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0TEFF2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTMEFF2
DescriptionTransmembrane protein with egf-like and two follistatin-like domains 2 precursor (transmembrane protein containing epidermal growth factor and follistatin domains) (tomoregulin) (tr) (hyperplastic polyposis protein 1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (NAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors.espectively. In many cases they are synthesised as part of a larger precursor protein.ither as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. This family of Kazal inhibitors.elongs to MEROPS inhibitor family I1.lan IA. They inhibit serine peptidases of the S1 family () . The members are primarily metazoan.ut includes exceptions in the alveolata (apicomplexa).tramenopiles.igher plants and bacteria.Kazal inhibitors.hich inhibit a number of serine proteases (such astrypsin and elastase).elong to family of proteins that includespancreatic secretory trypsin inhibitor; avian ovomucoid; acrosin inhibitor;and elastase inhibitor. These proteins contain between 1 and 7 Kazal-typeinhibitor repeats . The structure of the Kazal repeat includes a large quantity of extended chain. short alpha-helices and a 3-stranded anti-parallel beta sheet .The inhibitor makes 11 contacts with its enzyme substrate: unusually. of these important residues are hypervariable . Altering the enzyme-contact residues.nd especially that of the active site bond.ffects the the strength of inhibition and specificity of the inhibitor for particular serine proteases . The presence of this Pfam domain is usually indicative of serine protease inhibitors.owever.azal-like domains are also seen in the extracellular part of agrins which are not known to be proteinase inhibitors.
  IPR002350:Proteinase inhibitor I1, Kazal
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
IPR002350:KAZAL 
Evalue:-13.397940008672 
Location:90-135IPR002350:KAZAL 
Evalue:-12.2076083105017 
Location:181-227IPR006209:EGF 
Evalue:-5.85387182235718 
Location:265-300
SequencesProtein: TEFF2_HUMAN (374 aa)
mRNA: AL157430 NM_016192
Local Annotation
Synapse Ontology
introduce the substructure of the synapse and the location where the molecule can be seen. It will contain all the constructive special organelle and molecule we known.
sdb:0001 Structure/Biochemistry of synapse  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 473 residues, 192522017-192523435Exon2: 55 residues, 192526649-192526808Exon3: 43 residues, 192529225-192529349Exon4: 22 residues, 192571232-192571292Exon5: 51 residues, 192572030-192572179Exon6: 34 residues, 192630649-192630746Exon7: 11 residues, 192752638-192752665Exon8: 45 residues, 192757324-192757454Exon9: 38 residues, 192764850-192764960Exon10: 190 residues, 192767323-192767887Exon11: 2 residues, -Jump to TEFF2_HUMANExon1: 129 residues, 192522993-192523378Exon2: 55 residues, 192526649-192526808Exon3: 43 residues, 192529225-192529349Exon4: 22 residues, 192571232-192571292Exon5: 51 residues, 192572030-192572179Exon6: 34 residues, 192630649-192630746Exon7: 11 residues, 192752638-192752665Exon8: 45 residues, 192757324-192757454Exon9: 38 residues, 192764850-192764960Exon10: 190 residues, 192767323-192767889Exon11: 2 residues, -Jump to TEFF2_HUMAN  
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