2-hydroxyacyl-CoA lyase 1

<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

<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

• 2-hydroxy-3-methylhexadecanoyl-CoA

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  • See the description of this molecule in ChEBI.

  = 2-methylpentadecanal

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  + formyl-CoA

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  2 Publications

  Manual assertion based on experiment inⁱ

  • Ref.1

    "Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine hydrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids."
    Foulon V., Antonenkov V.D., Croes K., Waelkens E., Mannaerts G.P., Van Veldhoven P.P., Casteels M.
    Proc. Natl. Acad. Sci. U.S.A. 96:10039-10044(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION.
  • Ref.7

    "Role of thiamine pyrophosphate in oligomerisation, functioning and import of peroxisomal 2-hydroxyacyl-CoA lyase."
    Fraccascia P., Casteels M., De Schryver E., Van Veldhoven P.P.
    Biochim. Biophys. Acta 1814:1226-1233(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-455 AND SER-456, SUBUNIT, CATALYTIC ACTIVITY.
  EC:4.1.2.n2
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  2 Publications

  Manual assertion based on experiment inⁱ

  • Ref.1

    "Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine hydrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids."
    Foulon V., Antonenkov V.D., Croes K., Waelkens E., Mannaerts G.P., Van Veldhoven P.P., Casteels M.
    Proc. Natl. Acad. Sci. U.S.A. 96:10039-10044(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION.
  • Ref.7

    "Role of thiamine pyrophosphate in oligomerisation, functioning and import of peroxisomal 2-hydroxyacyl-CoA lyase."
    Fraccascia P., Casteels M., De Schryver E., Van Veldhoven P.P.
    Biochim. Biophys. Acta 1814:1226-1233(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-455 AND SER-456, SUBUNIT, CATALYTIC ACTIVITY.
  This reaction proceeds in the forward

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  1 Publication

  <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromⁱ

  • Ref.1

    "Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine hydrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids."
    Foulon V., Antonenkov V.D., Croes K., Waelkens E., Mannaerts G.P., Van Veldhoven P.P., Casteels M.
    Proc. Natl. Acad. Sci. U.S.A. 96:10039-10044(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION.

  direction.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  2-hydroxy-3-methylhexadecanoyl-CoA

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  zoom

  =

  2-methylpentadecanal

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  zoom

  +

  formyl-CoA

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  zoom
• 2-hydroxyoctadecanoyl-CoA

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  = formyl-CoA

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  • See the description of this molecule in ChEBI.

  + heptadecanal

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  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.13

    "Phytosphingosine degradation pathway includes fatty acid alpha-oxidation reactions in the endoplasmic reticulum."
    Kitamura T., Seki N., Kihara A.
    Proc. Natl. Acad. Sci. U.S.A. 114:E2616-E2623(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
  This reaction proceeds in the forward

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  • See the description of this reaction in Rhea.

  1 Publication

  Manual assertion inferred by curator fromⁱ

  • Ref.13

    "Phytosphingosine degradation pathway includes fatty acid alpha-oxidation reactions in the endoplasmic reticulum."
    Kitamura T., Seki N., Kihara A.
    Proc. Natl. Acad. Sci. U.S.A. 114:E2616-E2623(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.

  direction.
  Source: Rhea

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  • See the description of this reaction in Rhea.

  . Show »« Hide
  2-hydroxyoctadecanoyl-CoA

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  zoom

  =

  formyl-CoA

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  zoom

  +

  heptadecanal

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  zoom
• 2-hydroxyphytanoyl-CoA

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  = 2,6,10,14-tetramethylpentadecanal

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  • See the description of this molecule in ChEBI.

  + formyl-CoA

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  • See the description of this molecule in ChEBI.

  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.13

    "Phytosphingosine degradation pathway includes fatty acid alpha-oxidation reactions in the endoplasmic reticulum."
    Kitamura T., Seki N., Kihara A.
    Proc. Natl. Acad. Sci. U.S.A. 114:E2616-E2623(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
  EC:4.1.2.n2
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.13

    "Phytosphingosine degradation pathway includes fatty acid alpha-oxidation reactions in the endoplasmic reticulum."
    Kitamura T., Seki N., Kihara A.
    Proc. Natl. Acad. Sci. U.S.A. 114:E2616-E2623(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
  This reaction proceeds in the forward

