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Entry version 60 (02 Jun 2021)
Sequence version 2 (18 Sep 2019)
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Protein

Amorpha-4,11-diene 12-monooxygenase

Gene

CYP71AV1

Organism
Artemisia annua (Sweet wormwood)
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

Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (PubMed:16458889, PubMed:16612385, PubMed:20351109, PubMed:27488942).

Catalyzes three consecutive oxidations of amorpha-4,11-diene to produce artemisinic acid, with artemisinic alcohol and artemisinic aldehyde as intermediates products, but is unable to oxidize germacrene A (PubMed:16458889, PubMed:16612385, PubMed:20351109, PubMed:23246612).

No activity with limonene, alpha-pinene, beta-pinene, pinocarveol, (-)-alloisolongifolene, caryophyllene, (-)-alpha-gurjunene, (+)-gamma-gurjunene, (+)-ledene, (+)-beta-selinene and (+)-valencene as substrates (PubMed:16458889, PubMed:16612385, PubMed:20351109).

1 Publication4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

hemeBy similarity

<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=0.04 nmol/min/mg enzyme with artemisinic alcohol as substrate1 Publication
    2. Vmax=0.02 nmol/min/mg enzyme with dihydroartemisinic alcohol as substrate1 Publication
    3. Vmax=0.510 nmol/min/mg enzyme with artemisinic aldehyde as substrate1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Sesquiterpene biosynthesis

    This protein is involved in Sesquiterpene biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in Sesquiterpene biosynthesis.

    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 bindingi439Iron (heme axial ligand)By similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei479Required for artemisinic alcohol oxidizing activity that catalyzes the conversion of artemisinic alcohol to artemisinic aldehyde1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <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 functionMonooxygenase, Oxidoreductase
    LigandHeme, Iron, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.14.13.158, 7150
    1.14.14.114, 7150

    <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:
    Amorpha-4,11-diene 12-monooxygenase1 Publication (EC:1.14.14.1144 Publications)
    Alternative name(s):
    Amorpha-4,11-diene C-12 oxidase2 Publications
    Short name:
    Amorphadiene oxidase1 Publication
    Cytochrome P450 71AV13 Publications
    <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:CYP71AV13 Publications
    <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>OrganismiArtemisia annua (Sweet wormwood)
    <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 identifieri35608 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeAnthemideaeArtemisiinaeArtemisia
    <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
    • UP000245207 <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: Unassembled WGS sequence

    <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

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 6CytoplasmicSequence analysis6
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei7 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
    Topological domaini30 – 495LumenalSequence analysisAdd BLAST466

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    <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

    <p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Artemisinin and derivatives (e.g. artesunate), are antimalarial drugs due to their endoperoxidase properties; they also display multiple pharmacological actions against inflammation,viral infections, and cell and tumor proliferation (PubMed:32514287, PubMed:32405226). Artesunate may be a promising treatment for COVID-19 mediated by the severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2) because of its anti-inflammatory activity, NF-kappaB (nuclear factor kappa B)-coronavirus effect and chloroquine-like endocytosis inhibition mechanism (PubMed:32514287, PubMed:32405226).2 Publications
    Yeast (S.cerevisiae) has been engineered to produce artemisinic-acid, a precursor of the antimalarial artemisinin compound, by expressing AMS1/ADS, CYP71AV1, ADH1 and ALDH1 in conjunction with CYB5 and CPR1.3 Publications

    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>Mutagenesisi307S → A: Reduced activity leading to a slightly reduced accumulation of artemisinic acid. 1 Publication1
    Mutagenesisi369L → M: Reduced activity leading to a reduced accumulation of artemisinic acid. 1 Publication1
    Mutagenesisi479S → F: Altered artemisinic alcohol oxidizing activity leading to the accumulation of artemisinic alcohol. 1 Publication1
    Mutagenesisi483M → V: Reduced activity leading to a reduced accumulation of artemisinic acid. 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_00004127671 – 495Amorpha-4,11-diene 12-monooxygenaseAdd BLAST495

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi176N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi261N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi267N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi386N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi417N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

