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Entry version 84 (02 Jun 2021)
Sequence version 2 (13 Apr 2004)
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Chitin-binding lectin 1

Solanum tuberosum (Potato)
Reviewed-Annotation score:

Annotation score:4 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

This protein might function as a defense against chitin containing pathogens. Binds to several branched or linear N-acetyllactosamine-containing glycosphingolipids and also to lactosylceramide with sphingosine and non-hydroxy fatty acids.


Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="">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 sitei78ChitooligosaccharideBy similarity1
Binding sitei80ChitooligosaccharideBy similarity1
Binding sitei82ChitooligosaccharideBy similarity1
Binding sitei89ChitooligosaccharideBy similarity1
Binding sitei230ChitooligosaccharideBy similarity1
Binding sitei232ChitooligosaccharideBy similarity1
Binding sitei234ChitooligosaccharideBy similarity1
Binding sitei241ChitooligosaccharideBy similarity1

<p>The <a href="">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="">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

Biological processPlant defense
LigandChitin-binding, Lectin

<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="">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:
Chitin-binding lectin 1
Alternative name(s):
<p>This subsection of the <a href="">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>OrganismiSolanum tuberosum (Potato)
<p>This subsection of the <a href="">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 identifieri4113 [NCBI]
<p>This subsection of the <a href="">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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
<p>This subsection of the <a href="">Names and taxonomy</a> section is present for entries that are part of a <a href="">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
  • UP000011115 <p>A UniProt <a href="">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 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 – 22Sequence analysisAdd BLAST22
<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_000000527423 – 323Chitin-binding lectin 1Add BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="">lipids</a>, <a href="">glycans</a> and <a href="">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei504-hydroxyproline1 Publication1
<p>This subsection of the <a href="">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>Glycosylationi50O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei514-hydroxyproline1 Publication1
Glycosylationi51O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei534-hydroxyproline1 Publication1
Glycosylationi53O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei554-hydroxyproline1 Publication1
Glycosylationi55O-linked (Ara...) hydroxyproline1 Publication1
<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 bondi61 ↔ 77PROSITE-ProRule annotation
Disulfide bondi70 ↔ 83PROSITE-ProRule annotation
Disulfide bondi76 ↔ 90PROSITE-ProRule annotation
Disulfide bondi95 ↔ 99PROSITE-ProRule annotation
Disulfide bondi108 ↔ 125PROSITE-ProRule annotation
Disulfide bondi117 ↔ 131PROSITE-ProRule annotation
Disulfide bondi124 ↔ 138PROSITE-ProRule annotation
Disulfide bondi143 ↔ 147PROSITE-ProRule annotation
Glycosylationi151O-linked (Gal) serine1 Publication1
Modified residuei1524-hydroxyproline1 Publication1 Publication1
Glycosylationi152O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1534-hydroxyproline1 Publication1 Publication1
Glycosylationi153O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1544-hydroxyproline1 Publication1 Publication1
Glycosylationi154O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1554-hydroxyproline1 Publication1 Publication1
Glycosylationi155O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1564-hydroxyproline1 Publication1 Publication1
Glycosylationi156O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1574-hydroxyproline1 Publication1 Publication1
Glycosylationi157O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1584-hydroxyproline1 Publication1
Glycosylationi158O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1594-hydroxyproline1 Publication1 Publication1
Glycosylationi159O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi160O-linked (Gal) serine1 Publication1
Modified residuei1614-hydroxyproline1 Publication1 Publication1
Glycosylationi161O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1624-hydroxyproline1 Publication1 Publication1
Glycosylationi162O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1634-hydroxyproline1 Publication1 Publication1
Glycosylationi163O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1644-hydroxyproline1 Publication1 Publication1
Glycosylationi164O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi165O-linked (Gal) serine1 Publication1
Modified residuei1664-hydroxyproline1 Publication1 Publication1
Glycosylationi166O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1674-hydroxyproline1 Publication1 Publication1
Glycosylationi167O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi168O-linked (Gal) serine1 Publication1