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  1 Publication

  Manual assertion inferred by curator fromⁱ

  • Ref.13

    "Phytosphingosine degradation pathway includes fatty acid alpha-oxidation reactions in the endoplasmic reticulum."
    Kitamura T., Seki N., Kihara A.
    Proc. Natl. Acad. Sci. U.S.A. 114:E2616-E2623(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.

  direction.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  2-hydroxyphytanoyl-CoA

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  • See the description of this molecule in ChEBI.

  zoom

  =

  2,6,10,14-tetramethylpentadecanal

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  zoom

  +

  formyl-CoA

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  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

<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

• Mg²⁺
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  • See the description of this molecule in ChEBI.
  By similarity

  Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:Q8CHM7 (HACL1_RAT)
  Note: Binds 1 Mg²⁺ ion per subunit.By similarity

  Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:Q8CHM7 (HACL1_RAT)
• thiamine diphosphate
  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.
  By similarity

  Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:Q8CHM7 (HACL1_RAT)
  Note: Binds 1 thiamine pyrophosphate per subunit.By similarity

  Manual assertion inferred from sequence similarity toⁱ

  • UniProtKB:Q8CHM7 (HACL1_RAT)

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

• carbon-carbon lyase activity Source: UniProtKB <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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Breakdown of 2-hydroxylated straight chain fatty acids via peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the alpha-oxidation of straight chain fatty acids."
    Foulon V., Sniekers M., Huysmans E., Asselberghs S., Mahieu V., Mannaerts G.P., Van Veldhoven P.P., Casteels M.
    J. Biol. Chem. 280:9802-9812(2005) [PubMed] [Europe PMC] [Abstract]
  • Ref.7

    "Role of thiamine pyrophosphate in oligomerisation, functioning and import of peroxisomal 2-hydroxyacyl-CoA lyase."
    Fraccascia P., Casteels M., De Schryver E., Van Veldhoven P.P.
    Biochim. Biophys. Acta 1814:1226-1233(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-455 AND SER-456, SUBUNIT, CATALYTIC ACTIVITY.
• cofactor binding Source: UniProtKBInferred from direct assayⁱ
  • "Breakdown of 2-hydroxylated straight chain fatty acids via peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the alpha-oxidation of straight chain fatty acids."
    Foulon V., Sniekers M., Huysmans E., Asselberghs S., Mahieu V., Mannaerts G.P., Van Veldhoven P.P., Casteels M.
    J. Biol. Chem. 280:9802-9812(2005) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKB <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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.7

    "Role of thiamine pyrophosphate in oligomerisation, functioning and import of peroxisomal 2-hydroxyacyl-CoA lyase."
    Fraccascia P., Casteels M., De Schryver E., Van Veldhoven P.P.
    Biochim. Biophys. Acta 1814:1226-1233(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-455 AND SER-456, SUBUNIT, CATALYTIC ACTIVITY.
• magnesium ion binding Source: InterPro
• thiamine pyrophosphate binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "Role of thiamine pyrophosphate in oligomerisation, functioning and import of peroxisomal 2-hydroxyacyl-CoA lyase."
    Fraccascia P., Casteels M., De Schryver E., Van Veldhoven P.P.
    Biochim. Biophys. Acta 1814:1226-1233(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-455 AND SER-456, SUBUNIT, CATALYTIC ACTIVITY.

GO - Biological processⁱ

• fatty acid alpha-oxidation Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "Role of thiamine pyrophosphate in oligomerisation, functioning and import of peroxisomal 2-hydroxyacyl-CoA lyase."
    Fraccascia P., Casteels M., De Schryver E., Van Veldhoven P.P.
    Biochim. Biophys. Acta 1814:1226-1233(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-455 AND SER-456, SUBUNIT, CATALYTIC ACTIVITY.
  • Ref.13

    "Phytosphingosine degradation pathway includes fatty acid alpha-oxidation reactions in the endoplasmic reticulum."
    Kitamura T., Seki N., Kihara A.
    Proc. Natl. Acad. Sci. U.S.A. 114:E2616-E2623(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
• fatty acid metabolic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.13

    "Phytosphingosine degradation pathway includes fatty acid alpha-oxidation reactions in the endoplasmic reticulum."
    Kitamura T., Seki N., Kihara A.
    Proc. Natl. Acad. Sci. U.S.A. 114:E2616-E2623(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
• methyl-branched fatty acid metabolic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "Role of thiamine pyrophosphate in oligomerisation, functioning and import of peroxisomal 2-hydroxyacyl-CoA lyase."
    Fraccascia P., Casteels M., De Schryver E., Van Veldhoven P.P.
    Biochim. Biophys. Acta 1814:1226-1233(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-455 AND SER-456, SUBUNIT, CATALYTIC ACTIVITY.
  • Ref.13

