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Entry version 105 (07 Apr 2021)
Sequence version 1 (01 Nov 1996)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi139Zinc 1; catalyticBy similarity1
Metal bindingi142Zinc 1; catalyticBy similarity1
Metal bindingi260Zinc 1; catalyticBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei353Proton donor/acceptor 11 Publication1
Metal bindingi573Zinc 2; catalyticBy similarity1
Metal bindingi576Zinc 2; catalyticBy similarity1
Metal bindingi680Zinc 2; catalyticBy similarity1
Active sitei771Proton donor/acceptor 21 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCarboxypeptidase, Hydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.17.22, 334

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q90240

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M14.950

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Carboxypeptidase D (EC:3.4.17.22)
Alternative name(s):
Metallocarboxypeptidase D
gp180
p170
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CPD
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAnas platyrhynchos (Mallard) (Anas boschas)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8839 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeAnseriformesAnatidaeAnatinaeAnas

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini26 – 1308ExtracellularSequence analysisAdd BLAST1283
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1309 – 1329HelicalSequence analysisAdd BLAST21
Topological domaini1330 – 1389CytoplasmicSequence analysisAdd BLAST60

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi353E → Q: Loss of catalytic activity in carboxypeptidase domain 1. Total loss of catalytic activity; when associated with Q-771. 1 Publication1
Mutagenesisi771E → Q: Loss of catalytic activity in carboxypeptidase domain 2. Total loss of catalytic activity; when associated with Q-535. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000440426 – 1389Carboxypeptidase DSequence analysisAdd BLAST1364

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi172N-linked (GlcNAc...) asparagineBy similarity1
Glycosylationi221N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi402N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi413N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi432N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi472N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi635N-linked (GlcNAc...) asparagineBy similarity1
Glycosylationi820N-linked (GlcNAc...) asparagineBy similarity1
Glycosylationi876N-linked (GlcNAc...) asparagineBy similarity1
Glycosylationi958N-linked (GlcNAc...) asparagineBy similarity1
Glycosylationi981N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1073N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1151N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi1326S-palmitoyl cysteineBy similarity1
Lipidationi1330S-palmitoyl cysteineBy similarity1
Lipidationi1332S-palmitoyl cysteineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate

PTM databases

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q90240

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

3 Publications

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q90240

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni26 – 502Carboxypeptidase 1Add BLAST477
Regioni503 – 902Carboxypeptidase 2Add BLAST400
Regioni903 – 1308Carboxypeptidase-likeAdd BLAST406

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi118 – 211Gly-richAdd BLAST94

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M14 family.Sequence analysis

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...
OMAi
ILEKFAH

Database of Orthologous Groups

More...
OrthoDBi
101221at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03863, M14_CPD_II, 1 hit
cd06245, M14_CPD_III, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

The PANTHER Classification System

More...
PANTHERi
PTHR11532:SF73, PTHR11532:SF73, 4 hits

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00246, Peptidase_M14, 3 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00765, CRBOXYPTASEA

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00631, Zn_pept, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49464, SSF49464, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00132, CARBOXYPEPT_ZN_1, 2 hits
PS00133, CARBOXYPEPT_ZN_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iAD2604E157B058E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti40G → GG (PubMed:10482623).Curated1
Sequence conflicti108Missing in AAB96915 (PubMed:10482623).Curated1
Sequence conflicti196 – 197Missing in AAB96915 (PubMed:10482623).Curated2
Sequence conflicti390F → Y in AAB96915 (PubMed:10482623).Curated1
Sequence conflicti453A → G in AAB96915 (PubMed:10482623).Curated1
Sequence conflicti483P → L in AAB96915 (PubMed:10482623).Curated1
Sequence conflicti493V → A in AAB96915 (PubMed:10482623).Curated1
Sequence conflicti503Q → R in AAB96915 (PubMed:10482623).Curated1
Sequence conflicti558I → V in AAB96915 (PubMed:10482623).Curated1
Sequence conflicti558I → V AA sequence (PubMed:7797483).Curated1
Sequence conflicti1076W → R in AAB96915 (PubMed:10482623).Curated1
Sequence conflicti1126E → D in AAB96915 (PubMed:10482623).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U25126 mRNA Translation: AAA78903.1
AF039749 mRNA Translation: AAB96915.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I50090

NCBI Reference Sequences

More...
RefSeqi
NP_001297311.1, NM_001310382.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
101802114

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
apla:101802114

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

SMRiQ90240
ModBaseiSearch...

Protein family/group databases

MEROPSiM14.950

PTM databases

SwissPalmiQ90240

Genome annotation databases

GeneIDi101802114
KEGGiapla:101802114

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1362

Phylogenomic databases

OMAiILEKFAH
OrthoDBi101221at2759

Enzyme and pathway databases

BRENDAi3.4.17.22, 334
SABIO-RKiQ90240

Family and domain databases

CDDicd03863, M14_CPD_II, 1 hit
cd06245, M14_CPD_III, 1 hit
InterProiView protein in InterPro
IPR008969, CarboxyPept-like_regulatory
IPR034224, M14_CPD_II
IPR033848, M14_CPD_III
IPR015567, Pept_M14B_carboxypept_D2
IPR000834, Peptidase_M14
PANTHERiPTHR11532:SF73, PTHR11532:SF73, 4 hits
PfamiView protein in Pfam
PF00246, Peptidase_M14, 3 hits
PRINTSiPR00765, CRBOXYPTASEA
SMARTiView protein in SMART
SM00631, Zn_pept, 3 hits
SUPFAMiSSF49464, SSF49464, 3 hits
PROSITEiView protein in PROSITE
PS00132, CARBOXYPEPT_ZN_1, 2 hits
PS00133, CARBOXYPEPT_ZN_2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCBPD_ANAPL
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q90240
Secondary accession number(s): O57512
, Q9PXB2, Q9PXB3, Q9PXB4, Q9PXB5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated 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.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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