Modified residuei1694-hydroxyproline1 Publication1 Publication1
Glycosylationi169O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1704-hydroxyproline1 Publication1 Publication1
Glycosylationi170O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1714-hydroxyproline1 Publication1 Publication1
Glycosylationi171O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1724-hydroxyproline1 Publication1 Publication1
Glycosylationi172O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi173O-linked (Gal) serine1 Publication1
Modified residuei1744-hydroxyproline1 Publication1 Publication1
Glycosylationi174O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1754-hydroxyproline1 Publication1 Publication1
Glycosylationi175O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1764-hydroxyproline1 Publication1
Glycosylationi176O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1774-hydroxyproline1 Publication1 Publication1
Glycosylationi177O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1784-hydroxyproline1 Publication1
Glycosylationi178O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1794-hydroxyproline1 Publication1
Glycosylationi179O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1804-hydroxyproline1 Publication1
Glycosylationi180O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi181O-linked (Gal) serine1 Publication1
Modified residuei1824-hydroxyproline1 Publication1
Glycosylationi182O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1834-hydroxyproline1 Publication1
Glycosylationi183O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1844-hydroxyproline1 Publication1
Glycosylationi184O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1854-hydroxyproline1 Publication1
Glycosylationi185O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi186O-linked (Gal) serine1 Publication1
Modified residuei1874-hydroxyproline1 Publication1
Glycosylationi187O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1884-hydroxyproline1 Publication1
Glycosylationi188O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1894-hydroxyproline1 Publication1
Glycosylationi189O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1904-hydroxyproline1 Publication1
Glycosylationi190O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi191O-linked (Gal) serine1 Publication1
Modified residuei1924-hydroxyproline1 Publication1
Glycosylationi192O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi193O-linked (Gal) serine1 Publication1
Modified residuei1944-hydroxyproline1 Publication1
Glycosylationi194O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1954-hydroxyproline1 Publication1
Glycosylationi195O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1964-hydroxyproline1 Publication1
Glycosylationi196O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1974-hydroxyproline1 Publication1
Glycosylationi197O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei1984-hydroxyproline1 Publication1
Glycosylationi198O-linked (Ara...) hydroxyproline1 Publication1
Glycosylationi200O-linked (Gal) serine1 Publication1
Modified residuei2014-hydroxyproline1 Publication1
Glycosylationi201O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2024-hydroxyproline1 Publication1
Glycosylationi202O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2034-hydroxyproline1 Publication1
Glycosylationi203O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2044-hydroxyproline1 Publication1
Glycosylationi204O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2054-hydroxyproline1 Publication1
Glycosylationi205O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2064-hydroxyproline1 Publication1
Glycosylationi206O-linked (Ara...) hydroxyproline1 Publication1
Modified residuei2094-hydroxyproline1 Publication1
Glycosylationi209O-linked (Ara...) hydroxyproline1 Publication1
Disulfide bondi213 ↔ 229PROSITE-ProRule annotation
Disulfide bondi222 ↔ 235PROSITE-ProRule annotation
Disulfide bondi228 ↔ 242PROSITE-ProRule annotation
Disulfide bondi247 ↔ 251PROSITE-ProRule annotation
Disulfide bondi260 ↔ 277PROSITE-ProRule annotation
Disulfide bondi269 ↔ 283PROSITE-ProRule annotation
Disulfide bondi276 ↔ 290PROSITE-ProRule annotation
Disulfide bondi295 ↔ 299PROSITE-ProRule annotation

<p>This subsection of the <a href="">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

Heavily glycosylated with beta-arabinose on hydroxyprolines and with alpha-galactose on serines of the extensin-like domain. As no other sugars could be detected in the native lectin, it is unlikely that the three putative N-glycosylation sites are actually glycosylated.1 Publication
The N-terminus is blocked. The N-terminal sequences proposed in PubMed:9022287 and PubMed:11056399 originate probably from truncated proteins.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

PTM databases

iPTMnet integrated resource for PTMs in systems biology context


<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

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

Q9S8M0, baseline and differential

<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="">'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="">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei



