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Protein

Carboxypeptidase D

Gene

CPD

Organism
Anas platyrhynchos (Mallard) (Anas boschas)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Releases C-terminal Arg and Lys from polypeptides.2 Publications

Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Zinc 1; catalyticBy similarity
Metal bindingi142 – 1421Zinc 1; catalyticBy similarity
Metal bindingi260 – 2601Zinc 1; catalyticBy similarity
Active sitei353 – 3531Proton donor/acceptor 11 Publication
Metal bindingi573 – 5731Zinc 2; catalyticBy similarity
Metal bindingi576 – 5761Zinc 2; catalyticBy similarity
Metal bindingi680 – 6801Zinc 2; catalyticBy similarity
Active sitei771 – 7711Proton donor/acceptor 21 Publication

GO - Molecular functioni

  • metallocarboxypeptidase activity Source: UniProtKB
  • serine-type carboxypeptidase activity Source: InterPro
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.22. 334.
SABIO-RKQ90240.

Protein family/group databases

MEROPSiM14.950.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase D (EC:3.4.17.22)
Alternative name(s):
Metallocarboxypeptidase D
gp180
p170
Gene namesi
Name:CPD
OrganismiAnas platyrhynchos (Mallard) (Anas boschas)
Taxonomic identifieri8839 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeAnas
Proteomesi
  • UP000016666 Componenti: Unassembled WGS sequence

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 13081283ExtracellularSequence analysisAdd
BLAST
Transmembranei1309 – 132921HelicalSequence analysisAdd
BLAST
Topological domaini1330 – 138960CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi353 – 3531E → Q: Loss of catalytic activity in carboxypeptidase domain 1. Total loss of catalytic activity; when associated with Q-771. 1 Publication
Mutagenesisi771 – 7711E → Q: Loss of catalytic activity in carboxypeptidase domain 2. Total loss of catalytic activity; when associated with Q-535. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 13891364Carboxypeptidase DSequence analysisPRO_0000004404Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi172 – 1721N-linked (GlcNAc...)By similarity
Glycosylationi221 – 2211N-linked (GlcNAc...)Sequence analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence analysis
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence analysis
Glycosylationi432 – 4321N-linked (GlcNAc...)Sequence analysis
Glycosylationi472 – 4721N-linked (GlcNAc...)Sequence analysis
Glycosylationi635 – 6351N-linked (GlcNAc...)By similarity
Glycosylationi820 – 8201N-linked (GlcNAc...)By similarity
Glycosylationi876 – 8761N-linked (GlcNAc...)By similarity
Glycosylationi958 – 9581N-linked (GlcNAc...)By similarity
Glycosylationi981 – 9811N-linked (GlcNAc...)Sequence analysis
Glycosylationi1073 – 10731N-linked (GlcNAc...)Sequence analysis
Glycosylationi1151 – 11511N-linked (GlcNAc...)Sequence analysis
Lipidationi1326 – 13261S-palmitoyl cysteineBy similarity
Lipidationi1330 – 13301S-palmitoyl cysteineBy similarity
Lipidationi1332 – 13321S-palmitoyl cysteineBy similarity

Post-translational modificationi

The N-terminus is blocked.1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiQ90240.

PTM databases

SwissPalmiQ90240.

Expressioni

Tissue specificityi

Expressed in liver, lung, kidney, heart, stomach, pancreas, spleen, gall bladder and intestine, but not in skeletal muscle.2 Publications

Interactioni

Subunit structurei

Binds to pre-S, hepatitis B virus large envelope protein, via the carboxypeptidase-like domain.3 Publications

Structurei

3D structure databases

ProteinModelPortaliQ90240.
SMRiQ90240. Positions 503-882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 502477Carboxypeptidase 1Add
BLAST
Regioni503 – 902400Carboxypeptidase 2Add
BLAST
Regioni903 – 1308406Carboxypeptidase-likeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi118 – 21194Gly-richAdd
BLAST

Domaini

There are 3 carboxypeptidase domains. Only the first two domains have any catalytic activity. The first domain preferentially cleaves C-terminal Arg residues, whereas the second preferentially cleaves C-terminal Lys residues. The third domain binds to pre-S, hepatitis B virus large envelope protein.2 Publications

Sequence similaritiesi

Belongs to the peptidase M14 family.Sequence analysis

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG006932.
KOiK07752.

