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UniProtKB - P00727 (AMPL_BOVIN)

Entry version 180 (25 May 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

Cytosol aminopeptidase

Gene

LAP3

Organism
Bos taurus (Bovine)
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

Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides (PubMed:14583094, PubMed:16519517).

The presence of Zn2+ ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme (PubMed:16519517).

For instance, in the presence of Mn2+, it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates (PubMed:16519517).

Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status (PubMed:14583094).

2 Publications

<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+1 Publication, Mn2+1 PublicationNote: Binds two metal ions per subunit. Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals: site 1 is occupied by Zn2+, Mn2+, Mg2+ or Co2+, while the tight binding site 2 can be occupied by only Zn2+ or Co2+ (PubMed:16519517). One Zn2+ ion is tightly bound to site 2 and essential for enzyme activity in vivo, while site 1 can be occupied by different metals to give different enzymatic activities (PubMed:16519517). Mn2+ is required for Cys-Gly hydrolysis activity (PubMed:16519517). A third metal binding site may serve a structural role, possibly stabilizing part of the interface between the N-terminal and the catalytic domain (PubMed:7619821).1 Publication2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Zofenoprilat inhibits Cys-Gly hydrolysis activity.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 3400 min(-1) for Cys-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 11500 min(-1) for Leu-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 8150 min(-1) for Met-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius) (PubMed:14583094). kcat is 6000 min(-1) for Cys-Gly hydrolysis activity (at pH 7.4 and 25 degrees Celsius). kcat is 24000 min(-1) for Leu-Gly hydrolysis activity (at pH 7.4 and 25 degrees Celsius). kcat is 28100 min(-1) for Met-Gly hydrolysis activity (at pH 7.4 and 25 degrees Celsius). kcat is 1000 min(-1) for Ser-Gly hydrolysis activity (at pH 7.4 and 25 degrees Celsius) (PubMed:14583094). kcat is 7100 min(-1) for Cys-Gly hydrolysis activity (at pH 8.3 and 25 degrees Celsius). kcat is 40500 min(-1) for Leu-Gly hydrolysis activity (at pH 8.3 and 25 degrees Celsius). kcat is 59300 min(-1) for Met-Gly hydrolysis activity (at pH 8.3 and 25 degrees Celsius). kcat is 2500 min(-1) for Ser-Gly hydrolysis activity (at pH 8.3 and 25 degrees Celsius) (PubMed:14583094).1 Publication
  1. KM=0.42 mM for Cys-Gly (at pH 6.9 and 25 degrees Celsius)1 Publication
  2. KM=2.3 mM for Leu-Gly (at pH 6.9 and 25 degrees Celsius)1 Publication
  3. KM=2.8 mM for Met-Gly (at pH 6.9 and 25 degrees Celsius)1 Publication
  4. KM=0.57 mM for Cys-Gly (at pH 7.4 and 25 degrees Celsius)1 Publication
  5. KM=2.5 mM for Leu-Gly (at pH 7.4 and 25 degrees Celsius)1 Publication
  6. KM=1.5 mM for Met-Gly (at pH 7.4 and 25 degrees Celsius)1 Publication
  7. KM=5.2 mM for Ser-Gly (at pH 7.4 and 25 degrees Celsius)1 Publication
  8. KM=0.59 mM for Cys-Gly (at pH 8.3 and 25 degrees Celsius)1 Publication
  9. KM=1.5 mM for Leu-Gly (at pH 8.3 and 25 degrees Celsius)1 Publication
  10. KM=1.3 mM for Met-Gly (at pH 8.3 and 25 degrees Celsius)1 Publication
  11. KM=5.0 mM for Ser-Gly (at pH 8.3 and 25 degrees Celsius)1 Publication

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 bindingi202Zinc 3; via carbonyl oxygen; structuralCombined sources1 Publication1
Metal bindingi203Zinc 3; via carbonyl oxygen; structuralCombined sources1 Publication1
Metal bindingi205Zinc 3; via carbonyl oxygen; structuralCombined sources1 Publication1
Metal bindingi282Zinc 2; catalyticCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei282SubstrateCombined sources2 Publications1
Metal bindingi287Magnesium; catalyticCombined sources1 Publication1
Metal bindingi287Zinc 1; catalyticCombined sources3 Publications1
Metal bindingi287Zinc 2; catalyticCombined sources2 Publications1
Binding sitei287SubstrateCombined sources2 Publications1
Binding sitei292SubstrateCombined sources1 Publication1
<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 sitei2941 Publication1
Binding sitei294SubstrateCombined sources2 Publications1
Metal bindingi303Zinc 3; via carbonyl oxygen; structuralCombined sources1 Publication1
Metal bindingi305Zinc 2; catalyticCombined sources2 Publications1
Binding sitei305SubstrateCombined sources1 Publication1
Metal bindingi364Magnesium; catalyticCombined sources1 Publication1
Metal bindingi364Zinc 1; catalyticCombined sources3 Publications1
Binding sitei364SubstrateCombined sources1 Publication1
Metal bindingi366Magnesium; catalyticCombined sources1 Publication1
Metal bindingi366Zinc 1; catalyticCombined sources3 Publications1
Metal bindingi366Zinc 2; catalyticCombined sources3 Publications1
Active sitei3681 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

Complete GO annotation on QuickGO ...

