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Entry version 133 (23 Feb 2022)
Sequence version 2 (27 Sep 2005)
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Protein

4-coumarate--CoA ligase 1

Gene

4CL1

Organism
Oryza sativa subsp. japonica (Rice)
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 phenylpropanoid metabolism by mediating the activation of a number of hydroxycinnamates for the biosynthesis of monolignols and other phenolic secondary metabolites (PubMed:21807887, PubMed:23246835).

Catalyzes the formation of CoA esters of cinnamate, 4-coumarate, caffeate and ferulate (PubMed:21807887, PubMed:23246835).

Is more efficient with substrates in the following order: ferulate > 4-coumarate > cinnamate > caffeate (PubMed:21807887).

Cannot convert sinapate to its corresponding CoA ester (PubMed:21807887, PubMed:23246835).

2 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 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 0.37 min(-1) with cinnamate as substrate (PubMed:21807887). kcat is 0.49 min(-1) with 4-coumarate as substrate (PubMed:21807887). kcat is 0.52 min(-1) with caffeate as substrate (PubMed:21807887). kcat is 0.41 min(-1) with ferulate as substrate (PubMed:21807887).1 Publication
  1. KM=9.4 µM for cinnamate1 Publication
  2. KM=11.9 µM for 4-coumarate1 Publication
  3. KM=29.3 µM for caffeate1 Publication
  4. KM=8.3 µM for ferulate1 Publication
  1. Vmax=100 pmol/sec/mg enzyme with cinnamate as substrate1 Publication
  2. Vmax=130 pmol/sec/mg enzyme with 4-coumarate as substrate1 Publication
  3. Vmax=140 pmol/sec/mg enzyme with caffeate as substrate1 Publication
  4. Vmax=110 pmol/sec/mg enzyme with ferulate 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: 3,4',5-trihydroxystilbene biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 3,4',5-trihydroxystilbene from trans-4-coumarate.Curated This subpathway is part of the pathway 3,4',5-trihydroxystilbene biosynthesis, which is itself part of Phytoalexin biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 3,4',5-trihydroxystilbene from trans-4-coumarate, the pathway 3,4',5-trihydroxystilbene biosynthesis and in Phytoalexin 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 sitei257ATPBy similarity1
Binding sitei356ATPBy similarity1
Binding sitei440ATPBy similarity1
Binding sitei455ATPBy similarity1
Binding sitei547ATPBy 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 bindingi209 – 217ATPBy similarity9
Nucleotide bindingi352 – 357ATPBy similarity6

<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 functionLigase
Biological processPhenylpropanoid metabolism
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.2.1.12, 4460

Reactome - a knowledgebase of biological pathways and processes for plant species

More...
PlantReactomei
R-OSA-1119316, Phenylpropanoid biosynthesis
R-OSA-1119418, Suberin biosynthesis
R-OSA-1119531, Flavonoid biosynthesis

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

More...
UniPathwayi
UPA00372;UER00547

<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:
4-coumarate--CoA ligase 11 Publication (EC:6.2.1.122 Publications)
Short name:
4CL 11 Publication
Short name:
Os4CL11 Publication
Alternative name(s):
4-coumaroyl-CoA synthase 1Curated
<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:4CL11 Publication
Synonyms:4CLCurated
Ordered Locus Names:Os08g0245200Imported, LOC_Os08g14760Curated
ORF Names:OJ1033_B09.16Imported
<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>OrganismiOryza sativa subsp. japonica (Rice)
<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 identifieri39947 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryzaOryza sativa
<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
  • UP000059680 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8
  • UP000000763 Componenti: Chromosome 8

<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_00001930311 – 5644-coumarate--CoA ligase 1Add BLAST564

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P17814

<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 roots, stems, leaf blades and leaf sheaths.1 Publication

<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

Induced by fungal elicitor and UV irradiation. Down-regulated by wounding and UV irradiation (PubMed:23246835).1 Publication

Gene expression databases

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P17814, OS

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
4530.OS08T0245200-01

<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

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SMRi
P17814

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni282 – 351SBD1By similarityAdd BLAST70
Regioni352 – 419SBD2By similarityAdd BLAST68

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity.By similarity

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1176, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000022_59_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P17814

Identification of Orthologs from Complete Genome Data

More...
OMAi
AHMRLFI

Database of Orthologous Groups

More...
OrthoDBi
683933at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.300.30, 1 hit
3.40.50.12780, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025110, AMP-bd_C
IPR045851, AMP-bd_C_sf
IPR020845, AMP-binding_CS
IPR000873, AMP-dep_Synth/Lig
IPR042099, ANL_N_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00501, AMP-binding, 1 hit
PF13193, AMP-binding_C, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00455, AMP_BINDING, 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.