Family and domain databases

Gene3Di2.60.40.1120. 3 hits.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF50. PTHR11532:SF50. 4 hits.
PfamiPF00246. Peptidase_M14. 3 hits.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 3 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 3 hits.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 2 hits.
PS00133. CARBOXYPEPT_ZN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q90240-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGAARGLLW AALSLCLLPE PLRAAHIKKA EAAAAGGGGG VGGELRYLHA
60 70 80 90 100
AELGQALRDL VAEAPPGLAR LFSIGRSVEG RPLWVLRLTA GLPELPEARQ
110 120 130 140 150
DGEKKKKEEE EEEEEEEGEE GGGGALPGRP QVKLVGNMHG DEPLARPLLL
160 170 180 190 200
RLAQELVRGW AGGDERLGRL LNTTDLYLLP SLNPDGFERA REGDCGGGGG
210 220 230 240 250
GGGEGGGEPG GRENSRGRDL NRSFPDQFGS AQPDLEPVPE VRALIAWMRR
260 270 280 290 300
NKFLLSGNLH GGSVVASYPY DDSPTHRPTG VYSKSADDEV FKYLAKAYAS
310 320 330 340 350
HHPIMRTGKP NCPGEEGETF QDGITNGAQW YDVEGGMQDY NYVWANCFEI
360 370 380 390 400
TLELSCCKYP PTSELQQEWE NNRESLLTFI EKVHIGVKGF VRDAITGAGL
410 420 430 440 450
ENATIVVAGI AHNITAGKFG DYHRLLVPGT YNVTAVVMGY APVTKENIEV
460 470 480 490 500
KEADATVVDF SLQPTVVAPD PNLTQFTATP APPSTLTPSV AQVEPPATTS
510 520 530 540 550
LHQAVQPVDF RHHHFSDMEI FLRRYANEYP SITRLYSVGK SVELRELYVM
560 570 580 590 600
EISDNPGIHE AGEPEFKYIG NMHGNEVVGR ELLLNLIEYL CKNFGTDPEV
610 620 630 640 650
TDLVQSTRIH IMPSMNPDGY EKSQEGDRGG TVGRNNSNNY DLNRNFPDQF
660 670 680 690 700
FQVTDPPQPE TLAVMSWLKT YPFVLSANLH GGSLVVNYPF DDDEQGIAIY
710 720 730 740 750
SKSPDDAVFQ QLALSYSKEN KKMYQGSPCK DLYPTEYFPH GITNGAQWYN
760 770 780 790 800
VPGGMQDWNY LNTNCFEVTI ELGCVKYPKA EELPKYWEQN RRSLLQFIKQ
810 820 830 840 850
VHRGIWGFVL DATDGRGILN ATISVADINH PVTTYKDGDY WRLLVQGTYK
860 870 880 890 900
VTASARGYDP VTKTVEVDSK GGVQVNFTLS RTDAKVEEGK VPVLNTPDTS
910 920 930 940 950
DPNEKEFETL IKDLSAENGL ERLLLASSGK VSPYRYRPYK DLSEFLRGLY
960 970 980 990 1000
LNYPHITNLT SLGQSVEFRQ IWSLEISNKP NHSEPEEPKI RFVAGIHGNA
1010 1020 1030 1040 1050
PVGTELLLAL AEFLCMNYKK NSAVTKLIDR TRIVIVPSLN PDGREIAQER
1060 1070 1080 1090 1100
GCTSKLGHAN AHGRDLDTDF TSNYSWYSGT REPETKAIIE NLILKQDFSL
1110 1120 1130 1140 1150
SVALDGGSLL VTYPFDKPAQ TVENKETLKH LASVYANNHP LMHLGQPGCP
1160 1170 1180 1190 1200
NKSDENIPGG VIRGSEWHSH LGSMKDFSVT FGHCPEITVY TSCCYFPSAG
1210 1220 1230 1240 1250
QLPGLWADHR KSLLSMLVEV HKGVHGFVQD KSGKAISKAT IVLNEGLRVY
1260 1270 1280 1290 1300
TKEGGYFHVL LAPGLHNINA IADGYQQKHM KVLVRHDAPS SVFIVFDMEN
1310 1320 1330 1340 1350
RIFGLPRELV VTVAGASMSA LVLTACIIWC VCSIKSNRHK DGFPTLRQHH
1360 1370 1380
DDYEDEIRMM STGSKKSLLS HEFQDETDTE EETLYSSKH
Length:1,389
Mass (Da):153,506
Last modified:November 1, 1996 - v1
Checksum:iAD2604E157B058E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401G → GG (PubMed:10482623).Curated
Sequence conflicti108 – 1081Missing in AAB96915 (PubMed:10482623).Curated
Sequence conflicti196 – 1972Missing in AAB96915 (PubMed:10482623).Curated
Sequence conflicti390 – 3901F → Y in AAB96915 (PubMed:10482623).Curated
Sequence conflicti453 – 4531A → G in AAB96915 (PubMed:10482623).Curated
Sequence conflicti483 – 4831P → L in AAB96915 (PubMed:10482623).Curated
Sequence conflicti493 – 4931V → A in AAB96915 (PubMed:10482623).Curated
Sequence conflicti503 – 5031Q → R in AAB96915 (PubMed:10482623).Curated
Sequence conflicti558 – 5581I → V in AAB96915 (PubMed:10482623).Curated
Sequence conflicti558 – 5581I → V AA sequence (PubMed:7797483).Curated
Sequence conflicti1076 – 10761W → R in AAB96915 (PubMed:10482623).Curated
Sequence conflicti1126 – 11261E → D in AAB96915 (PubMed:10482623).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25126 mRNA. Translation: AAA78903.1.
AF039749 mRNA. Translation: AAB96915.1.
PIRiI50090.
RefSeqiNP_001297311.1. NM_001310382.1.

