SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0MT3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMT3
DescriptionMetallothionein-3 (mt-3) (metallothionein-iii) (mt-iii) (growth inhibitory factor) (gif) (gifb).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008021 synaptic vesicle (ISS)
0016209 antioxidant activity (NAS)
0005507 copper ion binding (TAS)
0008270 zinc ion binding (ISS)
0008283 cell proliferation (TAS)
0006875 metal ion homeostasis (NAS)
0030308 negative regulation of cell growth (ISS)
0050774 negative regulation of dendrite morphogenesis (ISS)
0019430 removal of superoxide radicals (IDA)
0001666 response to hypoxia (IDA)

Warning: fopen(/home/kongl/syndb/www/temp/1416934288.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Metallothioneins (MT) are small proteins that bind heavy metals.uch as zinc.opper.admium.ickel.tc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds . An empirical classification into three classes has been proposed by Fowler and coworkers and Kojima . Members of class I are defined to include polypeptides related in the positions of their cysteines to equine MT-1B.nd include mammalian MTs as well as from crustaceans and molluscs. Class II groups MTs from a variety of species.ncluding sea urchins.ungi.nsects and cyanobacteria. Class III MTs are atypical polypeptides composed of gamma-glutamylcysteinyl units .This original classification system has been found to be limited.n the sense that it does not allow clear differentiation of patterns of structural similarities.ither between or within classes. Consequently.ll class I and class II MTs (the proteinaceous sequences) have now been grouped into families of phylogenetically-related and thus alignable sequences. This system subdivides the MT superfamily into families.ubfamilies.ubgroups.nd isolated isoforms and alleles. The metallothionein superfamily comprises all polypeptides that resemble equine renal metallothionein in several respects : e.g..ow molecular weight; high metal content; amino acid composition with high Cys and low aromatic residue content; unique sequence with characteristic distribution of cysteines.nd spectroscopic manifestations indicative of metal thiolate clusters. A MT family subsumes MTs that share particular sequence-specific features and are thought to be evolutionarily related. The inclusion of a MT within a family presupposes that its amino acid sequence is alignable with that of all members. Fifteen MT families [http://www.unizh.ch/~mtpage/MT.html] have been characterised.ach family being identified by its number and its taxonomic range: e.g..amily 1: vertebrate MTs. This entry is a superfamily of metallothioneins.ontaining 3 families.
  IPR003019:Metallothionein superfamily
Metallothioneins (MT) are small proteins that bind heavy metals.uch as zinc.opper.admium.ickel.tc. They have a high content of cysteine residues that bind the metal ions through clusters of thiolate bonds . An empirical classification into three classes has been proposed by Fowler and coworkers and Kojima . Members of class I are defined to include polypeptides related in the positions of their cysteines to equine MT-1B.nd include mammalian MTs as well as from crustaceans and molluscs. Class II groups MTs from a variety of species.ncluding sea urchins.ungi.nsects and cyanobacteria. Class III MTs are atypical polypeptides composed of gamma-glutamylcysteinyl units .This original classification system has been found to be limited.n the sense that it does not allow clear differentiation of patterns of structural similarities.ither between or within classes. Consequently.ll class I and class II MTs (the proteinaceous sequences) have now been grouped into families of phylogenetically-related and thus alignable sequences. This system subdivides the MT superfamily into families.ubfamilies.ubgroups.nd isolated isoforms and alleles. The metallothionein superfamily comprises all polypeptides that resemble equine renal metallothionein in several respects : e.g..ow molecular weight; high metal content; amino acid composition with high Cys and low aromatic residue content; unique sequence with characteristic distribution of cysteines.nd spectroscopic manifestations indicative of metal thiolate clusters. A MT family subsumes MTs that share particular sequence-specific features and are thought to be evolutionarily related. The inclusion of a MT within a family presupposes that its amino acid sequence is alignable with that of all members. Fifteen MT families [http://www.unizh.ch/~mtpage/MT.html] have been characterised.ach family being identified by its number and its taxonomic range: e.g..amily 1: vertebrate MTs. The members of family 1 are recognised by the sequence pattern K-x(1.)-C-C-x-C-C-P-x(2)-C located at the beginning of the third exon. The taxonomic range of the members extends to vertebrates. Known characteristics: 60 to 68 AAs; 20 Cys (21 in one case).9 of them are totally conserved; the protein sequence is divided into two structural domains.ontaining 9 and 11 Cys all binding 3 and 4 bivalent metal ions.espectively. The gene is composed of 3 exons. introns and the splicing sites are conserved. Family 1 includes subfamilies: m1.2.3.4...1.2..a..ll of them hit the same InterPro entry.
  IPR000006:Vertebrate metallothionein
Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions; they fall into several subgroups according to the nature of their iron-sulphur cluster(s) . One group.riginally found in bacteria.as been termed "bacterial-type".n which the active centre is a 4Fe-4S cluster. 4Fe-4S ferredoxins may in turn be subdivided into further groups.ased on their sequence properties. Most contain at least one conserved domain.ncluding four Cys residues that bind to a 4Fe-4S centre. During the evolution of bacterial-type ferredoxins.ntrasequence gene duplication.ransposition and fusion events occured.esulting in the appearance of proteins with multiple iron-sulphur centres: e.g. dicluster- type (2[4Fe-4S]) and polyferredoxins.ron-sulphur subunits of bacterial succinate dehydrogenase/fumarate reductase.ormate hydrogenlyase and formate dehydrogenase complexes.yruvate-flavodoxin oxidoreductase.ADH:ubiquinone reductase and others. In some bacterial ferredoxins.ne of the duplicated domains has lost one or more of the four conserved Cys residues. These domains have either lost their iron-sulphur binding property.r bind to a 3Fe-4S centre instead of a 4Fe-4S centre. 3D structures are now known both for a number of monocluster-type and dicluster-type 4Fe-4S ferredoxins.CAUTION: PRINTS signature in the current entry is known to miss protein matches and should be updated in the near future.
  IPR001450:4Fe-4S ferredoxin, iron-sulfur binding
A group of proteins containing 8 characteristically-spaced cysteine residues.hich are involved in disulphide bond formation.ave been termed 4-disulphide core proteins . While the pattern of conserved cysteines suggests that the sequences may adopt a similar fold.he overall degree of sequence similarity is low (e.g. a few Pro and Gly residues are reasonably well conserved.s is the polar/acidic nature of residues between the third and fourth Cys.ut otherwise there is little sequence conservation). The group of sequences that share this pattern include whey acidic protein (WAP) ; WDNM1 protein (which is involved in the metastatic potential of adenocarcinomas in rats ; Kallmann syndrome protein ; and caltrin-like protein II from guinea pig (which inhibits calcium transport into spermatozoa); and elafin a serine elastase inhibitor.hich belongs to MEROPS inhibitor family I17. Elafin has no activity against plasmin.rypsin.lpha-chymotrypsin.nd cathepsin G .
  IPR008197:Whey acidic protein, core region
IPR003019:Metallothio 
Evalue:-20.2006587982178 
Location:1-68
SequencesProtein: MT3_HUMAN (68 aa)
mRNA: NM_005954
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 assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 90 residues, 55180767-55181034Exon2: 24 residues, 55181282-55181348Exon3: 84 residues, 55182252-55182500Exon4: 2 residues, -Jump to MT3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2942 55321607-55436177 ~-115K 14148(NUP93)(+)Loci: 2941 55180767-55182500 ~-2K 14132(MT3)(+)Link out to UCSC