Protein detail

CBPD

Carboxypeptidase D (EC 3.4.17.22) (Metallocarboxypeptidase D) (gp180)

Entry name
CBPD
UniProt ID
EVMP score
0.47
Frequency
16
Transmembrane count
1
Protein classification
EnzymesPredicted intracellular proteinsPredicted membrane proteins
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Carboxypeptidase D (EC 3.4.17.22) (Metallocarboxypeptidase D) (gp180)
Protein Class
EnzymesPredicted intracellular proteinsPredicted membrane proteins
Protein Function
  • Peptidases:Metallopeptidases
  • Enzymes
  • Predicted intracellular proteins
  • ENZYME proteins:Hydrolases
Transmembrane
1300..1320; Helical
Transmembrane Count
1
Entrez Gene Symbol
Gene Synonym
GP180
Gene Description
Carboxypeptidase D
Chromosome
17
Position
30378927-30469989
Frequency
16
EVMP Score
0.47
Fluorescence & Localization
Tissue SpecificbrainCell SpecificCone photoreceptor cellsBlood Cell Specificbasophil
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

29 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
transmembranetransmembraneUniProt_topologyNoNoNoYesNo
transmembranetransmembraneUniProt_keywordNoNoNoYesNo
transmembrane_predictedtransmembraneOmniPathNoNoNoYesNo
transmembranetransmembraneTopDBNoNoNoYesNo
transmembranetransmembraneLOCATENoNoNoYesNo
transmembranetransmembraneRamilowski_locationNoNoNoYesNo
transmembranetransmembraneOmniPathNoNoNoYesNo
plasma_membraneplasma_membraneUniProt_locationNoNoNoYesNo
plasma_membraneplasma_membraneOmniPathNoNoNoYesNo
plasma_membrane_transmembraneplasma_membrane_transmembraneMembranomeNoNoNoYesNo
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Regulatory Interaction Network

0 records.

Protein Complex Composition

6 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
CPDO759762PDBPDB:5aq0
GPCPD1SLC35D3Q5M8T2Q9NPB80:0hu.MAP2
SCCPDHUSP13Q8NBX0Q929950:0hu.MAP
CRIPTSCCPDHTMEM160USP13Q8NBX0Q92995Q9NX00Q9P0210:0:0:0hu.MAP2
CRIPTSCCPDHUSP13Q8NBX0Q92995Q9P0210:0:0hu.MAP2
GPCPD1Q9NPB86PDBPDB:2z0b

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyImmunoaffinity CaptureMass spectrometry23811336838207106
Sequence, Structure & Domains

Sequences

Length
1,380
Mass
152,931
Sequence
MASGRDERPPWRLGRLLLLMCLLLLGSSARAAHIKKAEATTTTTSAGAEAAEGQFDRYYHEEELESALREAAAAGLPGLARLFSIGRSVEGRPLWVLRLTAGLGSLIPEGDAGPDAAGPDAAGPLLPGRPQVKLVGNMHGDETVSRQVLIYLARELAAGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGFGDGGPSGASGRDNSRGRDLNRSFPDQFSTGEPPALDEVPEVRALIEWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKATGIYSKTSDDEVFKYLAKAYASNHPIMKTGEPHCPGDEDETFKDGITNGAHWYDVEGGMQDYNYVWANCFEITLELSCCKYPPASQLRQEWENNRESLITLIEKVHIGVKGFVKDSITGSGLENATISVAGINHNITTGRFGDFYRLLVPGTYNLTVVLTGYMPLTVTNVVVKEGPATEVDFSLRPTVTSVIPDTTEAVSTASTVAIPNILSGTSSSYQPIQPKDFHHHHFPDMEIFLRRFANEYPNITRLYSLGKSVESRELYVMEISDNPGVHEPGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTDLVHNTRIHLMPSMNPDGYEKSQEGDSISVIGRNNSNNFDLNRNFPDQFVQITDPTQPETIAVMSWMKSYPFVLSANLHGGSLVVNYPFDDDEQGLATYSKSPDDAVFQQIALSYSKENSQMFQGRPCKNMYPNEYFPHGITNGASWYNVPGGMQDWNYLQTNCFEVTIELGCVKYPLEKELPNFWEQNRRSLIQFMKQVHQGVRGFVLDATDGRGILNATISVAEINHPVTTYKTGDYWRLLVPGTYKITASARGYNPVTKNVTVKSEGAIQVNFTLVRSSTDSNNESKKGKGASSSTNDASDPTTKEFETLIKDLSAENGLESLMLRSSSNLALALYRYHSYKDLSEFLRGLVMNYPHITNLTNLGQSTEYRHIWSLEISNKPNVSEPEEPKIRFVAGIHGNAPVGTELLLALAEFLCLNYKKNPAVTQLVDRTRIVIVPSLNPDGRERAQEKDCTSKIGQTNARGKDLDTDFTNNASQPETKAIIENLIQKQDFSLSVALDGGSMLVTYPYDKPVQTVENKETLKHLASLYANNHPSMHMGQPSCPNKSDENIPGGVMRGAEWHSHLGSMKDYSVTYGHCPEITVYTSCCYFPSAARLPSLWADNKRSLLSMLVEVHKGVHGFVKDKTGKPISKAVIVLNEGIKVQTKEGGYFHVLLAPGVHNIIAIADGYQQQHSQVFVHHDAASSVVIVFDTDNRIFGLPRELVVTVSGATMSALILTACIIWCICSIKSNRHKDGFHRLRQHHDEYEDEIRMMSTGSKKSLLSHEFQDETDTEEETLYSSKH
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O75976-1; Sequence=Displayed; Name=2; IsoId=O75976-2; Sequence=VSP_045833, VSP_045834
Alternative Sequence
1..2; MA -> MR (in isoform 2); 3..249; Missing (in isoform 2)

3D Structural Models

Turn
391..393
Beta Strand
383..390; 401..404; 417..422; 425..433; 440..447; 449..451; 457..459
3D Structure
Electron microscopy (2); X-ray crystallography (1)

Domain & Motif Annotations

Compositional Bias
195..204; Gly residues; 887..897; Polar residues
Motif
162..164; Cell attachment site
Domain (CC)
There are 3 carboxypeptidase-like domains. Only the first two domains seem to have kept a catalytic activity.
Domain (FT)
57..380; Peptidase M14 1; 502..792; Peptidase M14 2; 932..1211; Peptidase M14 3
Region
190..232; Disordered; 874..899; Disordered; 1359..1380; Disordered
Protein Families
Peptidase M14 family
Sequence Similarities
Belongs to the peptidase M14 family.
Clinical Relevance
Antibody
Interaction Protein
ENSG00000127022
Interaction Count
1
Interaction Dataset
biogrid_opencell