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0ECEL1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameECEL1
DescriptionEndothelin-converting enzyme-like 1 (ec 3.4.24.-) (xce protein).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0008237 metallopeptidase activity (TAS)
0007218 neuropeptide signaling pathway (TAS)

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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:
Metalloproteases are the most diverse of the four main types of protease.ith more than 30 families identified to date . In these enzymes. divalent cation.sually zinc.ctivates the water molecule. The metal ion is held in place by amino acid ligands.sually three in number. The known metal ligands are His.lu.sp or Lys and at least one other residue is required for catalysis.hich may play an electrophillic role. Of the known metalloproteases.round half contain an HEXXH motif.hich has been shown in crystallographic studies to form part of the metal-binding site . The HEXXH motif is relatively common.ut can be more stringently defined for metalloproteases as abXHEbbHbc.here a is most often valine or threonine and forms part of the S1 subsite in thermolysin and neprilysin. is an uncharged residue.nd c a hydrophobic residue. Proline is never found in this site.ossibly because it would break the helical structure adopted by this motif in metalloproteases .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of metallopeptidases belong to the MEROPS peptidase family M13 (neprilysin family.lan MA(E)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin.he type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH .M13 peptidases are well-studied proteases found in a wide range of organisms including mammals and bacteria. In mammals they participate in processes such as cardiovascular development.lood-pressure regulation.ervous control of respiration.nd regulation of the function of neuropeptides in the central nervous system. In bacteria they may be used for digestion of milk . The family includes eukaryotic and prokaryotic oligopeptidases.s well as some of the proteins responsible for the molecular basis of the blood group antigens e.g. Kell . Neprilysin ().s another member of this group.t is variously known as common acute lymphoblastic leukemia antigen (CALLA).nkephalinase (gp100) and neutral endopeptidase metalloendopeptidase (NEP). It is a plasma membrane-bound mammalian enzyme that is able to digest biologically-active peptides.ncluding enkephalins . The zinc ligands of neprilysin are known and are analogous to those in thermolysin. related peptidase . Neprilysins.ike thermolysin.re inhibited by phosphoramidon.hich appears to selectively inhibit this family in mammals. The enzymes are all oligopeptidases.igesting oligo- and polypeptides.ut not proteins . Neprilysin consists of a short cytoplasmic domain. membrane-spanning region and a large extracellular domain. The cytoplasmic domain contains a conformationally-restrained octapeptide.hich is thought to act as a stop transfer sequence that prevents proteolysis and secretion .
  IPR008753:Peptidase M13
Metalloproteases are the most diverse of the four main types of protease.ith more than 30 families identified to date . In these enzymes. divalent cation.sually zinc.ctivates the water molecule. The metal ion is held in place by amino acid ligands.sually three in number. The known metal ligands are His.lu.sp or Lys and at least one other residue is required for catalysis.hich may play an electrophillic role. Of the known metalloproteases.round half contain an HEXXH motif.hich has been shown in crystallographic studies to form part of the metal-binding site . The HEXXH motif is relatively common.ut can be more stringently defined for metalloproteases as abXHEbbHbc.here a is most often valine or threonine and forms part of the S1 subsite in thermolysin and neprilysin. is an uncharged residue.nd c a hydrophobic residue. Proline is never found in this site.ossibly because it would break the helical structure adopted by this motif in metalloproteases .Peptidases are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry. Families are grouped by their catalytic type.he first character representing the catalytic type: A.spartic; C.ysteine; G.lutamic acid; M.etallo; S.erine; T.hreonine; and U.nknown. A clan that contains families of more than one type is described as being of type P. The serine.hreonine and cysteine peptidases utilise the catalytic part of an amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic.lutamic and metallopeptidases.he nucleophile is an activated water molecule. This group of metallopeptidases belong to the MEROPS peptidase family M13 (neprilysin family.lan MA(E)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin.he type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH .M13 peptidases are well-studied proteases found in a wide range of organisms including mammals and bacteria. In mammals they participate in processes such as cardiovascular development.lood-pressure regulation.ervous control of respiration.nd regulation of the function of neuropeptides in the central nervous system. In bacteria they may be used for digestion of milk . The family includes eukaryotic and prokaryotic oligopeptidases.s well as some of the proteins responsible for the molecular basis of the blood group antigens e.g. Kell . Neprilysin ().s another member of this group.t is variously known as common acute lymphoblastic leukemia antigen (CALLA).nkephalinase (gp100) and neutral endopeptidase metalloendopeptidase (NEP). It is a plasma membrane-bound mammalian enzyme that is able to digest biologically-active peptides.ncluding enkephalins . The zinc ligands of neprilysin are known and are analogous to those in thermolysin. related peptidase . Neprilysins.ike thermolysin.re inhibited by phosphoramidon.hich appears to selectively inhibit this family in mammals. The enzymes are all oligopeptidases.igesting oligo- and polypeptides.ut not proteins . Neprilysin consists of a short cytoplasmic domain. membrane-spanning region and a large extracellular domain. The cytoplasmic domain contains a conformationally-restrained octapeptide.hich is thought to act as a stop transfer sequence that prevents proteolysis and secretion .
