Ribonuclease E

<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

Miscellaneous

<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

• Endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions.UniRule annotation

  Manual assertion according to rulesⁱ

  • HAMAP-Rule:MF_00970

  3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.19

    "'Zn-link': a metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E."
    Callaghan A.J., Redko Y., Murphy L.M., Grossmann J.G., Yates D., Garman E., Ilag L.L., Robinson C.V., Symmons M.F., McDowall K.J., Luisi B.F.
    Biochemistry 44:4667-4675(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, RNA-BINDING, SUBUNIT, ZINC-BINDING, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-404 AND CYS-407.
  • Ref.21

    "Rapid cleavage of RNA by RNase E in the absence of 5' monophosphate stimulation."
    Kime L., Jourdan S.S., Stead J.A., Hidalgo-Sastre A., McDowall K.J.
    Mol. Microbiol. 76:590-604(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF THR-170.
  • Ref.27

    "Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover."
    Callaghan A.J., Marcaida M.J., Stead J.A., McDowall K.J., Scott W.G., Luisi B.F.
    Nature 437:1187-1191(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-510 IN COMPLEXES WITH RNA; ZINC AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF PHE-57; PHE-67; LYS-112; THR-170; ASP-303; ASN-305; ASP-346 AND ARG-373.

  EC:3.1.26.12

<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

• Zn²⁺
  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.
  3 Publications

  Manual assertion based on experiment inⁱ

  • Ref.19

    "'Zn-link': a metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E."
    Callaghan A.J., Redko Y., Murphy L.M., Grossmann J.G., Yates D., Garman E., Ilag L.L., Robinson C.V., Symmons M.F., McDowall K.J., Luisi B.F.
    Biochemistry 44:4667-4675(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, RNA-BINDING, SUBUNIT, ZINC-BINDING, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-404 AND CYS-407.
  • Ref.27

    "Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover."
    Callaghan A.J., Marcaida M.J., Stead J.A., McDowall K.J., Scott W.G., Luisi B.F.
    Nature 437:1187-1191(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-510 IN COMPLEXES WITH RNA; ZINC AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF PHE-57; PHE-67; LYS-112; THR-170; ASP-303; ASN-305; ASP-346 AND ARG-373.
  • Ref.29

    "The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation."
    Koslover D.J., Callaghan A.J., Marcaida M.J., Garman E.F., Martick M., Scott W.G., Luisi B.F.
    Structure 16:1238-1244(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-515 IN COMPLEX WITH RNA AND ZINC IONS, SUBUNIT.
  Note: Binds 2 Zn²⁺ ions per homotetramer. Zinc ions are bound between subunits and are essential for homotetramerization and catalytic activity, but not for RNA binding. In the absence of zinc, the protein dissociates into inactive dimers.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.19

    "'Zn-link': a metal-sharing interface that organizes the quaternary structure and catalytic site of the endoribonuclease, RNase E."
    Callaghan A.J., Redko Y., Murphy L.M., Grossmann J.G., Yates D., Garman E., Ilag L.L., Robinson C.V., Symmons M.F., McDowall K.J., Luisi B.F.
    Biochemistry 44:4667-4675(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: CATALYTIC ACTIVITY, RNA-BINDING, SUBUNIT, ZINC-BINDING, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-404 AND CYS-407.
• Mg²⁺
  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.27

    "Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover."
    Callaghan A.J., Marcaida M.J., Stead J.A., McDowall K.J., Scott W.G., Luisi B.F.
    Nature 437:1187-1191(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-510 IN COMPLEXES WITH RNA; ZINC AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF PHE-57; PHE-67; LYS-112; THR-170; ASP-303; ASN-305; ASP-346 AND ARG-373.
  Note: Binds 1 Mg²⁺ ion per subunit.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.27

    "Structure of Escherichia coli RNase E catalytic domain and implications for RNA turnover."
    Callaghan A.J., Marcaida M.J., Stead J.A., McDowall K.J., Scott W.G., Luisi B.F.
    Nature 437:1187-1191(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-510 IN COMPLEXES WITH RNA; ZINC AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF PHE-57; PHE-67; LYS-112; THR-170; ASP-303; ASN-305; ASP-346 AND ARG-373.

