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Entry version 111 (02 Jun 2021)
Sequence version 1 (01 Jan 1998)
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Protein

Rhamnogalacturonan exolyase YesX

Gene

yesX

Organism
Bacillus subtilis (strain 168)
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

Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases disaccharide products (PubMed:17449691, PubMed:19193638).

Degrades rhamnogalacturonan, polygalacturonic acid and pectic acid. Has very low activity on pectin (PubMed:17449691).

2 Publications

Caution

This enzyme is expected to be secreted, but there is no predicted signal sequence.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Exotype eliminative cleavage of alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I oligosaccharides containing alpha-L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end. The products are the disaccharide 2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose and the shortened rhamnogalacturonan oligosaccharide containing one 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.2 Publications EC:4.2.2.24

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

Protein has several cofactor binding sites:

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.78 mg/ml for rhamnogalacturonan (RG) type I region of plant cell wall pectin1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei119SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi120Calcium 1Combined sources1 Publication1
Metal bindingi125Calcium 2Combined sources1 Publication1
Metal bindingi127Calcium 2Combined sources1 Publication1
Metal bindingi129Calcium 2Combined sources1 Publication1
Metal bindingi131Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi133Calcium 2Combined sources1 Publication1
Binding sitei139SubstrateBy similarity1
Binding sitei154SubstrateBy similarity1
Binding sitei174SubstrateBy similarity1
Metal bindingi189Calcium 3Combined sources1 Publication1
Metal bindingi191Calcium 3Combined sources1 Publication1
Metal bindingi193Calcium 3Combined sources1 Publication1
Metal bindingi195Calcium 3; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi197Calcium 3Combined sources1 Publication1
Binding sitei205Substrate; via carbonyl oxygenBy similarity1
Binding sitei222SubstrateBy similarity1
Metal bindingi330Calcium 4; via tele nitrogenCombined sources1 Publication1
Metal bindingi336Calcium 5Combined sources1 Publication1
Metal bindingi338Calcium 5Combined sources1 Publication1
Metal bindingi338Calcium 6Combined sources1 Publication1
Metal bindingi340Calcium 5Combined sources1 Publication1
Metal bindingi340Calcium 6Combined sources1 Publication1
Metal bindingi342Calcium 5; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi344Calcium 5Combined sources1 Publication1
Metal bindingi344Calcium 6Combined sources1 Publication1
Metal bindingi353Calcium 6Combined sources1 Publication1
Metal bindingi354Calcium 6; via pros nitrogenCombined sources1 Publication1
Metal bindingi366Calcium 4; via tele nitrogenCombined sources1 Publication1
Metal bindingi368Calcium 4Combined sources1 Publication1
Metal bindingi374Calcium 7Combined sources1 Publication1
Metal bindingi376Calcium 7; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi379Calcium 7; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi381Calcium 7; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi383Calcium 7Combined sources1 Publication1
Metal bindingi389Calcium 4Combined sources1 Publication1
Binding sitei419SubstrateBy similarity1
Metal bindingi472Calcium 8Combined sources1 Publication1
Metal bindingi474Calcium 8Combined sources1 Publication1
Metal bindingi476Calcium 8; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi478Calcium 8Combined sources1 Publication1
Metal bindingi527Calcium 10By similarity1
Metal bindingi529Calcium 10; via carbonyl oxygenBy similarity1
Metal bindingi529Calcium 9; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi531Calcium 10; via carbonyl oxygenBy similarity1
Metal bindingi531Calcium 9; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi533Calcium 10; via carbonyl oxygenBy similarity1
Metal bindingi533Calcium 9; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi535Calcium 10By similarity1
Metal bindingi535Calcium 9Combined sources1 Publication1
Metal bindingi576Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi578Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Binding sitei579SubstrateBy similarity1
Metal bindingi580Calcium 1Combined sources1 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 functionLyase
Biological processCell wall biogenesis/degradation
LigandCalcium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU07060-MONOMER
MetaCyc:BSU07060-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.2.24, 658

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
O31527

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
PL11, Polysaccharide Lyase Family 11

<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_and_taxonomy_section">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:
Rhamnogalacturonan exolyase YesX (EC:4.2.2.242 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:yesX
Ordered Locus Names:BSU07060
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiBacillus subtilis (strain 168)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri224308 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi439 – 447Missing : Changes the activity from exo- to endo-cleavage. 1 Publication9

<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_00003602131 – 612Rhamnogalacturonan exolyase YesXAdd BLAST612

Proteomic databases

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

More...
PaxDbi
O31527

PRoteomics IDEntifications database

More...
PRIDEi
O31527

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

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

Up-regulated by growth on type I rhamnogalacturonan.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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
224308.BSU07060

