UniProtKB - Q90240 (CBPD_ANAPL)
Protein
Carboxypeptidase D
Gene
CPD
Organism
Anas platyrhynchos (Mallard) (Anas boschas)
Status
Functioni
Catalytic activityi
- Releases C-terminal Arg and Lys from polypeptides.2 Publications EC:3.4.17.22
Cofactori
Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 139 | Zinc 1; catalyticBy similarity | 1 | |
Metal bindingi | 142 | Zinc 1; catalyticBy similarity | 1 | |
Metal bindingi | 260 | Zinc 1; catalyticBy similarity | 1 | |
Active sitei | 353 | Proton donor/acceptor 11 Publication | 1 | |
Metal bindingi | 573 | Zinc 2; catalyticBy similarity | 1 | |
Metal bindingi | 576 | Zinc 2; catalyticBy similarity | 1 | |
Metal bindingi | 680 | Zinc 2; catalyticBy similarity | 1 | |
Active sitei | 771 | Proton donor/acceptor 21 Publication | 1 |
GO - Molecular functioni
- metallocarboxypeptidase activity Source: UniProtKB
- zinc ion binding Source: UniProtKB
GO - Biological processi
- peptide metabolic process Source: InterPro
- proteolysis Source: UniProtKB
Keywordsi
Molecular function | Carboxypeptidase, Hydrolase, Metalloprotease, Protease |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.4.17.22, 334 |
SABIO-RKi | Q90240 |
Protein family/group databases
MEROPSi | M14.950 |
Names & Taxonomyi
Protein namesi | Recommended name: Carboxypeptidase D (EC:3.4.17.22)Alternative name(s): Metallocarboxypeptidase D gp180 p170 |
Gene namesi | Name:CPD |
Organismi | Anas platyrhynchos (Mallard) (Anas boschas) |
Taxonomic identifieri | 8839 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Anseriformes › Anatidae › Anatinae › Anas |
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication; Single-pass type I membrane protein Sequence analysis
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- integral component of membrane Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 26 – 1308 | ExtracellularSequence analysisAdd BLAST | 1283 | |
Transmembranei | 1309 – 1329 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1330 – 1389 | CytoplasmicSequence analysisAdd BLAST | 60 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 353 | E → Q: Loss of catalytic activity in carboxypeptidase domain 1. Total loss of catalytic activity; when associated with Q-771. 1 Publication | 1 | |
Mutagenesisi | 771 | E → Q: Loss of catalytic activity in carboxypeptidase domain 2. Total loss of catalytic activity; when associated with Q-535. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 25 | Sequence analysisAdd BLAST | 25 | |
ChainiPRO_0000004404 | 26 – 1389 | Carboxypeptidase DSequence analysisAdd BLAST | 1364 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 172 | N-linked (GlcNAc...) asparagineBy similarity | 1 | |
Glycosylationi | 221 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 402 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 413 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 432 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 472 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 635 | N-linked (GlcNAc...) asparagineBy similarity | 1 | |
Glycosylationi | 820 | N-linked (GlcNAc...) asparagineBy similarity | 1 | |
Glycosylationi | 876 | N-linked (GlcNAc...) asparagineBy similarity | 1 | |
Glycosylationi | 958 | N-linked (GlcNAc...) asparagineBy similarity | 1 | |
Glycosylationi | 981 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1073 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1151 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Lipidationi | 1326 | S-palmitoyl cysteineBy similarity | 1 | |
Lipidationi | 1330 | S-palmitoyl cysteineBy similarity | 1 | |
Lipidationi | 1332 | S-palmitoyl cysteineBy similarity | 1 |
Post-translational modificationi
The N-terminus is blocked.1 Publication
Keywords - PTMi
Glycoprotein, Lipoprotein, PalmitatePTM databases
SwissPalmi | Q90240 |
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 PublicationsFamily & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 26 – 502 | Carboxypeptidase 1Add BLAST | 477 | |