    Keywords - PTMi

    Glycoprotein

    <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

    Highly expressed both in apical and sub-apical cells of glandular secretory trichomes (PubMed:22195571, PubMed:19664791). Detected in flower buds, leaves and roots (PubMed:22986332). Also present in non-glandular trichome cells (PubMed:30851440).6 Publications

    <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

    Strongly induced by gibberellic acid (GA3) leading to an increased artemisinin yield (Ref. 19). Accumulates in the presence of trans-cinnamic acid (PubMed:22986332).2 Publications

    <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
    Q1PS23

    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 cytochrome P450 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.630.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR001128, Cyt_P450
    IPR017972, Cyt_P450_CS
    IPR002401, Cyt_P450_E_grp-I
    IPR036396, Cyt_P450_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00067, p450, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00463, EP450I
    PR00385, P450

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48264, SSF48264, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00086, CYTOCHROME_P450, 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: Q1PS23-1) [UniParc]FASTAAdd to basket
    Also known as: AMOLAP1 Publication

    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
    MKSILKAMAL SLTTSIALAT ILLFVYKFAT RSKSTKKSLP EPWRLPIIGH
    60 70 80 90 100
    MHHLIGTTPH RGVRDLARKY GSLMHLQLGE VPTIVVSSPK WAKEILTTYD
    110 120 130 140 150
    ISFANRPETL TGEIVLYHNT DVVLAPYGEY WRQLRKICTL ELLSVKKVKS
    160 170 180 190 200
    FQSLREEECW NLVQEIKASG SGRPVNLSEN VFKLIATILS RAAFGKGIKD
    210 220 230 240 250
    QKELTEIVKE ILRQTGGFDV ADIFPSKKFL HHLSGKRARL TSLRKKIDNL
    260 270 280 290 300
    IDNLVAEHTV NTSSKTNETL LDVLLRLKDS AEFPLTSDNI KAIILDMFGA
    310 320 330 340 350
    GTDTSSSTIE WAISELIKCP KAMEKVQAEL RKALNGKEKI HEEDIQELSY
    360 370 380 390 400
    LNMVIKETLR LHPPLPLVLP RECRQPVNLA GYNIPNKTKL IVNVFAINRD
    410 420 430 440 450
    PEYWKDAEAF IPERFENSSA TVMGAEYEYL PFGAGRRMCP GAALGLANVQ
    460 470 480 490
    LPLANILYHF NWKLPNGVSY DQIDMTESSG ATMQRKTELL LVPSF
    Length:495
    Mass (Da):55,711
    Last modified:September 18, 2019 - 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:iF4B6D33FD1E1BBA7
    GO
    Isoform 2 (identifier: Q1PS23-2) [UniParc]FASTAAdd to basket
    Also known as: AMOHAP1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         1-7: Missing.

    Note: Reduced production of artemisinic acid (AA) but increased accumulation of artemisinic alcohol (AAOH) and artemisinic aldehyde (AAA), and production of (DHAA) probably due to a lower catalytic activity.1 Publication
    Show »
    Length:488
    Mass (Da):54,939
    Checksum:iC1FB730ADECE8662
    GO

    <p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence ABC41927 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
    The sequence ABG49365 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti27K → E in ACF74516 (Ref. 6) Curated1
    Sequence conflicti62G → R in AFO64615 (PubMed:22986332).Curated1
    Sequence conflicti64R → G in ACF74516 (Ref. 6) Curated1
    Sequence conflicti95I → V in ABI31728 (PubMed:18816428).Curated1
    Sequence conflicti102 – 103SF → TS in ADU25498 (Ref. 7) Curated2
    Sequence conflicti102 – 103SF → TS in AIC83779 (Ref. 11) Curated2
    Sequence conflicti102S → T in ABB82944 (PubMed:16612385).1
    Sequence conflicti102S → T in ABG91755 (Ref. 3) 1
    Sequence conflicti102S → T in ABI31728 (PubMed:18816428).1
    Sequence conflicti102S → T in ABC41927 (PubMed:16458889).1
    Sequence conflicti102S → T in ABE57266 (Ref. 2) 1
    Sequence conflicti102S → T in AFP19100 (PubMed:23638869).1
    Sequence conflicti102S → T in AFO64615 (PubMed:22986332).1
    Sequence conflicti140L → S in ACF74516 (Ref. 6) Curated1
    Sequence conflicti181V → I in ABC41927 (PubMed:16458889).Curated1
    Sequence conflicti181V → I in ABG91755 (Ref. 3) Curated1
    Sequence conflicti211I → T in ACF74516 (Ref. 6) Curated1
    Sequence conflicti314S → P in ABI31728 (PubMed:18816428).Curated1
    Sequence conflicti323M → L in ABG91755 (Ref. 3) Curated1
    Sequence conflicti467G → D in ABG49365 (Ref. 4) Curated1
    Sequence conflicti467G → D in ABM88788 (Ref. 4) Curated1
    Sequence conflicti487T → A in ABI31728 (PubMed:18816428).Curated1
    Sequence conflicti487T → A in AFP19100 (PubMed:23638869).Curated1

