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Entry version 74 (02 Jun 2021)
Sequence version 2 (01 Oct 2003)
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Protein

(E,E)-alpha-farnesene synthase

Gene

AFS1

Organism
Malus domestica (Apple) (Pyrus malus)
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

Sesquiterpene synthase catalyzing the production of (E,E)-alpha-farnesene, the predominant terpene produced during storage of fruits. Produces all six isomers (E,E)-alpha-farnesene, (Z,E)-alpha-farnesene, (E,Z)-alpha-farnesene, (Z,Z)-alpha-farnesene, (E)-beta-farnesene and (Z)-beta-farnesene from a mix of isomeric forms of the farnesyl diphosphate precursor. Able to convert geranyl diphosphate to the monoterpenes (E)-beta-ocimene, linalool and beta-myrcene. Has also a prenyltransferase activity producing alpha-farnesene directly from geranyl diphosphate and isoprenyl diphosphate.

Miscellaneous

The activity enhancement by potassium is associated only with sesquiterpene synthase activity and not monoterpene or prenyltransferase activities.
Oxidation products of (E,E)-alpha-farnesene are the causal agents of superficial scald.

<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

Protein has several cofactor binding sites:

<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

activity enhanced 5-fold on addition of 30-50 mM potassium.
  1. KM=3 µM for farnesyl diphosphate1 Publication

    pH dependencei

    Optimum pH is 7.0-8.5.1 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 bindingi326Manganese 2 or magnesium 1By similarity1
    Metal bindingi326Manganese or magnesium 1By similarity1
    Metal bindingi330Manganese 1 or magnesium 1By similarity1
    Metal bindingi330Manganese 2 or magnesium 1By similarity1
    Metal bindingi484PotassiumCurated1
    Metal bindingi487Potassium1

    <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 functionLyase, Transferase
    LigandMagnesium, Manganese, Metal-binding, Potassium

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-13546

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    4.2.3.46, 3164

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q84LB2

    <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:
    (E,E)-alpha-farnesene synthase (EC:4.2.3.46)
    Short name:
    MdASF1
    Alternative name(s):
    Prenyltransferase (EC:2.5.1.-)
    <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:AFS1
    Synonyms:AFAR
    <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>OrganismiMalus domestica (Apple) (Pyrus malus)
    <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 identifieri3750 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeAmygdaloideaeMaleaeMalus

    <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

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi326D → A: Loss of monoterpene synthase, sesquiterpene synthase and prenyltransferase activities. Loss of monoterpene synthase, sesquiterpene synthase and prenyltransferase activities; when associated with A-330. 1 Publication1
    Mutagenesisi330D → A: Loss of monoterpene synthase, sesquiterpene synthase and prenyltransferase activities; when associated with A-326. 1 Publication1
    Mutagenesisi484D → A: No effect on sesquiterpene synthase activity, but loss of activity enhancement by potassium. 1 Publication1
    Mutagenesisi485S → A: No effect on sesquiterpene synthase activity and on activity enhancement by potassium, but 2-fold increase in monoterpene synthase activity. 1 Publication1
    Mutagenesisi487S → A: Loss of sesquiterpene synthase activity. 1 Publication1
    Mutagenesisi487S → K: 4-fold higher sesquiterpene synthase activity in absence of potassium, and loss of activity enhancement by potassium. 1 Publication1
    Mutagenesisi488S → A: Decreased mono- and sesquiterpene synthase activity, but no effect on activity enhancement by potassium. 1 Publication1

    <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_00004014831 – 576(E,E)-alpha-farnesene synthaseAdd BLAST576

    <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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Up-regulated by ethylene. Inhibited by 1-methylcyclopropene (1-MCP).1 Publication

    <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

    Monomer.

