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Entry version 88 (07 Apr 2021)
Sequence version 2 (27 Apr 2001)
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Protein

Ananain

Gene

AN1

Organism
Ananas comosus (Pineapple) (Ananas ananas)
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

Cysteine protease. Displays a high level of diversity in substrate specificity at the P1-P1' cleavage site. A hydrophilic P1 residue is preferred, with Gln or Arg strongly preferred. Favors an Ile/Leu residue at the P2 position of substrates, with an overall higher preference for Leu. The optimal tripeptide for cleavage is Pro-Leu-Gln, with cleavage occurring after the Gln residue. Another optimal tripeptide is Val-Leu-Arg, which may imply that a hydrophobic residue at the P3 position of substrates is preferred.1 Publication

<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 <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

Strongly inhibited by chicken egg-white cystatin (Probable). Inhibited by iodoacetamide and the active-site-directed inhibitor trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane (E-64) (PubMed:31306685).Curated1 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 13.9 s(-1) for Z-Phe-Val-Arg-AMC. kcat is 1.58 s(-1) for Z-Phe-Arg-AMC. kcat is 0.16 s(-1) for Z-Arg-Arg-AMC. kcat is 9.80 s(-1) for Pro-Leu-Gln. kcat is 7.13 s(-1) for Val-Leu-Arg. kcat is 5.62 s(-1) for Pro-Leu-Arg. kcat is 4.96 s(-1) for Ala-Leu-Arg. kcat is 6.29 s(-1) for Val-Leu-Lys. kcat is 6.08 s(-1) for Pro-Leu-Lys. kcat is 3.58 s(-1) for Ala-Leu-Lys. kcat is 0.36 s(-1) for Pro-Leu-Asn.1 Publication
  1. KM=10.5 µM for synthetic 7-amino-4-methylcoumarin (AMC) substrate Z-Phe-Val-Arg-AMC (at pH 5.0 and 37 degrees Celsius)1 Publication
  2. KM=18.0 µM for synthetic 7-amino-4-methylcoumarin (AMC) substrate Z-Phe-Arg-AMC (at pH 5.0 and 37 degrees Celsius)1 Publication
  3. KM=198 µM for synthetic 7-amino-4-methylcoumarin (AMC) substrate Z-Arg-Arg-AMC (at pH 5.0 and 37 degrees Celsius)1 Publication
  4. KM=5.92 µM for tripeptidyl substrate Pro-Leu-Gln (at pH 7.4 and 37 degrees Celsius)1 Publication
  5. KM=4.29 µM for tripeptidyl substrate Val-Leu-Arg (at pH 7.4 and 37 degrees Celsius)1 Publication
  6. KM=3.94 µM for tripeptidyl substrate Pro-Leu-Arg (at pH 7.4 and 37 degrees Celsius)1 Publication
  7. KM=4.15 µM for tripeptidyl substrate Ala-Leu-Arg (at pH 7.4 and 37 degrees Celsius)1 Publication
  8. KM=5.36 µM for tripeptidyl substrate Val-Leu-Lys (at pH 7.4 and 37 degrees Celsius)1 Publication
  9. KM=6.94 µM for tripeptidyl substrate Pro-Leu-Lys (at pH 7.4 and 37 degrees Celsius)1 Publication
  10. KM=5.85 µM for tripeptidyl substrate Ala-Leu-Lys (at pH 7.4 and 37 degrees Celsius)1 Publication
  11. KM=4.50 µM for tripeptidyl substrate Pro-Leu-Asn (at pH 7.4 and 37 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei147PROSITE-ProRule annotation1 Publication1
    Active sitei279PROSITE-ProRule annotation1 Publication1
    Active sitei300PROSITE-ProRule annotation1

    <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 functionHydrolase, Protease, Thiol protease

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    C01.026

    <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:
    Ananain2 Publications (EC:3.4.22.311 Publication)
    <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:AN11 PublicationImported
    <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>OrganismiAnanas comosus (Pineapple) (Ananas ananas)
    <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 identifieri4615 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaLiliopsidaPoalesBromeliaceaeBromelioideaeAnanas

    <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

    Protein family/group databases

    Allergome; a platform for allergen knowledge

    More...
    Allergomei
    694, Ana c 2

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002640025 – 122Sequence analysis1 PublicationAdd BLAST98
    <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_0000026401123 – 345Ananain1 PublicationAdd BLAST223

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi144 ↔ 184Combined sources1 Publication
    Disulfide bondi178 ↔ 217Combined sources1 Publication
    Disulfide bondi273 ↔ 325Combined sources1 Publication

