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Entry version 176 (07 Apr 2021)
Sequence version 3 (23 Jan 2007)
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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

Cytolosic 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 bindingi287Zinc 1 or magnesium; 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 bindingi364Zinc 1 or magnesium; catalyticCombined sources3 Publications1
    Binding sitei364SubstrateCombined sources1 Publication1
    Metal bindingi366Zinc 1 or magnesium; 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

    <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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
    <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

    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 adult mammalian kidney and 18 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

    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

    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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 <div> <p><b>What is the canonical sequence?</b><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[»]
    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
    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 adult mammalian kidney and 18 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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    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: April 7, 2021
    This is version 176 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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