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Entry version 52 (25 May 2022)
Sequence version 1 (06 Dec 2005)
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Protein

Cannabichromenic acid synthase

Gene

CBCAS

Organism
Cannabis sativa (Hemp) (Marijuana)
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

Oxidoreductase involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (Ref. 5, Ref. 3, PubMed:9862135). Catalyzes the oxidative cyclization of the monoterpene moiety in cannabigerolic acid (CBGA) producing cannabichromenic acid (CBCA), which exhibits anti-inflammatory, antifungal and antimicrobial effects (Ref. 5, Ref. 3, PubMed:9862135). Can also use cannabinerolic acid (CBNRA) as substrate (PubMed:9862135).

Unable to catalyze the production of delta9-tetrahydrocannabinolate (THCA), the precursor of Delta1-tetrahydrocannabinol (PubMed:16143478).

4 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

FADBy similarityNote: Binds 1 FAD per subunit in a bicovalent manner.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

Inhibited by hydrogen peroxide H2O2 and FMN (PubMed:9862135). Completely repressed activity by Hg2+ (PubMed:9862135).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

kcat is 0.04 sec(-1) with cannabigerolic acid as substrate.1 Publication
  1. KM=23 µM for cannabigerolic acid1 Publication
  2. KM=33 µM for cannabinerolic acid1 Publication
  1. Vmax=0.63 nmol/sec/mg enzyme with cannabigerolic acid as substrate1 Publication
  2. Vmax=0.14 nmol/sec/mg enzyme with cannabinerolic acid as substrate1 Publication

pH dependencei

Optimum pH is 6.5.1 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: terpenoid biosynthesis

This protein is involved in the pathway terpenoid biosynthesis, which is part of Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway terpenoid biosynthesis and in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei120FADBy similarity1
Binding sitei176FADBy similarity1
Binding sitei190FAD; via carbonyl oxygenBy similarity1
Binding sitei236FADBy similarity1
Binding sitei241FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei292CannabigerolateBy similarity1
Binding sitei417CannabigerolateBy similarity1
Binding sitei442CannabigerolateBy 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 sitei484Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi109 – 115FADBy similarity7
Nucleotide bindingi180 – 184FADBy similarity5
Nucleotide bindingi481 – 483FADBy similarity3

<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 functionOxidoreductase
LigandFAD, Flavoprotein

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00213

<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:
Cannabichromenic acid synthase3 Publications (EC:1.21.99.-3 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:CBCAS3 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>OrganismiCannabis sativa (Hemp) (Marijuana)
<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 identifieri3483 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesCannabaceaeCannabis

<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 – 28Sequence analysisAdd BLAST28
<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_000042114329 – 545Cannabichromenic acid synthaseAdd BLAST517

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 bondi37 ↔ 99By similarity
<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>Glycosylationi65N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi89N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki114 ↔ 1766-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)By similarity
Glycosylationi168N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi297N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi305N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi329N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi467N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi499N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage.By similarity

Keywords - PTMi

Disulfide bond, 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

Expressed in young leaves.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 (By similarity). May form homodimer (PubMed:9862135).

By similarity1 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

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
Q33DQ2

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

More...
SMRi
Q33DQ2

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini77 – 251FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST175

<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

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.43.10, 1 hit
3.30.465.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012951, BBE
IPR016166, FAD-bd_PCMH
IPR036318, FAD-bd_PCMH-like_sf
IPR016167, FAD-bd_PCMH_sub1
IPR016169, FAD-bd_PCMH_sub2
IPR006094, Oxid_FAD_bind_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08031, BBE, 1 hit
PF01565, FAD_binding_4, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56176, SSF56176, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51387, FAD_PCMH, 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.

