Detail Information for IndEnz0002018933
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;