<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

Secondary structure

1612
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
O31527

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
O31527

<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>Regioni516 – 518Substrate bindingBy similarity3

<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 polysaccharide lyase 11 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3401, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O31527

Identification of Orthologs from Complete Genome Data

More...
OMAi
DDGLMWG

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O31527

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10318, RGL11, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013517, FG-GAP
IPR013783, Ig-like_fold
IPR041624, RGI_lyase
IPR034641, RGL11

The PANTHER Classification System

More...
PANTHERi
PTHR43118, PTHR43118, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01839, FG-GAP, 1 hit
PF18370, RGI_lyase, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

O31527-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKPKKRQMEY LTRGLIAVQT EQGVFVSWRF LGTDHETTAF HLYRDGKRIT
60 70 80 90 100
RDPIAESTNF LDQNGTADSV YQVAAVNKGR EEKLSKKARV WQENVLEVPL
110 120 130 140 150
AKPEGGVTPD GKPYTYSAND ASVGDIDGDG EYEMILKWDP SNSKDNAHDG
160 170 180 190 200
YTGEVLIDAY KLDGTFLWRI NLGRNIRAGA HYTQFMVYDL DGDGKAEIAM
210 220 230 240 250
KTADGTTDGK GHIIGDEQAD FRNEQGRILS GPEYLTVFKG ETGEALTTVE
260 270 280 290 300
YEPPRGKLED WGDGYGNRMD RFLAGTAYLD GERPSLVMAR GYYTRTVLVA
310 320 330 340 350
YDFRNGRLKK RWVFDSNQPG HEAYAGQGNH SLSVADVDGD GKDEIIYGAM
360 370 380 390 400
AVDHDGTGLY STGLGHGDAM HVGDLDPSRK GLEVFQVHED ATKPYGLSLR
410 420 430 440 450
DAGTGEILWG VHAGTDVGRG MAAHIDPSYK GSLVWGIDPP GNDGMSYGLF
460 470 480 490 500
TSKGEKISDK APSSANFAIW WDGDLVRELL DHDWDGTIGR PKIEKWDAEN
510 520 530 540 550
GCLKTIFQPA GVLSNNGTKG NPVLQANLFG DWREEVIWRT EDSSALRIYT
560 570 580 590 600
TTHLTRHCFY TLMHDPVYRL GIAWQNTAYN QPPHTSFYLG TGMKKPPKPA
610
LYIAGSKAEA PL
Length:612
Mass (Da):67,690
Last modified:January 1, 1998 - 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:iE7A320888A608D4B
GO

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
AL009126 Genomic DNA Translation: CAB12525.1

Protein sequence database of the Protein Information Resource

More...
PIRi
G69797

NCBI Reference Sequences

More...
RefSeqi
NP_388587.1, NC_000964.3
WP_010886437.1, NZ_CP053102.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB12525; CAB12525; BSU_07060

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
936081

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU07060

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.43.peg.744

<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
AL009126 Genomic DNA Translation: CAB12525.1
PIRiG69797
RefSeqiNP_388587.1, NC_000964.3
WP_010886437.1, NZ_CP053102.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZUYX-ray1.65A1-612[»]
SMRiO31527
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU07060

Protein family/group databases

CAZyiPL11, Polysaccharide Lyase Family 11

Proteomic databases

PaxDbiO31527
PRIDEiO31527

Genome annotation databases

EnsemblBacteriaiCAB12525; CAB12525; BSU_07060
GeneIDi936081
KEGGibsu:BSU07060
PATRICifig|224308.43.peg.744

Phylogenomic databases

eggNOGiCOG3401, Bacteria
InParanoidiO31527
OMAiDDGLMWG
PhylomeDBiO31527

Enzyme and pathway databases

BioCyciBSUB:BSU07060-MONOMER
MetaCyc:BSU07060-MONOMER
BRENDAi4.2.2.24, 658
SABIO-RKiO31527

Miscellaneous databases

EvolutionaryTraceiO31527

Family and domain databases

CDDicd10318, RGL11, 1 hit
Gene3Di2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR013517, FG-GAP
IPR013783, Ig-like_fold
IPR041624, RGI_lyase
IPR034641, RGL11
PANTHERiPTHR43118, PTHR43118, 1 hit
PfamiView protein in Pfam
PF01839, FG-GAP, 1 hit
PF18370, RGI_lyase, 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 nameiYESX_BACSU
<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: O31527
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: June 2, 2021
This is version 111 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 programProkaryotic 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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