Protein detail

CBPD

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

Entry name
CBPD
UniProt ID
EVMP confidence score
0.47
Supporting publications (n)
16
Transmembrane count
1
Protein classification
EnzymesPredicted intracellular proteinsPredicted membrane proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information13
Protein Names
Carboxypeptidase D (EC 3.4.17.22) (Metallocarboxypeptidase D) (gp180)
Protein Class (3)
EnzymesPredicted intracellular proteinsPredicted membrane proteins
Protein Function (4)
  • 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
Supporting publications (n)
16
EVMP confidence score
0.47
Fluorescence & Localization3
Tissue SpecificbrainCell SpecificCone photoreceptor cellsBlood Cell Specificbasophil
Function & Pathway6
Relations & Evidence36

Ligand-Receptor Signaling (29)

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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Protein Complex Composition (6)

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)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyImmunoaffinity CaptureMass spectrometry23811336838207106
Sequence, Structure & Domains15

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 Relevance5
Supporting Publications16
PMIDTitleAbstract
34817906Proteomic dissection of large extracellular vesicle surfaceome unravels interactive surface platform.No abstract available
37786918Rapid and in-depth proteomic profiling of small extracellular vesicles for ultralow samples.No abstract available
38168906Defining the relationship between cellular and extracellular vesicle (EV) content in breast cancer via an integrative multi-omic analysis.No abstract available
38321535Identification of specific markers for human pluripotent stem cell-derived small extracellular vesicles.No abstract available
39409015SILAC-Based Characterization of Plasma-Derived Extracellular Vesicles in Patients Undergoing Partial Hepatectomy.No abstract available
40089067Metabolic Reprogramming Into a Glycolysis Phenotype Induced by Extracellular Vesicles Derived From Prostate Cancer Cells.No abstract available
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