    "Phytosphingosine degradation pathway includes fatty acid alpha-oxidation reactions in the endoplasmic reticulum."
    Kitamura T., Seki N., Kihara A.
    Proc. Natl. Acad. Sci. U.S.A. 114:E2616-E2623(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
• phytanic acid metabolic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.13

    "Phytosphingosine degradation pathway includes fatty acid alpha-oxidation reactions in the endoplasmic reticulum."
    Kitamura T., Seki N., Kihara A.
    Proc. Natl. Acad. Sci. U.S.A. 114:E2616-E2623(2017) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY.
• protein targeting to peroxisome Source: UniProtKB <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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.1

    "Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine hydrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during alpha-oxidation of 3-methyl-branched fatty acids."
    Foulon V., Antonenkov V.D., Croes K., Waelkens E., Mannaerts G.P., Van Veldhoven P.P., Casteels M.
    Proc. Natl. Acad. Sci. U.S.A. 96:10039-10044(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION.

<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

Chemistry 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

Organism-specific databases

<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

<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

Organism-specific databases

Miscellaneous databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific 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%27">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

• identical protein binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.7

    "Role of thiamine pyrophosphate in oligomerisation, functioning and import of peroxisomal 2-hydroxyacyl-CoA lyase."
    Fraccascia P., Casteels M., De Schryver E., Van Veldhoven P.P.
    Biochim. Biophys. Acta 1814:1226-1233(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-455 AND SER-456, SUBUNIT, CATALYTIC ACTIVITY.

Protein-protein interaction databases

Miscellaneous 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

3D structure 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

Region

Motif

<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>Sequences (4+)ⁱ

<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.

This entry has 4 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MPDSNFAERS EEQVSGAKVI AQALKTQDVE YIFGIVGIPV TEIAIAAQQL 
        60         70         80         90        100
GIKYIGMRNE QAACYAASAI GYLTSRPGVC LVVSGPGLIH ALGGMANANM 
       110        120        130        140        150
NCWPLLVIGG SSERNQETMG AFQEFPQVEA CRLYTKFSAR PSSIEAIPFV 
       160        170        180        190        200
IEKAVRSSIY GRPGACYVDI PADFVNLQVN VNSIKYMERC MSPPISMAET 
       210        220        230        240        250
SAVCTAASVI RNAKQPLLII GKGAAYAHAE ESIKKLVEQY KLPFLPTPMG 
       260        270        280        290        300
KGVVPDNHPY CVGAARSRAL QFADVIVLFG ARLNWILHFG LPPRYQPDVK 
       310        320        330        340        350
FIQVDICAEE LGNNVKPAVT LLGNIHAVTK QLLEELDKTP WQYPPESKWW 
       360        370        380        390        400
KTLREKMKSN EAASKELASK KSLPMNYYTV FYHVQEQLPR DCFVVSEGAN 
       410        420        430        440        450
TMDIGRTVLQ NYLPRHRLDA GTFGTMGVGL GFAIAAAVVA KDRSPGQWII 
       460        470        480        490        500
CVEGDSAFGF SGMEVETICR YNLPIILLVV NNNGIYQGFD TDTWKEMLKF 
       510        520        530        540        550
QDATAVVPPM CLLPNSHYEQ VMTAFGGKGY FVQTPEELQK SLRQSLADTT 
       560        570 
KPSLINIMIE PQATRKAQDF HWLTRSNM                         

