKITASARGYNPVTKNVTVRSEGAVQVNFTLVRSSADANNESKKGRGHSTSTDDTSDPTSKEFEALIKHLSAENGLEGFMLSSSSDLALYRYHSYKDLSEFLRGLVMNYPHITNLTTLGQSVEYRHIWSLEISNKPNISEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCLNYKRNPVVTQLVDRTRIVIVPSLNPDGRERAQEKDCTSKTGHTNAHGKDLDTDFTSNASQPETKAIIENLIQKQDFSLSIALDGGSVLVTYPYDKPVQTVENKETLKHLASLYANNHPSMHMGQPSCPNNSDENIPGGVMRGAEWHSHLGSMKDYSVTYGHCPEITVYTSCCYFPSAAQLPALWAENKKSLLSMLVEVHKGVHGLVKDKAGKPISKAVIVLNEGIKVYTKEGGYFHVLLAPGVHNINAIADGYQQQHTQVFVHHDAASSVVIVFDTDNRIFGLPRELVVTVSGATMSALILTACIIWCICSIKSNRHKDGFHRLRQHHDEYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH
Enzyme Length 1377
Uniprot Accession Number O89001
Absorption
Active Site ACT_SITE 761; /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;
DNA Binding
EC Number 3.4.17.22
Enzyme Function
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Compositional bias (2); Glycosylation (15); Lipidation (3); Metal binding (6); Modified residue (6); Motif (1); Region (7); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1)
Keywords Carboxypeptidase;Cell membrane;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Palmitate;Phosphoprotein;Protease;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane protein {ECO:0000255}.
Modified Residue MOD_RES 264; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 269; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1355; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1358; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1365; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 1367; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
Post Translational Modification
Signal Peptide SIGNAL 1..37; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11891854; 12466851; 12643288; 14681479; 15870393; 15918796; 16615898; 17177860; 20925061; 21267068; 24515436; 9260933; 9628828;
Motif MOTIF 161..163; /note=Cell attachment site; /evidence=ECO:0000255
Gene Encoded By
Mass 152,406
Kinetics
Metal Binding METAL 138; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 141; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 256; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P19222; METAL 563; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 566; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00730; METAL 670; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P00730
Rhea ID
Cross Reference Brenda 3.4.17.22;