| IED ID | IndEnz0002018933 |
| Enzyme Type ID | protease018933 |
| Protein Name |
Carboxypeptidase D EC 3.4.17.22 Metallocarboxypeptidase D gp180 p170 |
| Gene Name | CPD |
| Organism | Anas platyrhynchos (Mallard) (Anas boschas) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Anseriformes (ducks geese and swans) Anatidae (waterfowl) Anatinae Anas (ducks) Anas platyrhynchos (Mallard) (Anas boschas) |
| Enzyme Sequence | MAGAARGLLWAALSLCLLPEPLRAAHIKKAEAAAAGGGGGVGGELRYLHAAELGQALRDLVAEAPPGLARLFSIGRSVEGRPLWVLRLTAGLPELPEARQDGEKKKKEEEEEEEEEEGEEGGGGALPGRPQVKLVGNMHGDEPLARPLLLRLAQELVRGWAGGDERLGRLLNTTDLYLLPSLNPDGFERAREGDCGGGGGGGGEGGGEPGGRENSRGRDLNRSFPDQFGSAQPDLEPVPEVRALIAWMRRNKFLLSGNLHGGSVVASYPYDDSPTHRPTGVYSKSADDEVFKYLAKAYASHHPIMRTGKPNCPGEEGETFQDGITNGAQWYDVEGGMQDYNYVWANCFEITLELSCCKYPPTSELQQEWENNRESLLTFIEKVHIGVKGFVRDAITGAGLENATIVVAGIAHNITAGKFGDYHRLLVPGTYNVTAVVMGYAPVTKENIEVKEADATVVDFSLQPTVVAPDPNLTQFTATPAPPSTLTPSVAQVEPPATTSLHQAVQPVDFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEISDNPGIHEAGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVQSTRIHIMPSMNPDGYEKSQEGDRGGTVGRNNSNNYDLNRNFPDQFFQVTDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGIAIYSKSPDDAVFQQLALSYSKENKKMYQGSPCKDLYPTEYFPHGITNGAQWYNVPGGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRSLLQFIKQVHRGIWGFVLDATDGRGILNATISVADINHPVTTYKDGDYWRLLVQGTYKVTASARGYDPVTKTVEVDSKGGVQVNFTLSRTDAKVEEGKVPVLNTPDTSDPNEKEFETLIKDLSAENGLERLLLASSGKVSPYRYRPYKDLSEFLRGLYLNYPHITNLTSLGQSVEFRQIWSLEISNKPNHSEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCMNYKKNSAVTKLIDRTRIVIVPSLNPDGREIAQERGCTSKLGHANAHGRDLDTDFTSNYSWYSGTREPETKAIIENLILKQDFSLSVALDGGSLLVTYPFDKPAQTVENKETLKHLASVYANNHPLMHLGQPGCPNKSDENIPGGVIRGSEWHSHLGSMKDFSVTFGHCPEITVYTSCCYFPSAGQLPGLWADHRKSLLSMLVEVHKGVHGFVQDKSGKAISKATIVLNEGLRVYTKEGGYFHVLLAPGLHNINAIADGYQQKHMKVLVRHDAPSSVFIVFDMENRIFGLPRELVVTVAGASMSALVLTACIIWCVCSIKSNRHKDGFPTLRQHHDDYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH |
| Enzyme Length | 1389 |
| Uniprot Accession Number | Q90240 |
| Absorption | |
| Active Site | ACT_SITE 353; /note=Proton donor/acceptor 1; /evidence=ECO:0000305|PubMed:10506132; ACT_SITE 771; /note=Proton donor/acceptor 2; /evidence=ECO:0000305|PubMed:10506132 |
| 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:0000269|PubMed:10506132, ECO:0000269|PubMed:9525948}; |
| DNA Binding | |
| EC Number | 3.4.17.22 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Glycosylation (13); Lipidation (3); Metal binding (6); Mutagenesis (2); Region (7); Sequence conflict (12); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Carboxypeptidase;Cell membrane;Direct protein sequencing;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Palmitate;Protease;Repeat;Signal;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8138993}; Single-pass type I membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7797483}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 153,506 |
| Kinetics | |
| Metal Binding | METAL 139; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:O75976; METAL 142; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:O75976; METAL 260; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:O75976; METAL 573; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P83852; METAL 576; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P83852; METAL 680; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P83852 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.17.22; |