<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 functionAminopeptidase, Dipeptidase, Hydrolase, Protease
LigandCobalt, Magnesium, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.11.1, 908

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P00727

Protein family/group databases

MEROPS protease database

More...MEROPSi		M17.001

<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:
Cytosol aminopeptidaseCurated (EC:3.4.11.11 Publication)
Alternative name(s):
Cysteinylglycine-S-conjugate dipeptidase1 Publication (EC:3.4.13.231 Publication)
Leucine aminopeptidase 3By similarity
Short name:
LAP-3
Leucyl aminopeptidase1 Publication
Short name:
LAP1 Publication
Peptidase SBy similarity
Proline aminopeptidaseBy similarity (EC:3.4.11.5By similarity)
Prolyl aminopeptidaseBy similarity
<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:LAP3By similarity
<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>OrganismiBos taurus (Bovine)
<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 identifieri9913 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSBTAG00000005989

Vertebrate Gene Nomenclature Database

More...VGNCi		VGNC:30786, LAP3

<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

Keywords - Cellular componenti

Cytoplasm

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1671610

DrugCentral

More...DrugCentrali		P00727

<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 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_00001658241 – 519Cytosol aminopeptidaseAdd BLAST519
Isoform 3 (identifier: P00727-3)
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved5 Publications

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei42PhosphoserineBy similarity1
Modified residuei45N6-succinyllysineBy similarity1
Modified residuei54PhosphoserineBy similarity1
Modified residuei61N6-succinyllysineBy similarity1
Modified residuei103N6-succinyllysineBy similarity1
Modified residuei180PhosphoserineBy similarity1
Modified residuei194PhosphoserineBy similarity1
Modified residuei238PhosphoserineBy similarity1
Modified residuei455N6-acetyllysine; alternateBy similarity1
Modified residuei455N6-succinyllysine; alternateBy similarity1
Modified residuei476N6-succinyllysineBy similarity1
Modified residuei489N6-acetyllysine; alternateBy similarity1
Modified residuei489N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P00727

PeptideAtlas

More...PeptideAtlasi		P00727

PRoteomics IDEntifications database

More...PRIDEi		P00727

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSBTAG00000005989, Expressed in caput epididymis and 97 other tissues

<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

Homohexamer.

1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000007860

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P00727

<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

Secondary structure

1519
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P00727

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

More...SMRi		P00727

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P00727

<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

<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 M17 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2597, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00530000063255

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P00727

Identification of Orthologs from Complete Genome Data

More...OMAi		MKNTGPR

Database of Orthologous Groups

More...OrthoDBi		562530at2759

TreeFam database of animal gene trees

More...TreeFami		TF314954

Family and domain databases

Conserved Domains Database

More...CDDi		cd00433, Peptidase_M17, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.220.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00181, Cytosol_peptidase_M17, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011356, Leucine_aapep/pepB
IPR043472, Macro_dom-like
IPR000819, Peptidase_M17_C
IPR023042, Peptidase_M17_leu_NH2_pept
IPR008283, Peptidase_M17_N

The PANTHER Classification System

More...PANTHERi		PTHR11963, PTHR11963, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00883, Peptidase_M17, 1 hit
PF02789, Peptidase_M17_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00481, LAMNOPPTDASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52949, SSF52949, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00631, CYTOSOL_AP, 1 hit

<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>Sequences (3)i

<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.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform 1 (identifier: P00727-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MFLLPLPAAA RVAVRHLSVK RLWAPGPAAA DMTKGLVLGI YSKEKEEDEP 
        60         70         80         90        100
QFTSAGENFN KLVSGKLREI LNISGPPLKA GKTRTFYGLH EDFPSVVVVG 
       110        120        130        140        150
LGKKTAGIDE QENWHEGKEN IRAAVAAGCR QIQDLEIPSV EVDPCGDAQA 
       160        170        180        190        200
AAEGAVLGLY EYDDLKQKRK VVVSAKLHGS EDQEAWQRGV LFASGQNLAR 
       210        220        230        240        250
RLMETPANEM TPTKFAEIVE ENLKSASIKT DVFIRPKSWI EEQEMGSFLS 
       260        270        280        290        300
VAKGSEEPPV FLEIHYKGSP NASEPPLVFV GKGITFDSGG ISIKAAANMD 
       310        320        330        340        350
LMRADMGGAA TICSAIVSAA KLDLPINIVG LAPLCENMPS GKANKPGDVV 
       360        370        380        390        400
RARNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDIAL 
       410        420        430        440        450
GSGATGVFTN SSWLWNKLFE ASIETGDRVW RMPLFEHYTR QVIDCQLADV 
       460        470        480        490        500
NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL DIAGVMTNKD EVPYLRKGMA 
       510 
GRPTRTLIEF LFRFSQDSA
Length:519
Mass (Da):56,289
Last modified:January 23, 2007 - v3
<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:iCDA6AED4D937F624
GO
Isoform 2 (identifier: P00727-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     11-31: Missing.

