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0VAT1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameVAT1
DescriptionSynaptic vesicle membrane protein vat-1 homolog (ec 1.-.-.-).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Alcohol dehydrogenase () (ADH) catalyzes the reversible oxidation ofalcohols to their corresponding acetaldehyde or ketone with the concomitant reduction of NAD:alcohol + NAD = aldehyde or ketone + NADHCurrently three structurally and catalytically different types of alcoholdehydrogenases are known:Zinc-containing long-chain alcohol dehydrogenases.Insect-type.r short-chain alcohol dehydrogenases.Iron-containing alcohol dehydrogenases.Zinc-containing ADHs .re dimeric or tetrameric enzymes that bind twoatoms of zinc per subunit. One of the zinc atom is essential for catalyticactivity while the other is not. Both zinc atoms are coordinated by eithercysteine or histidine residues; the catalytic zinc is coordinated by twocysteines and one histidine. Zinc-containing ADHs are found in bacteria.ammals.lants.nd in fungi. In many species there is more than one isozyme(for example.umans have at least six isozymes.east have three.tc.). Anumber of other zinc-dependent dehydrogenases are closely related to zincADH and are included in this family.Sorbitol dehydrogenase ()L-threonine 3-dehydrogenase ()Glutathione-dependent formaldehyde dehydrogenase ()Mannitol dehydrogenase () In addition.his family includes NADP-dependent quinone oxidoreductase ().n enzyme found in bacteria (gene qor).n yeast and in mammals where.n somespecies such as rodents.t has been recruited as an eye lens protein and isknown as zeta-crystallin . The sequence of quinone oxidoreductase isdistantly related to that other zinc-containing alcohol dehydrogenases and itlacks the zinc-ligand residues. The torpedo fish and mammalian synaptic vesiclemembrane protein vat-1 is related to qor.This entry represents the cofactor-binding domain of these enzymes.hich is mornally found towards the C-terminus. Structural studies indicate that it forms a classical Rossman fold that reversibly binds NAD(H) .
  IPR013149:Alcohol dehydrogenase, zinc-binding
This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure .
  IPR013154:Alcohol dehydrogenase GroES-like
GroES (chaperonin 10) is an oligomeric molecular chaperone.hich functions in protein folding and possibly in intercellular signalling.eing found on the surface of various prokaryotic and eukaryotic cells.s well as being released from cells. Secreted chaperonins are thought to act as intercellular signals.nteracting with a variety of cell types.ncluding leukocytes.ascular endothelial cells and epithelial cells.s well as activating key cellular activities such as the synthesis of cytokines and adhesion proteins . GroES works as a co-chaperone with GroEL (chaperonin 60) during protein folding. The polypeptide substrate is captured by GroEL.hich bind the co-chaperone GroES and ATP.nd discharges the substrate into a unique microenvironment inside of the chaperone.hich promotes productive folding. After hydrolysis of ATP.he polypeptide is released into solution . GP31 from bacteriophage T4 is functionally equivalent to GroES. GroES folds as a partly opened beta-barrel.The N-terminal domain of alcohol dehydrogenase-like proteins have a GroES-like fold.he C-terminal domain having a classical Rossman-fold . These proteins include.lcohol dehydrogenase.hich contains a zinc-finger subdomain within the GroES-like domain.etose reductase (sorbitol dehydrogenase).ormaldehyde dehydrogenase.uinone oxidoreductase and 2.-dienoyl-CoA reductase.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011032:GroES-like
IPR013149:ADH_zinc_N 
Evalue:-25.6989707946777 
Location:188-347IPR013154:ADH_N 
Evalue:-22.32790184021 
Location:76-157
SequencesProtein: VAT1_HUMAN (393 aa)
mRNA: NM_006373
Local Annotation
Synapse Ontology
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords)
KO assignmentK00540
  Level 3 annotation:
    
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 514 residues, 38420147-38421687Exon2: 82 residues, 38421849-38422091Exon3: 32 residues, 38423383-38423473Exon4: 59 residues, 38423578-38423749Exon5: 71 residues, 38424134-38424342Exon6: 149 residues, 38427478-38427921Exon7: 2 residues, -Jump to VAT1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4288 37562438-37586822 ~-24K 15872(KCNH4)(-)Loci: 4289 37589603-37590996 ~-1K 15873(HCRT)(-)Loci: 3002 37864387-37928122 ~-64K 15882(ATP6V0A1)(+)Loci: 3003 37941476-37949990 ~-9K 15887(NAGLU)(+)Loci: 3004 38064836-38072549 ~-8K 15898(TUBG2)(+)Loci: 3005 38088157-38105358 ~-17K 15903(CNTNAP1)(+)Loci: 4290 38105819-38150574 ~-45K 15904(EZH1)(-)Loci: 3006 38186221-38202605 ~-16K 15907(WNK4)(+)Loci: 4291 38215677-38229807 ~-14K 15912(BECN1)(-)Loci: 3007 38250134-38256248 ~-6K 15916(AOC2)(+)Loci: 3008 38256726-38263664 ~-7K 15917(AOC3)(+)Loci: 4292 38420147-38427921 ~-8K 15927(VAT1)(-)Loci: 4293 38449839-38530657 ~-81K 15931(BRCA1)(-)Loci: 4287 37530523-37560548 ~-30K 15871(RAB5C)(-)Link out to UCSC