Vesicle-fusing ATPase

<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

• ATP

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  • See the description of this molecule in ChEBI.

  + H₂O

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  • See the description of this molecule in ChEBI.

  = ADP

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  + H⁺

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  • See the description of this molecule in ChEBI.

  + phosphate

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  EC:3.6.4.6
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  • See the description of this EC number in ENZYME.
  Source: Rhea

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  • See the description of this reaction in Rhea.

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  ATP

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

  

  +

  H₂O

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

  

  =

  ADP

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

  

  +

  H⁺

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

  

  +

  phosphate

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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

Sites

Regions

<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

• ATPase activity Source: MGI <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
  • "Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation."
    Widberg C.H., Bryant N.J., Girotti M., Rea S., James D.E.
    J. Biol. Chem. 278:35093-35101(2003) [PubMed] [Europe PMC] [Abstract]
• ATP binding Source: UniProtKB-KW
• ATP-dependent protein binding Source: MGI
• D1 dopamine receptor binding Source: MGI
• ionotropic glutamate receptor binding Source: MGI
• metal ion binding Source: UniProtKB-KW
• PDZ domain binding Source: MGI
• protein-containing complex binding Source: ParkinsonsUK-UCL
• protein C-terminus binding Source: MGI
• protein kinase binding Source: ParkinsonsUK-UCL <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
  • "LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool."
    Piccoli G., Condliffe S.B., Bauer M., Giesert F., Boldt K., De Astis S., Meixner A., Sarioglu H., Vogt-Weisenhorn D.M., Wurst W., Gloeckner C.J., Matteoli M., Sala C., Ueffing M.
    J Neurosci 31:2225-2237(2011) [PubMed] [Europe PMC] [Abstract]
• Rab GTPase binding Source: MGI
• SNARE binding Source: ParkinsonsUK-UCL
• syntaxin-1 binding Source: ParkinsonsUK-UCL <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
  • "LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool."
    Piccoli G., Condliffe S.B., Bauer M., Giesert F., Boldt K., De Astis S., Meixner A., Sarioglu H., Vogt-Weisenhorn D.M., Wurst W., Gloeckner C.J., Matteoli M., Sala C., Ueffing M.
    J Neurosci 31:2225-2237(2011) [PubMed] [Europe PMC] [Abstract]
• syntaxin binding Source: MGIInferred from direct assayⁱ
  • "The gene for soluble N-ethylmaleimide sensitive factor attachment protein alpha is mutated in hydrocephaly with hop gait (hyh) mice."
    Hong H.K., Chakravarti A., Takahashi J.S.
    Proc Natl Acad Sci U S A 101:1748-1753(2004) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• Golgi to plasma membrane protein transport 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%2Dgo%2Devidence%2Dcodes#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]
• Golgi vesicle docking 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]
• intracellular protein transport Source: MGI
• intra-Golgi vesicle-mediated transport 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]
• positive regulation of protein catabolic process Source: MGI
• positive regulation of receptor recycling Source: MGI
• potassium ion transport Source: MGIInferred from direct assayⁱ
  • Ref.1

    "Identification of a novel mammalian member of the NSF/CDC48p/Pas1p/TBP-1 family through heterologous expression in yeast."
    Perier F., Coulter K.L., Liang H., Radeke C.M., Gaber R.F., Vandenberg C.A.
    FEBS Lett. 351:286-290(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• protein-containing complex disassembly Source: MGI
• protein transport Source: MGI
• regulation of exocytosis Source: MGI
• regulation of receptor internalization Source: MGI
• SNARE complex disassembly Source: ParkinsonsUK-UCL
• vesicle-mediated transport Source: MGI

<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

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

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Keywords - PTMⁱ

Proteomic databases

2D gel 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

Gene expression 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

• ATP-dependent protein binding Source: MGI
• D1 dopamine receptor binding Source: MGI
• ionotropic glutamate receptor binding Source: MGI
• PDZ domain binding Source: MGI
• protein C-terminus binding Source: MGI
• protein kinase binding Source: ParkinsonsUK-UCLInferred from physical interactionⁱ
  • "LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool."
    Piccoli G., Condliffe S.B., Bauer M., Giesert F., Boldt K., De Astis S., Meixner A., Sarioglu H., Vogt-Weisenhorn D.M., Wurst W., Gloeckner C.J., Matteoli M., Sala C., Ueffing M.
    J Neurosci 31:2225-2237(2011) [PubMed] [Europe PMC] [Abstract]
• Rab GTPase binding Source: MGI
• SNARE binding Source: ParkinsonsUK-UCL
• syntaxin-1 binding Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "LRRK2 controls synaptic vesicle storage and mobilization within the recycling pool."
    Piccoli G., Condliffe S.B., Bauer M., Giesert F., Boldt K., De Astis S., Meixner A., Sarioglu H., Vogt-Weisenhorn D.M., Wurst W., Gloeckner C.J., Matteoli M., Sala C., Ueffing M.
    J Neurosci 31:2225-2237(2011) [PubMed] [Europe PMC] [Abstract]
• syntaxin binding Source: MGIInferred from direct assayⁱ
  • "The gene for soluble N-ethylmaleimide sensitive factor attachment protein alpha is mutated in hydrocephaly with hop gait (hyh) mice."
    Hong H.K., Chakravarti A., Takahashi J.S.
    Proc Natl Acad Sci U S A 101:1748-1753(2004) [PubMed] [Europe PMC] [Abstract]

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

<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

Keywords - Domainⁱ

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>Sequence (1+)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 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MAGRTMQAAR CPTDELSLSN CAVVNEKDFQ SGQHVMVRTS PNHKYIFTLR 
        60         70         80         90        100
THPSVVPGCI AFSLPQRKWA GLSIGQDIEV ALYSFDKAKQ CIGTMTIEID 
       110        120        130        140        150
FLQKKNIDSN PYDTDKMAAE FIQQFNNQAF SVGQQLVFSF NDKLFGLLVK 
       160        170        180        190        200
DIEAMDPSIL KGEPASGKRQ KIEVGLVVGN SQVAFEKAEN SSLNLIGKAK 
       210        220        230        240        250
TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF PPEIVEQMGC 
       260        270        280        290        300
KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA 
       310        320        330        340        350
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV 
       360        370        380        390        400
VNQLLSKIDG VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE 
       410        420        430        440        450
KGRLQILHIH TARMRGHQLL SADVDIKELA VETKNFSGAE LEGLVRAAQS 
       460        470        480        490        500
TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF LASLENDIKP AFGTNQEDYA 
       510        520        530        540        550
SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL LEGPPHSGKT 
       560        570        580        590        600
ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV 
       610        620        630        640        650
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD 
       660        670        680        690        700
VLQEMEMLNA FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG 
       710        720        730        740 
KKVWIGIKKL LMLIEMSLQM DPEYRVRKFL ALMREEGASP LDFD       

<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

PTM databases

2D gel 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. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. SIMILARITY comments
   Index of protein domains and families