        10         20         30         40         50
MPDSNFAERS EEQVSGAKVI AQALKTQDVE YIFGIVGIPV TEIAIAAQQL 
        60         70         80         90        100
GIKYIGMRNE QAACYAASAI GYLTSRPLLV IGGSSERNQE TMGAFQEFPQ 
       110        120        130        140        150
VEACRLYTKF SARPSSIEAI PFVIEKAVRS SIYGRPGACY VDIPADFVNL 
       160        170        180        190        200
QVNVNSIKYM ERCMSPPISM AETSAVCTAA SVIRNAKQPL LIIGKGAAYA 
       210        220        230        240        250
HAEESIKKLV EQYKLPFLPT PMGKGVVPDN HPYCVGAARS RALQFADVIV 
       260        270        280        290        300
LFGARLNWIL HFGLPPRYQP DVKFIQVDIC AEELGNNVKP AVTLLGNIHA 
       310        320        330        340        350
VTKQLLEELD KTPWQYPPES KWWKTLREKM KSNEAASKEL ASKKSLPMNY 
       360        370        380        390        400
YTVFYHVQEQ LPRDCFVVSE GANTMDIGRT VLQNYLPRHR LDAGTFGTMG 
       410        420        430        440        450
VGLGFAIAAA VVAKDRSPGQ WIICVEGDSA FGFSGMEVET ICRYNLPIIL 
       460        470        480        490        500
LVVNNNGIYQ GFDTDTWKEM LKFQDATAVV PPMCLLPNSH YEQVMTAFGG 
       510        520        530        540        550
KGYFVQTPEE LQKSLRQSLA DTTKPSLINI MIEPQATRKA QDFHWLTRSN 

M                                                      

        10         20         30         40         50
MPDSNFAERS EEQVSGAKVI AQALKTQDVE YIFGIVGIPV TEIAIAAQQL 
        60         70         80         90        100
GIKYIGMRNE QAACYAASAI GYLTSRPGVC LVVSGPGLIH ALGGMANANM 
       110        120        130        140        150
NCWPLLVIGG SSERNQETMG AFQEFPQAVR SSIYGRPGAC YVDIPADFVN 
       160        170        180        190        200
LQVNVNSIKY MERCMSPPIS MAETSAVCTA ASVIRNAKQP LLIIGKGAAY 
       210        220        230        240        250
AHAEESIKKL VEQYKLPFLP TPMGKGVVPD NHPYCVGAAR SRALQFADVI 
       260        270        280        290        300
VLFGARLNWI LHFGLPPRYQ PDVKFIQVDI CAEELGNNVK PAVTLLGNIH 
       310        320        330        340        350
AVTKQELASK KSLPMNYYTV FYHVQEQLPR DCFVVSEGAN TMDIGRTVLQ 
       360        370        380        390        400
NYLPRHRLDA GTFGTMGVGL GFAIAAAVVA KDRSPGQWII CVEGDSAFGF 
       410        420        430        440        450
SGMEVETICR YNLPIILLVV NNNGIYQGFD TDTWKEMLKF QDATAVVPPM 
       460        470        480        490        500
CLLPNSHYEQ VMTAFGGKGY FVQTPEELQK SLRQSLADTT KPSLINIMIE 
       510 
PQATRKAQDF HWLTRSNM                                    

        10         20         30         40         50
MPDSNFAERS EEQVSGAKVI AQALKTQDVE YIFGIVGIPV TEIAIAAQQL 
        60         70         80         90        100
GIKYIGMRNE QAACYAASAI GYLTSRPGVC LVVSGPGLIH ALGGMANANM 
       110        120        130        140        150
NCWYMERCMS PPISMAETSA VCTAASVIRN AKQPLLIIGK GAAYAHAEES 
       160        170        180        190        200
IKKLVEQYKL PFLPTPMGKG VVPDNHPYCV GAARSRALQF ADVIVLFGAR 
       210        220        230        240        250
LNWILHFGLP PRYQPDVKFI QVDICAEELG NNVKPAVTLL GNIHAVTKQL 
       260        270        280        290        300
LEELDKTPWQ YPPESKWWKT LREKMKSNEA ASKELASKKS LPMNYYTVFY 
       310        320        330        340        350
HVQEQLPRDC FVVSEGANTM DIGRTVLQNY LPRHRLDAGT FGTMGVGLGF 
       360        370        380        390        400
AIAAAVVAKD RSPGQWIICV EGDSAFGFSG MEVETICRYN LPIILLVVNN 
       410        420        430        440        450
NGIYQGFDTD TWKEMLKFQD ATAVVPPMCL LPNSHYEQVM TAFGGKGYFV 
       460        470        480        490 
QTPEELQKSL RQSLADTTKP SLINIMIEPQ ATRKAQDFHW LTRSNM     

<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

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression 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. PATHWAY comments
   Index of metabolic and biosynthesis pathways
2. SIMILARITY comments
   Index of protein domains and families
3. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
4. Human chromosome 3
   Human chromosome 3: entries, gene names and cross-references to MIM