    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

    3D structure databases

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

    More...
    SMRi
    Q84LB2

    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 terpene synthase family. Tpsb subfamily.Curated

    Phylogenomic databases

    Database of Orthologous Groups

    More...
    OrthoDBi
    401091at2759

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.600.10, 1 hit
    1.50.10.130, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR008949, Isoprenoid_synthase_dom_sf
    IPR034741, Terpene_cyclase-like_1_C
    IPR001906, Terpene_synth_N
    IPR036965, Terpene_synth_N_sf
    IPR005630, Terpene_synthase_metal-bd
    IPR008930, Terpenoid_cyclase/PrenylTrfase

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01397, Terpene_synth, 1 hit
    PF03936, Terpene_synth_C, 1 hit

    Structure-Function Linkage Database

    More...
    SFLDi
    SFLDG01019, Terpene_Cyclase_Like_1_C_Termi, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48239, SSF48239, 1 hit
    SSF48576, SSF48576, 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.

    Q84LB2-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEFRVHLQAD NEQKIFQNQM KPEPEASYLI NQRRSANYKP NIWKNDFLDQ
    60 70 80 90 100
    SLISKYDGDE YRKLSEKLIE EVKIYISAET MDLVAKLELI DSVRKLGLAN
    110 120 130 140 150
    LFEKEIKEAL DSIAAIESDN LGTRDDLYGT ALHFKILRQH GYKVSQDIFG
    160 170 180 190 200
    RFMDEKGTLE NHHFAHLKGM LELFEASNLG FEGEDILDEA KASLTLALRD
    210 220 230 240 250
    SGHICYPDSN LSRDVVHSLE LPSHRRVQWF DVKWQINAYE KDICRVNATL
    260 270 280 290 300
    LELAKLNFNV VQAQLQKNLR EASRWWANLG IADNLKFARD RLVECFACAV
    310 320 330 340 350
    GVAFEPEHSS FRICLTKVIN LVLIIDDVYD IYGSEEELKH FTNAVDRWDS
    360 370 380 390 400
    RETEQLPECM KMCFQVLYNT TCEIAREIEE ENGWNQVLPQ LTKVWADFCK
    410 420 430 440 450
    ALLVEAEWYN KSHIPTLEEY LRNGCISSSV SVLLVHSFFS ITHEGTKEMA
    460 470 480 490 500
    DFLHKNEDLL YNISLIVRLN NDLGTSAAEQ ERGDSPSSIV CYMREVNASE
    510 520 530 540 550
    ETARKNIKGM IDNAWKKVNG KCFTTNQVPF LSSFMNNATN MARVAHSLYK
    560 570
    DGDGFGDQEK GPRTHILSLL FQPLVN
    Length:576
    Mass (Da):66,183
    Last modified:October 1, 2003 - 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:i4FABCBE4B43B3465
    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 conflicti150G → S in AAX21242 (PubMed:17140613).Curated1
    Sequence conflicti311F → L in AAX21251 (PubMed:17140613).Curated1
    Sequence conflicti343N → S in AAX21251 (PubMed:17140613).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti105E → K in strain: cv. Idared. 1
    Natural varianti113I → V in strain: cv. Aotea. 1
    Natural varianti129G → A in strain: cv. Aotea. 1
    Natural varianti130T → A in strain: cv. Idared. 1
    Natural varianti237N → D in strain: cv. Aotea. 1
    Natural varianti281I → F in strain: cv. Idared, cv. Pinkie, cv. Ralls and cv. Royal Gala. 1
    Natural varianti291R → G in strain: cv. Idared. 1
    Natural varianti297A → S in strain: cv. cv. Idared, cv. Pinkie, cv. Ralls and cv. Royal Gala. 1
    Natural varianti381E → Q in strain: cv. Aotea. 1
    Natural varianti451D → G in strain: cv. Ralls. 1
    Natural varianti505K → E in strain: cv. Aotea. 1
    Natural varianti530F → S in strain: cv. Aotea. 1
    Natural varianti565H → Q in strain: cv. Aotea. 1