<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

<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

Sites

<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

• 7S RNA binding Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E."
    Callaghan A.J., Aurikko J.P., Ilag L.L., Gunter Grossmann J., Chandran V., Kuhnel K., Poljak L., Carpousis A.J., Robinson C.V., Symmons M.F., Luisi B.F.
    J Mol Biol 340:965-979(2004) [PubMed] [Europe PMC] [Abstract]
• DEAD/H-box RNA helicase binding Source: CAFA <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E."
    Callaghan A.J., Aurikko J.P., Ilag L.L., Gunter Grossmann J., Chandran V., Kuhnel K., Poljak L., Carpousis A.J., Robinson C.V., Symmons M.F., Luisi B.F.
    J Mol Biol 340:965-979(2004) [PubMed] [Europe PMC] [Abstract]
• endoribonuclease activity Source: UniProtKB-UniRule
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E."
    Callaghan A.J., Aurikko J.P., Ilag L.L., Gunter Grossmann J., Chandran V., Kuhnel K., Poljak L., Carpousis A.J., Robinson C.V., Symmons M.F., Luisi B.F.
    J Mol Biol 340:965-979(2004) [PubMed] [Europe PMC] [Abstract]
  • Ref.29

    "The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation."
    Koslover D.J., Callaghan A.J., Marcaida M.J., Garman E.F., Martick M., Scott W.G., Luisi B.F.
    Structure 16:1238-1244(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-515 IN COMPLEX WITH RNA AND ZINC IONS, SUBUNIT.
• magnesium ion binding Source: EcoCycInferred from mutant phenotypeⁱ
  • "Altering the divalent metal ion preference of RNase E."
    Thompson K.J., Zong J., Mackie G.A.
    J Bacteriol 197:477-482(2015) [PubMed] [Europe PMC] [Abstract]
• ribonuclease activity Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• ribonuclease E activity Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "The catalytic domain of RNase E shows inherent 3' to 5' directionality in cleavage site selection."
    Feng Y., Vickers T.A., Cohen S.N.
    Proc Natl Acad Sci U S A 99:14746-14751(2002) [PubMed] [Europe PMC] [Abstract]
• RNA binding Source: CAFAInferred from mutant phenotypeⁱ
  • "Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E."
    Callaghan A.J., Aurikko J.P., Ilag L.L., Gunter Grossmann J., Chandran V., Kuhnel K., Poljak L., Carpousis A.J., Robinson C.V., Symmons M.F., Luisi B.F.
    J Mol Biol 340:965-979(2004) [PubMed] [Europe PMC] [Abstract]
• rRNA binding Source: UniProtKB-KW
• tRNA binding Source: UniProtKB-KW
• zinc ion binding Source: UniProtKB-UniRule

GO - Biological processⁱ

• mRNA catabolic process Source: EcoCycInferred from mutant phenotypeⁱ
  • "The Ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli."
    Babitzke P., Kushner S.R.
    Proc Natl Acad Sci U S A 88:1-5(1991) [PubMed] [Europe PMC] [Abstract]
• protein homotetramerization Source: EcoCycInferred from physical interactionⁱ
  • "Quaternary structure and catalytic activity of the Escherichia coli ribonuclease E amino-terminal catalytic domain."
    Callaghan A.J., Grossmann J.G., Redko Y.U., Ilag L.L., Moncrieffe M.C., Symmons M.F., Robinson C.V., McDowall K.J., Luisi B.F.
    Biochemistry 42:13848-13855(2003) [PubMed] [Europe PMC] [Abstract]
• regulation of RNA helicase activity Source: CAFAInferred from mutant phenotypeⁱ
  • "Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E."
    Callaghan A.J., Aurikko J.P., Ilag L.L., Gunter Grossmann J., Chandran V., Kuhnel K., Poljak L., Carpousis A.J., Robinson C.V., Symmons M.F., Luisi B.F.
    J Mol Biol 340:965-979(2004) [PubMed] [Europe PMC] [Abstract]
• RNA catabolic process Source: EcoCycInferred from direct assayⁱ
  • Ref.7

    "RNase E activity is conferred by a single polypeptide: overexpression, purification, and properties of the ams/rne/hmp1 gene product."
    Cormack R.S., Genereaux J.L., Mackie G.A.
    Proc. Natl. Acad. Sci. U.S.A. 90:9006-9010(1993) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 844-1061, CHARACTERIZATION.
• rRNA 5'-end processing Source: EcoCycInferred from mutant phenotypeⁱ
  • Ref.12

    "RNase G (CafA protein) and RNase E are both required for the 5' maturation of 16S ribosomal RNA."
    Li Z., Pandit S., Deutscher M.P.
    EMBO J. 18:2878-2885(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN 16S RRNA MATURATION, DISRUPTION PHENOTYPE.
• rRNA processing Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• tRNA processing Source: EcoCycInferred from mutant phenotypeⁱ
  • Ref.16

    "RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors."
    Li Z., Deutscher M.P.
    RNA 8:97-109(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION IN TRNA MATURATION.

