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UniProtKB - Q68FS4 (AMPL_RAT)

Entry version 115 (23 Feb 2022)
Sequence version 1 (11 Oct 2004)
Previous versions | rss
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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

Cytosolic 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 bindingi287Magnesium; catalyticBy similarity1
Metal bindingi287Zinc 1; 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 bindingi364Magnesium; catalyticBy similarity1
Metal bindingi364Zinc 1; catalyticBy similarity1
Binding sitei364SubstrateBy similarity1
Metal bindingi366Magnesium; catalyticBy similarity1
Metal bindingi366Zinc 1; 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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.13.23, 5301

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.<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 <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
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

BRENDAi3.4.13.23, 5301

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

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: February 23, 2022
This is version 115 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
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