Regioni | 503 – 902 | Carboxypeptidase 2Add BLAST | 400 | |
Regioni | 903 – 1308 | Carboxypeptidase-likeAdd BLAST | 406 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 118 – 211 | Gly-richAdd BLAST | 94 |
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 helixPhylogenomic databases
OMAi | ILEKFAH |
OrthoDBi | 101221at2759 |
Family and domain databases
CDDi | cd03863, M14_CPD_II, 1 hit cd06245, M14_CPD_III, 1 hit |
InterProi | View protein in InterPro IPR008969, CarboxyPept-like_regulatory IPR034224, M14_CPD_II IPR033848, M14_CPD_III IPR015567, Pept_M14B_carboxypept_D2 IPR000834, Peptidase_M14 |
PANTHERi | PTHR11532:SF73, PTHR11532:SF73, 4 hits |
Pfami | View protein in Pfam PF00246, Peptidase_M14, 3 hits |
PRINTSi | PR00765, CRBOXYPTASEA |
SMARTi | View protein in SMART SM00631, Zn_pept, 3 hits |
SUPFAMi | SSF49464, SSF49464, 3 hits |
PROSITEi | View protein in PROSITE PS00132, CARBOXYPEPT_ZN_1, 2 hits PS00133, CARBOXYPEPT_ZN_2, 2 hits |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q90240-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 40 | G → GG (PubMed:10482623).Curated | 1 | |
Sequence conflicti | 108 | Missing in AAB96915 (PubMed:10482623).Curated | 1 | |
Sequence conflicti | 196 – 197 | Missing in AAB96915 (PubMed:10482623).Curated | 2 | |
Sequence conflicti | 390 | F → Y in AAB96915 (PubMed:10482623).Curated | 1 | |
Sequence conflicti | 453 | A → G in AAB96915 (PubMed:10482623).Curated | 1 | |
Sequence conflicti | 483 | P → L in AAB96915 (PubMed:10482623).Curated | 1 | |
Sequence conflicti | 493 | V → A in AAB96915 (PubMed:10482623).Curated | 1 | |
Sequence conflicti | 503 | Q → R in AAB96915 (PubMed:10482623).Curated | 1 | |
Sequence conflicti | 558 | I → V in AAB96915 (PubMed:10482623).Curated | 1 | |
Sequence conflicti | 558 | I → V AA sequence (PubMed:7797483).Curated | 1 | |
Sequence conflicti | 1076 | W → R in AAB96915 (PubMed:10482623).Curated | 1 | |
Sequence conflicti | 1126 | E → D in AAB96915 (PubMed:10482623).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U25126 mRNA Translation: AAA78903.1 AF039749 mRNA Translation: AAB96915.1 |
PIRi | I50090 |
RefSeqi | NP_001297311.1, NM_001310382.1 |
Genome annotation databases
GeneIDi | 101802114 |
KEGGi | apla:101802114 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U25126 mRNA Translation: AAA78903.1 AF039749 mRNA Translation: AAB96915.1 |
PIRi | I50090 |
RefSeqi | NP_001297311.1, NM_001310382.1 |
3D structure databases
SMRi | Q90240 |
ModBasei | Search... |
Protein family/group databases
MEROPSi | M14.950 |
PTM databases
SwissPalmi | Q90240 |
Genome annotation databases
GeneIDi | 101802114 |
KEGGi | apla:101802114 |
Organism-specific databases
CTDi | 1362 |
Phylogenomic databases
OMAi | ILEKFAH |
OrthoDBi | 101221at2759 |
Enzyme and pathway databases
BRENDAi | 3.4.17.22, 334 |
SABIO-RKi | Q90240 |
Family and domain databases
CDDi | cd03863, M14_CPD_II, 1 hit cd06245, M14_CPD_III, 1 hit |
InterProi | View protein in InterPro IPR008969, CarboxyPept-like_regulatory IPR034224, M14_CPD_II IPR033848, M14_CPD_III IPR015567, Pept_M14B_carboxypept_D2 IPR000834, Peptidase_M14 |
PANTHERi | PTHR11532:SF73, PTHR11532:SF73, 4 hits |
Pfami | View protein in Pfam PF00246, Peptidase_M14, 3 hits |
PRINTSi | PR00765, CRBOXYPTASEA |
SMARTi | View protein in SMART SM00631, Zn_pept, 3 hits |
SUPFAMi | SSF49464, SSF49464, 3 hits |
PROSITEi | View protein in PROSITE PS00132, CARBOXYPEPT_ZN_1, 2 hits PS00133, CARBOXYPEPT_ZN_2, 2 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CBPD_ANAPL | |
Accessioni | Q90240Primary (citable) accession number: Q90240 Secondary accession number(s): O57512 Q9PXB5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 4, 2005 |
Last sequence update: | November 1, 1996 | |
Last modified: | April 7, 2021 | |
This is version 105 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families