P17814-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGSMEQQQPE SAAPATEASP EIIFRSKLQD IAITNTLPLH RYCFERLPEV
60 70 80 90 100
AARPCLIDGA TGGVLTYADV DRLSRRLAAA LRRAPLGLRR GGVVMSLLRN
110 120 130 140 150
SPEFVLSFFA ASRVGAAVTT ANPMSTPHEI ESQLAAAGAT VVITESMAAD
160 170 180 190 200
KLPSHSHGAL TVVLIDERRD GCLHFWDDLM SEDEASPLAG DEDDEKVFDP
210 220 230 240 250
DDVVALPYSS GTTGLPKGVM LTHRSLSTSV AQQVDGENPN IGLHAGDVIL
260 270 280 290 300
CALPMFHIYS LNTIMMCGLR VGAAIVVMRR FDLAAMMDLV ERHRVTIAPL
310 320 330 340 350
VPPIVVAVAK SEAAAARDLS SVRMVLSGAA PMGKDIEDAF MAKLPGAVLG
360 370 380 390 400
QGYGMTEAGP VLSMCLAFAK EPFKVKSGAC GTVVRNAELK IIDPDTGKSL
410 420 430 440 450
GRNLPGEICI RGQQIMKGYL NNPEATKNTI DAEGWLHTGD IGYVDDDDEI
460 470 480 490 500
FIVDRLKEII KYRGFQVAPA ELEALLITHP SIADAAVVGK QIEPEIGEIP
510 520 530 540 550
VAFVAKTEGS ELSEDDVKQF VAKEVIYYKK IREVFFVDKI PKAPSGKILR
560
KELRKQLQHL QQEA
Length:564
Mass (Da):60,902
Last modified:September 27, 2005 - 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:i9725A4B4A72F8C6E
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 BAD05189 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA36850 differs from that shown. Reason: Frameshift.Curated
The sequence CAA36850 differs from that shown. Reason: Erroneous gene model prediction.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 conflicti405P → R in CAA36850 (PubMed:2235510).Curated1
Sequence conflicti477I → N in CAA36850 (PubMed:2235510).Curated1

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
X52623 Genomic DNA Translation: CAA36850.1 Sequence problems.
AP003859 Genomic DNA Translation: BAD05189.1 Different initiation.
AP008214 Genomic DNA Translation: BAF23267.1
AP014964 Genomic DNA Translation: BAT04523.1
AK069932 mRNA Translation: BAG91685.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JU0311

NCBI Reference Sequences

More...
RefSeqi
XP_015650724.1, XM_015795238.1

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
Os08t0245200-01; Os08t0245200-01; Os08g0245200

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4345054

Gramene; a comparative resource for plants

More...
Gramenei
Os08t0245200-01; Os08t0245200-01; Os08g0245200

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
osa:4345054

<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
X52623 Genomic DNA Translation: CAA36850.1 Sequence problems.
AP003859 Genomic DNA Translation: BAD05189.1 Different initiation.
AP008214 Genomic DNA Translation: BAF23267.1
AP014964 Genomic DNA Translation: BAT04523.1
AK069932 mRNA Translation: BAG91685.1
PIRiJU0311
RefSeqiXP_015650724.1, XM_015795238.1

3D structure databases

SMRiP17814
ModBaseiSearch...

Protein-protein interaction databases

STRINGi4530.OS08T0245200-01

Proteomic databases

PaxDbiP17814

Genome annotation databases

EnsemblPlantsiOs08t0245200-01; Os08t0245200-01; Os08g0245200
GeneIDi4345054
GrameneiOs08t0245200-01; Os08t0245200-01; Os08g0245200
KEGGiosa:4345054

Phylogenomic databases

eggNOGiKOG1176, Eukaryota
HOGENOMiCLU_000022_59_2_1
InParanoidiP17814
OMAiAHMRLFI
OrthoDBi683933at2759

Enzyme and pathway databases

UniPathwayiUPA00372;UER00547
BRENDAi6.2.1.12, 4460
PlantReactomeiR-OSA-1119316, Phenylpropanoid biosynthesis
R-OSA-1119418, Suberin biosynthesis
R-OSA-1119531, Flavonoid biosynthesis

Gene expression databases

GenevisibleiP17814, OS

Family and domain databases

Gene3Di3.30.300.30, 1 hit
3.40.50.12780, 1 hit
InterProiView protein in InterPro
IPR025110, AMP-bd_C
IPR045851, AMP-bd_C_sf
IPR020845, AMP-binding_CS
IPR000873, AMP-dep_Synth/Lig
IPR042099, ANL_N_sf
PfamiView protein in Pfam
PF00501, AMP-binding, 1 hit
PF13193, AMP-binding_C, 1 hit
PROSITEiView protein in PROSITE
PS00455, AMP_BINDING, 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 namei4CL1_ORYSJ
<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: P17814
Secondary accession number(s): B7EH38, Q0J6Z8, Q6ZKV9
<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: August 1, 1990
Last sequence update: September 27, 2005
Last modified: February 23, 2022
This is version 133 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. Oryza sativa (rice)
    Index of Oryza sativa entries and their corresponding gene designations
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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