Genome annotation databases

GeneIDi101802114.
KEGGiapla:101802114.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25126 mRNA. Translation: AAA78903.1.
AF039749 mRNA. Translation: AAB96915.1.
PIRiI50090.
RefSeqiNP_001297311.1. NM_001310382.1.

3D structure databases

ProteinModelPortaliQ90240.
SMRiQ90240. Positions 503-882.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM14.950.

PTM databases

SwissPalmiQ90240.

Proteomic databases

PRIDEiQ90240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101802114.
KEGGiapla:101802114.

Organism-specific databases

CTDi1362.

Phylogenomic databases

HOVERGENiHBG006932.
KOiK07752.

Enzyme and pathway databases

BRENDAi3.4.17.22. 334.
SABIO-RKQ90240.

Family and domain databases

Gene3Di2.60.40.1120. 3 hits.
InterProiIPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR015567. Pept_M14B_carboxypept_D2.
IPR000834. Peptidase_M14.
[Graphical view]
PANTHERiPTHR11532:SF50. PTHR11532:SF50. 4 hits.
PfamiPF00246. Peptidase_M14. 3 hits.
[Graphical view]
PRINTSiPR00765. CRBOXYPTASEA.
SMARTiSM00631. Zn_pept. 3 hits.
[Graphical view]
SUPFAMiSSF49464. SSF49464. 3 hits.
PROSITEiPS00132. CARBOXYPEPT_ZN_1. 2 hits.
PS00133. CARBOXYPEPT_ZN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBPD_ANAPL
AccessioniPrimary (citable) accession number: Q90240
Secondary accession number(s): O57512
, Q9PXB2, Q9PXB3, Q9PXB4, Q9PXB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 86 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.