Q33DQ2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNCSAFSFWF VCKIIFFFLS FNIQISIANP QENFLKCFSE YIPNNPANPK
60 70 80 90 100
FIYTQHDQLY MSVLNSTIQN LRFTSDTTPK PLVIVTPSNV SHIQASILCS
110 120 130 140 150
KKVGLQIRTR SGGHDAEGLS YISQVPFAIV DLRNMHTVKV DIHSQTAWVE
160 170 180 190 200
AGATLGEVYY WINEMNENFS FPGGYCPTVG VGGHFSGGGY GALMRNYGLA
210 220 230 240 250
ADNIIDAHLV NVDGKVLDRK SMGEDLFWAI RGGGGENFGI IAAWKIKLVV
260 270 280 290 300
VPSKATIFSV KKNMEIHGLV KLFNKWQNIA YKYDKDLMLT THFRTRNITD
310 320 330 340 350
NHGKNKTTVH GYFSSIFLGG VDSLVDLMNK SFPELGIKKT DCKELSWIDT
360 370 380 390 400
TIFYSGVVNY NTANFKKEIL LDRSAGKKTA FSIKLDYVKK LIPETAMVKI
410 420 430 440 450
LEKLYEEEVG VGMYVLYPYG GIMDEISESA IPFPHRAGIM YELWYTATWE
460 470 480 490 500
KQEDNEKHIN WVRSVYNFTT PYVSQNPRLA YLNYRDLDLG KTNPESPNNY
510 520 530 540
TQARIWGEKY FGKNFNRLVK VKTKADPNNF FRNEQSIPPL PPHHH
Length:545
Mass (Da):61,990
Last modified:December 6, 2005 - 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:i1A19BECE99931796
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 conflicti5A → T in AYW35088 (PubMed:31718081).Curated1
Sequence conflicti5A → T in AYW35091 (PubMed:31718081).Curated1
Sequence conflicti5A → T in AYW35095 (PubMed:31718081).Curated1
Sequence conflicti5A → T in AYW35097 (PubMed:31718081).Curated1
Sequence conflicti5A → T (Ref. 3) Curated1
Sequence conflicti244W → C (Ref. 3) Curated1
Sequence conflicti543H → R (Ref. 3) Curated1

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Several isoforms of the inactive tetrahydrocannabinolic acid synthase found in the 'fiber-type' cannabis plants exist due to polymorphism.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
JQ437493 Genomic DNA Translation: AFI24257.1
JQ437494 Genomic DNA Translation: AFI24258.1
JQ437495 Genomic DNA Translation: AFI24259.1
JQ437496 Genomic DNA Translation: AFI24260.1
AB212830 Genomic DNA Translation: BAE48242.1
AB212831 Genomic DNA Translation: BAE48243.1
MG996402 Genomic DNA Translation: AYW35088.1
MG996405 Genomic DNA Translation: AYW35091.1
MG996409 Genomic DNA Translation: AYW35095.1
MG996411 Genomic DNA Translation: AYW35097.1

<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
JQ437493 Genomic DNA Translation: AFI24257.1
JQ437494 Genomic DNA Translation: AFI24258.1
JQ437495 Genomic DNA Translation: AFI24259.1
JQ437496 Genomic DNA Translation: AFI24260.1
AB212830 Genomic DNA Translation: BAE48242.1
AB212831 Genomic DNA Translation: BAE48243.1
MG996402 Genomic DNA Translation: AYW35088.1
MG996405 Genomic DNA Translation: AYW35091.1
MG996409 Genomic DNA Translation: AYW35095.1
MG996411 Genomic DNA Translation: AYW35097.1

3D structure databases

AlphaFoldDBiQ33DQ2
SMRiQ33DQ2
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00213

Family and domain databases

Gene3Di3.30.43.10, 1 hit
3.30.465.10, 1 hit
InterProiView protein in InterPro
IPR012951, BBE
IPR016166, FAD-bd_PCMH
IPR036318, FAD-bd_PCMH-like_sf
IPR016167, FAD-bd_PCMH_sub1
IPR016169, FAD-bd_PCMH_sub2
IPR006094, Oxid_FAD_bind_N
PfamiView protein in Pfam
PF08031, BBE, 1 hit
PF01565, FAD_binding_4, 1 hit
SUPFAMiSSF56176, SSF56176, 1 hit
PROSITEiView protein in PROSITE
PS51387, FAD_PCMH, 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 nameiCBCAS_CANSA
<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: Q33DQ2
Secondary accession number(s): A0A3G5EA46, A0A3G5EAK0
<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: February 6, 2013
Last sequence update: December 6, 2005
Last modified: May 25, 2022
This is version 52 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 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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