Show »
Length:498
Mass (Da):54,037
Checksum:i70766756087AB1FD
GO
Isoform 3 (identifier: P00727-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Show »
Length:488
Mass (Da):53,011
Checksum:i11B49D671A1FBD4D
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB28170 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti77P → S in AAB28170 (PubMed:8369298).Curated1
Sequence conflicti414 – 415LW → M AA sequence (PubMed:7085616).Curated2
Sequence conflicti414 – 415LW → M AA sequence (PubMed:7085617).Curated2
Sequence conflicti506 – 513Missing AA sequence (PubMed:7085616).Curated8
Sequence conflicti506 – 513Missing AA sequence (PubMed:7085617).Curated8

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0581501 – 31Missing in isoform 3. CuratedAdd BLAST31
Alternative sequenceiVSP_02263411 – 31Missing in isoform 2. 1 PublicationAdd BLAST21

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
S65367 mRNA Translation: AAB28170.1 Different initiation.
BC105385 mRNA Translation: AAI05386.1
AJ871963 Genomic DNA Translation: CAI44744.1

Protein sequence database of the Protein Information Resource

More...PIRi		A54338, APBOL

NCBI Reference Sequences

More...RefSeqi		NP_776523.2, NM_174098.3 [P00727-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSBTAT00000007860; ENSBTAP00000007860; ENSBTAG00000005989 [P00727-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		781648

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bta:781648

Keywords - Coding sequence diversityi

Alternative initiation

<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
S65367 mRNA Translation: AAB28170.1 Different initiation.
BC105385 mRNA Translation: AAI05386.1
AJ871963 Genomic DNA Translation: CAI44744.1
PIRiA54338, APBOL
RefSeqiNP_776523.2, NM_174098.3 [P00727-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BLLX-ray2.40E33-519[»]
1BPMX-ray2.90A33-519[»]
1BPNX-ray2.90A33-519[»]
1LAMX-ray1.60A33-516[»]
1LANX-ray1.90A33-516[»]
1LAPX-ray2.70A33-519[»]
1LCPX-ray1.65A/B33-516[»]
2EWBX-ray1.85A33-518[»]
2J9AX-ray1.73A33-519[»]
AlphaFoldDBiP00727
SMRiP00727
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000007860

Chemistry databases

BindingDBiP00727
ChEMBLiCHEMBL1671610
DrugCentraliP00727

Protein family/group databases

MEROPSiM17.001

Proteomic databases

PaxDbiP00727
PeptideAtlasiP00727
PRIDEiP00727

Genome annotation databases

EnsembliENSBTAT00000007860; ENSBTAP00000007860; ENSBTAG00000005989 [P00727-1]
GeneIDi781648
KEGGibta:781648

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		51056
VEuPathDBiHostDB:ENSBTAG00000005989
VGNCiVGNC:30786, LAP3

Phylogenomic databases

eggNOGiKOG2597, Eukaryota
GeneTreeiENSGT00530000063255
InParanoidiP00727
OMAiMKNTGPR
OrthoDBi562530at2759
TreeFamiTF314954

Enzyme and pathway databases

BRENDAi3.4.11.1, 908
SABIO-RKiP00727

Miscellaneous databases

EvolutionaryTraceiP00727

Gene expression databases

BgeeiENSBTAG00000005989, Expressed in caput epididymis and 97 other tissues

Family and domain databases

CDDicd00433, Peptidase_M17, 1 hit
Gene3Di3.40.220.10, 1 hit
HAMAPiMF_00181, Cytosol_peptidase_M17, 1 hit
InterProiView protein in InterPro
IPR011356, Leucine_aapep/pepB
IPR043472, Macro_dom-like
IPR000819, Peptidase_M17_C
IPR023042, Peptidase_M17_leu_NH2_pept
IPR008283, Peptidase_M17_N
PANTHERiPTHR11963, PTHR11963, 1 hit
PfamiView protein in Pfam
PF00883, Peptidase_M17, 1 hit
PF02789, Peptidase_M17_N, 1 hit
PRINTSiPR00481, LAMNOPPTDASE
SUPFAMiSSF52949, SSF52949, 1 hit
PROSITEiView protein in PROSITE
PS00631, CYTOSOL_AP, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 nameiAMPL_BOVIN
<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: P00727
Secondary accession number(s): Q2HJH5, Q2PC24
<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: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 180 of the entry and version 3 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

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