    Keywords - PTMi

    Disulfide bond, Zymogen

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

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

    Stem (at protein level).1 Publication

    <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

    1345
    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
    P80884

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    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 C1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02248, Peptidase_C1A, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR038765, Papain-like_cys_pep_sf
    IPR025661, Pept_asp_AS
    IPR000169, Pept_cys_AS
    IPR025660, Pept_his_AS
    IPR000668, Peptidase_C1A_C
    IPR039417, Peptidase_C1A_papain-like
    IPR013201, Prot_inhib_I29

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF08246, Inhibitor_I29, 1 hit
    PF00112, Peptidase_C1, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00705, PAPAIN

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00848, Inhibitor_I29, 1 hit
    SM00645, Pept_C1, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF54001, SSF54001, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00640, THIOL_PROTEASE_ASN, 1 hit
    PS00139, THIOL_PROTEASE_CYS, 1 hit
    PS00639, THIOL_PROTEASE_HIS, 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>Sequencei

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

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P80884-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MTSKVQLVFL FLFLCVMWAS PSAASCDEPS DPMMKQFEEW MAEYGRVYKD
    60 70 80 90 100
    NDEKMLRFQI FKNNVNHIET FNNRNGNSYT LGINQFTDMT NNEFVAQYTG
    110 120 130 140 150
    LSLPLNIKRE PVVSFDDVDI SSVPQSIDWR DSGAVTSVKN QGRCGSCWAF
    160 170 180 190 200
    ASIATVESIY KIKRGNLVSL SEQQVLDCAV SYGCKGGWIN KAYSFIISNK
    210 220 230 240 250
    GVASAAIYPY KAAKGTCKTN GVPNSAYITR YTYVQRNNER NMMYAVSNQP
    260 270 280 290 300
    IAAALDASGN FQHYKRGVFT GPCGTRLNHA IVIIGYGQDS SGKKFWIVRN
    310 320 330 340
    SWGAGWGEGG YIRLARDVSS SFGLCGIAMD PLYPTLQSGP SVEVI
    Length:345
    Mass (Da):38,248
    Last modified:April 27, 2001 - v2
    <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:iFAF2989080174D87
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti291S → A AA sequence (PubMed:9355753).Curated1
    Sequence conflicti324L → I AA sequence (PubMed:9355753).Curated1

    <p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 23478 Da. Determined by ESI. 1 Publication

    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
    AJ002477 mRNA Translation: CAA05487.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    T07839

    NCBI Reference Sequences

    More...
    RefSeqi
    XP_020089326.1, XM_020233737.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    109710925

    <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
    AJ002477 mRNA Translation: CAA05487.1
    PIRiT07839
    RefSeqiXP_020089326.1, XM_020233737.1

    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
    6MISX-ray1.98A/B123-337[»]
    6OKJX-ray1.73A/B123-337[»]
    6Y6LX-ray1.30A/B123-338[»]
    6YCBX-ray1.26A/B123-338[»]
    6YCCX-ray1.30A/B123-338[»]
    6YCDX-ray1.35A/B123-338[»]
    SMRiP80884
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    Allergomei694, Ana c 2
    MEROPSiC01.026

    Genome annotation databases

    GeneIDi109710925

    Family and domain databases

    CDDicd02248, Peptidase_C1A, 1 hit
    InterProiView protein in InterPro
    IPR038765, Papain-like_cys_pep_sf
    IPR025661, Pept_asp_AS
    IPR000169, Pept_cys_AS
    IPR025660, Pept_his_AS
    IPR000668, Peptidase_C1A_C
    IPR039417, Peptidase_C1A_papain-like
    IPR013201, Prot_inhib_I29
    PfamiView protein in Pfam
    PF08246, Inhibitor_I29, 1 hit
    PF00112, Peptidase_C1, 1 hit
    PRINTSiPR00705, PAPAIN
    SMARTiView protein in SMART
    SM00848, Inhibitor_I29, 1 hit
    SM00645, Pept_C1, 1 hit
    SUPFAMiSSF54001, SSF54001, 1 hit
    PROSITEiView protein in PROSITE
    PS00640, THIOL_PROTEASE_ASN, 1 hit
    PS00139, THIOL_PROTEASE_CYS, 1 hit
    PS00639, THIOL_PROTEASE_HIS, 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 nameiANAN_ANACO
    <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: P80884
    Secondary accession number(s): O22293
    <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: November 1, 1997
    Last sequence update: April 27, 2001
    Last modified: April 7, 2021
    This is version 88 of the entry and version 2 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 programPlant 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

    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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