<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

Enzyme and pathway databases

<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 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

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypeⁱ

Mutagenesis

<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

Proteomic databases

<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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• DEAD/H-box RNA helicase binding Source: CAFAInferred from physical interactionⁱ
  • "Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E."
    Callaghan A.J., Aurikko J.P., Ilag L.L., Gunter Grossmann J., Chandran V., Kuhnel K., Poljak L., Carpousis A.J., Robinson C.V., Symmons M.F., Luisi B.F.
    J Mol Biol 340:965-979(2004) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • "Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E."
    Callaghan A.J., Aurikko J.P., Ilag L.L., Gunter Grossmann J., Chandran V., Kuhnel K., Poljak L., Carpousis A.J., Robinson C.V., Symmons M.F., Luisi B.F.
    J Mol Biol 340:965-979(2004) [PubMed] [Europe PMC] [Abstract]
  • Ref.29

    "The crystal structure of the Escherichia coli RNase E apoprotein and a mechanism for RNA degradation."
    Koslover D.J., Callaghan A.J., Marcaida M.J., Garman E.F., Martick M., Scott W.G., Luisi B.F.
    Structure 16:1238-1244(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-515 IN COMPLEX WITH RNA AND ZINC IONS, SUBUNIT.

Protein-protein interaction databases

<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

3D structure databases

Miscellaneous databases

<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

Region

Compositional bias

<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

<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

Family and domain databases

<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.

        10         20         30         40         50
MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE 
        60         70         80         90        100
PSLEAAFVDY GAERHGFLPL KEIAREYFPA NYSAHGRPNI KDVLREGQEV 
       110        120        130        140        150
IVQIDKEERG NKGAALTTFI SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE 
       160        170        180        190        200
LKEALASLEL PEGMGLIVRT AGVGKSAEAL QWDLSFRLKH WEAIKKAAES 
       210        220        230        240        250
RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVLELA RQHIAALGRP 
       260        270        280        290        300
DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT 
       310        320        330        340        350
AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM 
       360        370        380        390        400
TPVRHQRAVE NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS 
       410        420        430        440        450
HHVCPRCSGT GTVRDNESLS LSILRLIEEE ALKENTQEVH AIVPVPIASY 
       460        470        480        490        500
LLNEKRSAVN AIETRQDGVR CVIVPNDQME TPHYHVLRVR KGEETPTLSY 
       510        520        530        540        550
MLPKLHEEAM ALPSEEEFAE RKRPEQPALA TFAMPDVPPA PTPAEPAAPV 
       560        570        580        590        600
VAPAPKAAPA TPAAPAQPGL LSRFFGALKA LFSGGEETKP TEQPAPKAEA 
       610        620        630        640        650
KPERQQDRRK PRQNNRRDRN ERRDTRSERT EGSDNREENR RNRRQAQQQT 
       660        670        680        690        700
AETRESRQQA EVTEKARTAD EQQAPRRERS RRRNDDKRQA QQEAKALNVE 
       710        720        730        740        750
EQSVQETEQE ERVRPVQPRR KQRQLNQKVR YEQSVAEEAV VAPVVEETVA 
       760        770        780        790        800
AEPIVQEAPA PRTELVKVPL PVVAQTAPEQ QEENNADNRD NGGMPRRSRR 
       810        820        830        840        850
SPRHLRVSGQ RRRRYRDERY PTQSPMPLTV ACASPELASG KVWIRYPIVR 
       860        870        880        890        900
PQDVQVEEQR EQEEVHVQPM VTEVPVAAAI EPVVSAPVVE EVAGVVEAPV 
       910        920        930        940        950
QVAEPQPEVV ETTHPEVIAA AVTEQPQVIT ESDVAVAQEV AEQAEPVVEP 
       960        970        980        990       1000
QEETADIEEV VETAEVVVAE PEVVAQPAAP VVAEVAAEVE TVAAVEPEVT 
      1010       1020       1030       1040       1050
VEHNHATAPM TRAPAPEYVP EAPRHSDWQR PTFAFEGKGA AGGHTATHHA 
      1060 
SAAPARPQPV E                                           

<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

Experimental Info

Sequence databases

Genome annotation databases

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<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 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

Documents

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