    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_0602701 – 7Missing in isoform 2. 1 Publication7

    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
    DQ268763 mRNA Translation: ABB82944.1
    DQ453967 mRNA Translation: ABE57266.1
    DQ826743 Genomic DNA Translation: ABG91755.1
    EF197889 mRNA Translation: ABM88788.1
    DQ872632 mRNA Translation: ABI31728.1
    EU684540 mRNA Translation: ACF74516.1
    HQ315834 mRNA Translation: ADU25498.1
    JN594504 mRNA Translation: AFO64615.1
    AB706288 mRNA Translation: BAM68808.1
    JQ254992 mRNA Translation: AFP19100.1
    KJ609178 mRNA Translation: AIC83779.1
    PKPP01014078 Genomic DNA Translation: PWA40082.1
    HM048927 Genomic DNA Translation: ADI24872.1
    DQ667170 Genomic DNA Translation: ABG49365.1 Different initiation.
    DQ315671 mRNA Translation: ABC41927.1 Different initiation.

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:ABB82944

    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
    DQ268763 mRNA Translation: ABB82944.1
    DQ453967 mRNA Translation: ABE57266.1
    DQ826743 Genomic DNA Translation: ABG91755.1
    EF197889 mRNA Translation: ABM88788.1
    DQ872632 mRNA Translation: ABI31728.1
    EU684540 mRNA Translation: ACF74516.1
    HQ315834 mRNA Translation: ADU25498.1
    JN594504 mRNA Translation: AFO64615.1
    AB706288 mRNA Translation: BAM68808.1
    JQ254992 mRNA Translation: AFP19100.1
    KJ609178 mRNA Translation: AIC83779.1
    PKPP01014078 Genomic DNA Translation: PWA40082.1
    HM048927 Genomic DNA Translation: ADI24872.1
    DQ667170 Genomic DNA Translation: ABG49365.1 Different initiation.
    DQ315671 mRNA Translation: ABC41927.1 Different initiation.

    3D structure databases

    SMRiQ1PS23
    ModBaseiSearch...

    Genome annotation databases

    KEGGiag:ABB82944

    Enzyme and pathway databases

    BRENDAi1.14.13.158, 7150
    1.14.14.114, 7150

    Family and domain databases

    Gene3Di1.10.630.10, 1 hit
    InterProiView protein in InterPro
    IPR001128, Cyt_P450
    IPR017972, Cyt_P450_CS
    IPR002401, Cyt_P450_E_grp-I
    IPR036396, Cyt_P450_sf
    PfamiView protein in Pfam
    PF00067, p450, 1 hit
    PRINTSiPR00463, EP450I
    PR00385, P450
    SUPFAMiSSF48264, SSF48264, 1 hit
    PROSITEiView protein in PROSITE
    PS00086, CYTOCHROME_P450, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
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    <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 nameiAMO_ARTAN
    <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: Q1PS23
    Secondary accession number(s): A0A0G2R041
    , B4YUM0, D7RD93, G4WEL3, K7PPJ8, K7ZNY4, Q0GC64, Q0GYM3, Q0PIP7, Q0Z841, Q2F517, R9QHY0
    <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: September 21, 2011
    Last sequence update: September 18, 2019
    Last modified: June 2, 2021
    This is version 60 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

    Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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