  IPR000718:Peptidase M13, neprilysin
IPR008753:Peptidase_M13_N 
Evalue:-177.327896118164 
Location:121-513IPR000718:Peptidase_M13 
Evalue:-76.9208221435547 
Location:571-774
SequencesProtein: ECEL1_HUMAN (775 aa)
mRNA: AB030579 BC050453 NM_004826
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)
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentK01417
  Level 3 annotation:
    
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 143 residues, 233052780-233053206Exon2: 27 residues, 233053352-233053429Exon3: 34 residues, 233053671-233053767Exon4: 24 residues, 233054044-233054110Exon5: 43 residues, 233054459-233054584Exon6: 24 residues, 233054735-233054803Exon7: 19 residues, 233055371-233055423Exon8: 21 residues, 233055503-233055562Exon9: 36 residues, 233055804-233055908Exon10: 27 residues, 233056058-233056133Exon11: 35 residues, 233056369-233056468Exon12: 76 residues, 233056954-233057177Exon13: 43 residues, 233057425-233057550Exon14: 33 residues, 233057754-233057847Exon15: 38 residues, 233057934-233058043Exon16: 25 residues, 233058150-233058221Exon17: 297 residues, 233058821-233059708Exon18: 36 residues, 233060672-233060775Exon19: 2 residues, -Jump to ECEL1_HUMANExon1: 143 residues, 233052780-233053206Exon2: 27 residues, 233053352-233053429Exon3: 34 residues, 233053671-233053767Exon4: 24 residues, 233054044-233054110Exon5: 43 residues, 233054459-233054584Exon6: 24 residues, 233054735-233054803Exon7: 19 residues, 233055371-233055423Exon8: 21 residues, 233055503-233055562Exon9: 36 residues, 233055804-233055908Exon10: 27 residues, 233056058-233056133Exon11: 35 residues, 233056369-233056468Exon12: 76 residues, 233056954-233057177Exon13: 43 residues, 233057425-233057550Exon14: 33 residues, 233057754-233057847Exon15: 39 residues, 233057934-233058045Exon16: 25 residues, 233058152-233058221Exon17: 297 residues, 233058821-233059708Exon18: 38 residues, 233060672-233060782Exon19: 2 residues, -Jump to ECEL1_HUMANExon1: 143 residues, 233052780-233053206Exon2: 27 residues, 233053352-233053429Exon3: 34 residues, 233053671-233053767Exon4: 24 residues, 233054044-233054110Exon5: 43 residues, 233054459-233054584Exon6: 24 residues, 233054735-233054803Exon7: 19 residues, 233055371-233055423Exon8: 21 residues, 233055503-233055562Exon9: 36 residues, 233055804-233055908Exon10: 27 residues, 233056058-233056133Exon11: 35 residues, 233056369-233056468Exon12: 76 residues, 233056954-233057177Exon13: 43 residues, 233057425-233057550Exon14: 33 residues, 233057754-233057847Exon15: 97 residues, 233057934-233058221Exon16: 297 residues, 233058821-233059708Exon17: 36 residues, 233060672-233060775Exon18: 2 residues, -Jump to ECEL1_HUMAN  
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Loci Cluster (Details)Loci: 3220 233099165-233108448 ~-9K 22296(CHRND)(+)Loci: 3221 233112680-233119282 ~-7K 22297(CHRNG)(+)Loci: 4500 233339418-233349519 ~-10K 22308(KCNJ13)(-)Loci: 4499 233052780-233060782 ~-8K 22293(ECEL1)(-)Link out to UCSC