    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
    AY182241 mRNA Translation: AAO22848.2
    AY523409 mRNA Translation: AAS01424.1
    AY563622 mRNA Translation: AAS68019.1
    AY787633 mRNA Translation: AAX19772.1
    AY787634 mRNA Translation: AAX19773.1
    AY787635 mRNA Translation: AAX19774.1
    AY787636 mRNA Translation: AAX19775.1
    AY787638 mRNA Translation: AAX19777.1
    AY787639 mRNA Translation: AAX19778.1
    AY787640 mRNA Translation: AAX19779.1
    AY787641 mRNA Translation: AAX19780.1
    AY805408 Genomic DNA Translation: AAX21241.1
    AY805409 Genomic DNA Translation: AAX21242.1
    AY805410 Genomic DNA Translation: AAX21243.1
    AY805413 Genomic DNA Translation: AAX21246.1
    AY805414 Genomic DNA Translation: AAX21247.1
    AY805415 Genomic DNA Translation: AAX21248.1
    AY805416 Genomic DNA Translation: AAX21249.1
    AY805417 Genomic DNA Translation: AAX21250.1
    AY805418 Genomic DNA Translation: AAX21251.1
    AY805419 Genomic DNA Translation: AAX21252.1
    DQ901739 Genomic DNA Translation: ABJ90485.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001280822.1, NM_001293893.1

    Genome annotation databases

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    103446592

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mdm:103446592

    <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
    AY182241 mRNA Translation: AAO22848.2
    AY523409 mRNA Translation: AAS01424.1
    AY563622 mRNA Translation: AAS68019.1
    AY787633 mRNA Translation: AAX19772.1
    AY787634 mRNA Translation: AAX19773.1
    AY787635 mRNA Translation: AAX19774.1
    AY787636 mRNA Translation: AAX19775.1
    AY787638 mRNA Translation: AAX19777.1
    AY787639 mRNA Translation: AAX19778.1
    AY787640 mRNA Translation: AAX19779.1
    AY787641 mRNA Translation: AAX19780.1
    AY805408 Genomic DNA Translation: AAX21241.1
    AY805409 Genomic DNA Translation: AAX21242.1
    AY805410 Genomic DNA Translation: AAX21243.1
    AY805413 Genomic DNA Translation: AAX21246.1
    AY805414 Genomic DNA Translation: AAX21247.1
    AY805415 Genomic DNA Translation: AAX21248.1
    AY805416 Genomic DNA Translation: AAX21249.1
    AY805417 Genomic DNA Translation: AAX21250.1
    AY805418 Genomic DNA Translation: AAX21251.1
    AY805419 Genomic DNA Translation: AAX21252.1
    DQ901739 Genomic DNA Translation: ABJ90485.1
    RefSeqiNP_001280822.1, NM_001293893.1

    3D structure databases

    SMRiQ84LB2
    ModBaseiSearch...

    Genome annotation databases

    GeneIDi103446592
    KEGGimdm:103446592

    Phylogenomic databases

    OrthoDBi401091at2759

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13546
    BRENDAi4.2.3.46, 3164
    SABIO-RKiQ84LB2

    Family and domain databases

    Gene3Di1.10.600.10, 1 hit
    1.50.10.130, 1 hit
    InterProiView protein in InterPro
    IPR008949, Isoprenoid_synthase_dom_sf
    IPR034741, Terpene_cyclase-like_1_C
    IPR001906, Terpene_synth_N
    IPR036965, Terpene_synth_N_sf
    IPR005630, Terpene_synthase_metal-bd
    IPR008930, Terpenoid_cyclase/PrenylTrfase
    PfamiView protein in Pfam
    PF01397, Terpene_synth, 1 hit
    PF03936, Terpene_synth_C, 1 hit
    SFLDiSFLDG01019, Terpene_Cyclase_Like_1_C_Termi, 1 hit
    SUPFAMiSSF48239, SSF48239, 1 hit
    SSF48576, SSF48576, 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 nameiAFS1_MALDO
    <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: Q84LB2
    Secondary accession number(s): Q2VU74
    , Q2VU78, Q2VU82, Q2VU83, Q32WH6, Q32WH8, Q32WI0, Q32WI2, Q6Q2J2, Q6QWJ1
    <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 30, 2010
    Last sequence update: October 1, 2003
    Last modified: June 2, 2021
    This is version 74 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
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