Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q68FS4 (AMPL_RAT)

Entry version 112 (07 Apr 2021)
Sequence version 1 (11 Oct 2004)
Previous versions | rss
Add a publicationFeedback
Protein

Cytosol aminopeptidase

Gene

Lap3

Organism
Rattus norvegicus (Rat)
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:6108111, PubMed:12675513). 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 (By similarity). For instance, in the presence of Mn2+, it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates (By similarity). 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:12675513).By similarity2 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

  • Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.1 Publication EC:3.4.11.1
  • Release of N-terminal proline from a peptide.By similarity EC:3.4.11.5

<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+By similarity, Mn2+By similarityNote: 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+. 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. Mn2+ is required for Cys-Gly hydrolysis activity. A third metal binding site may serve a structural role, possibly stabilizing part of the interface between the N-terminal and the catalytic domain.By similarity

<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

Bimane-S-cysteinylglycine-hydrolyzing activity is inhibited by o-phenanthroline or bestatin, and is activated by the addition of zinc chloride.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

    1. Vmax=1.6 µmol/min/mg enzyme for peptidase activity with S-benzyl-cysteine-p-nitroanilide1 Publication
    2. Vmax=11.9 µmol/min/mg enzyme for peptidase activity with Leucine-p-nitroanilide1 Publication
    3. Vmax=9.4 µmol/min/mg enzyme for peptidase activity with Alanine-p-nitroanilide1 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; structuralBy similarity1
    Metal bindingi203Zinc 3; via carbonyl oxygen; structuralBy similarity1
    Metal bindingi282Zinc 2; catalyticBy similarity1
    <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 sitei282SubstrateBy similarity1
    Metal bindingi287Zinc 1 or magnesium; catalyticBy similarity1
    Metal bindingi287Zinc 2; catalyticBy similarity1
    Binding sitei287SubstrateBy similarity1
    Binding sitei292SubstrateBy 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 sitei294By similarity1
    Binding sitei294SubstrateBy similarity1
    Metal bindingi303Zinc 3; via carbonyl oxygen; structuralBy similarity1
    Metal bindingi305Zinc 2; catalyticBy similarity1
    Binding sitei305SubstrateBy similarity1
    Metal bindingi364Zinc 1 or magnesium; catalyticBy similarity1
    Binding sitei364SubstrateBy similarity1
    Metal bindingi366Zinc 1 or magnesium; catalyticBy similarity1
    Metal bindingi366Zinc 2; catalyticBy similarity1
    Active sitei368By similarity1

    <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, Hydrolase, Protease
    LigandMagnesium, Manganese, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:MONOMER-10001

    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 3Imported
    Short name:
    LAP-3
    Leucyl aminopeptidase1 Publication
    Short name:
    LAP1 Publication
    Peptidase SBy similarity
    Proline aminopeptidaseBy similarity (EC:3.4.11.5By similarity)
    Prolyl aminopeptidaseImported
    <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:Lap3Imported
    <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>OrganismiRattus norvegicus (Rat)
    <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 identifieri10116 [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 › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
    <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
    • UP000002494 <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 14

    Organism-specific databases

    Rat genome database

    More...    RGDi    		1307985, 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 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_00002741461 – 519Cytosol aminopeptidaseAdd BLAST519

    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 residuei42PhosphoserineCombined sources1
    Modified residuei45N6-succinyllysineBy similarity1
    Modified residuei54PhosphoserineCombined sources1
    Modified residuei61N6-succinyllysineBy similarity1
    Modified residuei103N6-succinyllysineBy similarity1
    Modified residuei180PhosphoserineBy similarity1
    Modified residuei194PhosphoserineBy similarity1
    Modified residuei221N6-acetyllysine; alternateBy similarity1
    Modified residuei221N6-succinyllysine; alternateBy 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

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		Q68FS4

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

    More...    PaxDbi    		Q68FS4

    PRoteomics IDEntifications database

    More...    PRIDEi    		Q68FS4

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		Q68FS4

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...    PhosphoSitePlusi    		Q68FS4

    <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    		ENSRNOG00000003289, Expressed in jejunum and 21 other tissues

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		Q68FS4, RN

    <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.

