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Protein

Carboxypeptidase D

Gene

CPD

Organism
Lophonetta specularioides (Crested duck) (Anas specularioides)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Releases C-terminal Arg and Lys from polypeptides.By similarity

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi71Zinc; catalytic1 Publication1
Metal bindingi74Zinc; catalytic1 Publication1
Metal bindingi178Zinc; catalytic1 Publication1
Active sitei269Proton donor/acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase D (EC:3.4.17.22)
Alternative name(s):
CPD-2
Metallocarboxypeptidase D
Gene namesi
Name:CPD
OrganismiLophonetta specularioides (Crested duck) (Anas specularioides)
Taxonomic identifieri75873 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeLophonetta

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000212786‹1 – ›380Carboxypeptidase DAdd BLAST›380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi133N-linked (GlcNAc...)1 Publication1
Disulfide bondi227 ↔ 2721 Publication
Glycosylationi318N-linked (GlcNAc...)1 Publication1
Glycosylationi374N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP83852.

Structurei

Secondary structure

1380
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 26Combined sources14
Turni28 – 30Combined sources3
Beta strandi31 – 38Combined sources8
Beta strandi44 – 53Combined sources10
Beta strandi63 – 67Combined sources5
Helixi76 – 91Combined sources16
Turni92 – 94Combined sources3
Helixi96 – 104Combined sources9
Beta strandi106 – 111Combined sources6
Helixi115 – 119Combined sources5
Turni130 – 132Combined sources3
Helixi140 – 142Combined sources3
Beta strandi147 – 149Combined sources3
Helixi157 – 168Combined sources12
Beta strandi171 – 178Combined sources8
Beta strandi180 – 187Combined sources8
Beta strandi195 – 197Combined sources3
Helixi204 – 215Combined sources12
Helixi219 – 222Combined sources4
Turni228 – 230Combined sources3
Helixi237 – 239Combined sources3
Beta strandi240 – 242Combined sources3
Helixi243 – 246Combined sources4
Helixi253 – 260Combined sources8
Beta strandi264 – 272Combined sources9
Helixi278 – 280Combined sources3
Helixi281 – 297Combined sources17
Helixi298 – 300Combined sources3
Beta strandi302 – 309Combined sources8
Turni310 – 312Combined sources3
Beta strandi320 – 323Combined sources4
Beta strandi326 – 331Combined sources6
Beta strandi336 – 340Combined sources5
Beta strandi344 – 352Combined sources9
Beta strandi359 – 365Combined sources7
Beta strandi370 – 372Combined sources3
Beta strandi375 – 377Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H8LX-ray2.60A1-380[»]
1QMUX-ray2.70A1-380[»]
ProteinModelPortaliP83852.
SMRiP83852.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83852.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – ›380Carboxypeptidase 2Add BLAST›380

Sequence similaritiesi

Belongs to the peptidase M14 family.Sequence analysis

Phylogenomic databases

HOVERGENiHBG003410.

Family and domain databases

Gene3Di2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF50. PTHR11532:SF50. 1 hit.
PfamiPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P83852-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QAVQPVDFRH HHFSDMEIFL RRYANEYPSI TRLYSVGKSV ELRELYVMEI
60 70 80 90 100
SDNPGIHEAG EPEFKYIGNM HGNEVVGREL LLNLIEYLCK NFGTDPEVTD
110 120 130 140 150
LVQSTRIHIM PSMNPDGYEK SQEGDRGGTV GRNNSNNYDL NRNFPDQFFQ
160 170 180 190 200
VTDPPQPETL AVMSWLKTYP FVLSANLHGG SLVVNYPFDD DEQGIAIYSK
210 220 230 240 250
SPDDAVFQQL ALSYSKENKK MYQGSPCKDL YPTEYFPHGI TNGAQWYNVP
260 270 280 290 300
GGMQDWNYLN TNCFEVTIEL GCVKYPKAEE LPKYWEQNRR SLLQFIKQVH
310 320 330 340 350
RGIWGFVLDA TDGRGILNAT ISVADINHPV TTYKDGDYWR LLVQGTYKVT
360 370 380
ASARGYDPVT KTVEVDSKGG VQVNFTLSRT
Length:380
Mass (Da):43,292
Last modified:April 13, 2004 - v1
Checksum:i536498919536E949
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11 Publication1
Non-terminal residuei3801 Publication1

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H8LX-ray2.60A1-380[»]
1QMUX-ray2.70A1-380[»]
ProteinModelPortaliP83852.
SMRiP83852.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP83852.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003410.

Miscellaneous databases

EvolutionaryTraceiP83852.

Family and domain databases

Gene3Di2.60.40.1120. 1 hit.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF50. PTHR11532:SF50. 1 hit.
PfamiPF00246. Peptidase_M14. 1 hit.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 1 hit.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 1 hit.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 1 hit.
PS00133. CARBOXYPEPT_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBPD_LOPSP
AccessioniPrimary (citable) accession number: P83852
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: April 13, 2004
Last modified: November 2, 2016
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.