<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


Database of comparative protein structure models


<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="">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>Domaini58 – 101Chitin-binding type-1 1PROSITE-ProRule annotationAdd BLAST44
Domaini105 – 149Chitin-binding type-1 2PROSITE-ProRule annotationAdd BLAST45
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati151 – 15919
Repeati160 – 16425
Repeati165 – 16733
Repeati168 – 17245
Repeati173 – 18058
Repeati181 – 18565
Repeati186 – 19075
Repeati191 – 19282
Repeati193 – 19896
Repeati200 – 206107
Domaini210 – 253Chitin-binding type-1 3PROSITE-ProRule annotationAdd BLAST44
Domaini257 – 301Chitin-binding type-1 4PROSITE-ProRule annotationAdd BLAST45


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>Regioni150 – 210Extensin-likeAdd BLAST61
Regioni151 – 20610 X approximate repeats of S-P-P-P-PAdd BLAST56
Regioni154 – 203DisorderedSequence analysisAdd BLAST50

<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

In the central section; belongs to the extensin family.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

Gene3Di, 4 hits

Integrated resource of protein families, domains and functional sites

View protein in InterPro
IPR001002, Chitin-bd_1
IPR036861, Endochitinase-like_sf

Pfam protein domain database

View protein in Pfam
PF00187, Chitin_bind_1, 4 hits

Simple Modular Architecture Research Tool; a protein domain database

View protein in SMART
SM00270, ChtBD1, 4 hits

Superfamily database of structural and functional annotation

SSF57016, SSF57016, 4 hits

PROSITE; a protein domain and family database

View protein in PROSITE
PS00026, CHIT_BIND_I_1, 2 hits
PS50941, CHIT_BIND_I_2, 4 hits

<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="">length</a> and <a href="">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="">Sequence</a> section indicates if the <a href="">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="">Sequence</a> section indicates if the <a href="">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.

Q9S8M0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
60 70 80 90 100
110 120 130 140 150
160 170 180 190 200
210 220 230 240 250
260 270 280 290 300
310 320
Mass (Da):33,554
Last modified:April 13, 2004 - 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="">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2E415620F8C7FC40

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 conflicti50P → T AA sequence (PubMed:9022287).Curated1
Sequence conflicti50P → T AA sequence (PubMed:11056399).Curated1
Sequence conflicti54S → P AA sequence (PubMed:9022287).Curated1
Sequence conflicti54S → P AA sequence (PubMed:11056399).Curated1
Sequence conflicti59 – 61PQC → LQY AA sequence (PubMed:11056399).Curated3
Sequence conflicti63M → L AA sequence (PubMed:9022287).Curated1
Sequence conflicti63M → L AA sequence (PubMed:11056399).Curated1
Sequence conflicti66G → P AA sequence (PubMed:9022287).Curated1
Sequence conflicti73T → G AA sequence (PubMed:11056399).Curated1
Sequence conflicti158P → H AA sequence (PubMed:8054990).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database


GenBank nucleotide sequence database


DNA Data Bank of Japan; a nucleotide sequence database

Links Updated
BG350800 mRNA No translation available.

<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="">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:
Links Updated
BG350800 mRNA No translation available.

3D structure databases


PTM databases


Gene expression databases

ExpressionAtlasiQ9S8M0, baseline and differential

Family and domain databases

Gene3Di3.30.60.10, 4 hits
InterProiView protein in InterPro
IPR001002, Chitin-bd_1
IPR036861, Endochitinase-like_sf
PfamiView protein in Pfam
PF00187, Chitin_bind_1, 4 hits
SMARTiView protein in SMART
SM00270, ChtBD1, 4 hits
SUPFAMiSSF57016, SSF57016, 4 hits
PROSITEiView protein in PROSITE
PS00026, CHIT_BIND_I_1, 2 hits
PS50941, CHIT_BIND_I_2, 4 hits

MobiDB: a database of protein disorder and mobility annotations


<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 nameiLECT_SOLTU
<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: Q9S8M0
<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="">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: June 2, 2021
This is version 84 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

Direct protein sequencing, Reference proteome


  1. SIMILARITY comments
    Index of protein domains and families
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