    By similarity

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		10116.ENSRNOP00000004770

    <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    		Q68FS4

    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

    <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

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_013734_1_2_1

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		Q68FS4

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		MKNTGPR

    Database of Orthologous Groups

    More...    OrthoDBi    		562530at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		Q68FS4

    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 (2)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.

    This entry describes 2 <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: Q68FS4-1) [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
    MYLLPLPAAA RVALRRLGVR GLWDRGLSTA DMTKGLVLGI YSKDKDDDVP 
            60         70         80         90        100
    QFTSAGENFN KLVSGRLREM LNISGPPLKA GKTRTFYGLH QDFPSVVVVG 
           110        120        130        140        150
    LGKRSAGVDD QENWHEGKEN IRAAVAAGCR QVQDLELPSV EVDPCGDAQA 
           160        170        180        190        200
    AAEGAVLGLY EYDDLKQKKK VAVSAKLHGS GDLEAWEKGV LFASGQNLAR 
           210        220        230        240        250
    QLMESPANEM TPTRFAEVIE KNLKSASSKT EVHIRTKSWI EEQEMGSFLS 
           260        270        280        290        300
    VAKGSEEPPV FLEIHYTGSP NATEAPLVFV GKGITFDSGG ISIKASANMD 
           310        320        330        340        350
    LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV 
           360        370        380        390        400
    RARNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDVAL 
           410        420        430        440        450
    GSGATGVFTN SSWLWNKLFE ASVETGDRVW RMPLFEHYTR QVIDCQLADV 
           460        470        480        490        500
    NNLGKYRSAG ACTAAAFLRE FVTHTKWAHL DIAGVMTNKD EIPYLRKGMS 
           510 
    GRPTRTLIEF LLRFSKDSS
    Length:519
    Mass (Da):56,150
    Last modified:October 11, 2004 - 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:i0D4DFDC93D0CFF9D
    GO
    Isoform 2 (identifier: Q68FS4-2) [UniParc]FASTAAdd to basket

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

    Show »
    Length:488
    Mass (Da):52,759
    Checksum:iADBF6E2235FB3D94
    GO

    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_0226331 – 31Missing in isoform 2. CuratedAdd BLAST31

    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
    		BC079381 mRNA Translation: AAH79381.1

    NCBI Reference Sequences

    More...    RefSeqi    		NP_001011910.1, NM_001011910.1 [Q68FS4-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENSRNOT00000004770; ENSRNOP00000004770; ENSRNOG00000003289 [Q68FS4-1]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		289668

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		rno:289668

    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
    		BC079381 mRNA Translation: AAH79381.1
    RefSeqiNP_001011910.1, NM_001011910.1 [Q68FS4-1]

    3D structure databases

    SMRiQ68FS4
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000004770

    Protein family/group databases

    MEROPSiM17.001

    PTM databases

    iPTMnetiQ68FS4
    PhosphoSitePlusiQ68FS4

    Proteomic databases

    jPOSTiQ68FS4
    PaxDbiQ68FS4
    PRIDEiQ68FS4

    Genome annotation databases

    EnsembliENSRNOT00000004770; ENSRNOP00000004770; ENSRNOG00000003289 [Q68FS4-1]
    GeneIDi289668
    KEGGirno:289668

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		51056
    RGDi1307985, Lap3

    Phylogenomic databases

    eggNOGiKOG2597, Eukaryota
    GeneTreeiENSGT00530000063255
    HOGENOMiCLU_013734_1_2_1
    InParanoidiQ68FS4
    OMAiMKNTGPR
    OrthoDBi562530at2759
    PhylomeDBiQ68FS4
    TreeFamiTF314954

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-10001

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:Q68FS4

    Gene expression databases

    BgeeiENSRNOG00000003289, Expressed in jejunum and 21 other tissues
    GenevisibleiQ68FS4, RN

    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_RAT
    <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: Q68FS4
    <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 23, 2007
    Last sequence update: October 11, 2004
    Last modified: April 7, 2021
    This is version 112 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, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again