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0GCP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameOSGEP
DescriptionProbable o-sialoglycoprotein endopeptidase (ec 3.4.24.57) (hosgep).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
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 MEROPS peptidase family M22 (clan MK). The type example being O-sialoglycoprotein endopeptidase from Pasteurella haemolytica.O-Sialoglycoprotein endopeptidase is secreted by the bacterium Mannheimia haemolytica and digests only proteins that are heavily sialylated.nparticular those with sialylated serine and threonine residues .Substrate proteins include glycophorin A and leukocyte surface antigensCD34.D43.D44 and CD45 . Removal of glycosylation.y treatmentwith neuraminidase.ompletely negates susceptibility to O-sialoglycoproteinendopeptidase digestion .Sequence similarity searches have revealed other members of the M22 family.rom yeast.ycobacterium.aemophilus influenzae and the cyanobacteriumSynechocystis . The zinc-binding and catalytic residues of this familyhave not been determined.lthough the motif HMEGH may be a zinc-bindingregion .
  IPR000905:Peptidase M22, glycoprotease
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 belongs to MEROPS peptidase family M22 (clan MK). The Pasteurella haemolytica secreted O-sialoglycoprotein endopeptidase Gcp (glycoprotease; ) cleaves only proteins that are heavily sialylated.n particular those with sialylated serine and threonine residues . It does not cleave unglycosylated proteins.esialylated glycoproteins or glycoproteins that are only N-glycosylated.In some organisms.he O-sialoglycoprotein endopeptidase domain is fused to the serine/threonine protein kinase domain STYKS ().
  IPR009180:Peptidase M22, O-sialoglycoprotein endopeptidase
IPR000905:Peptidase_M22 
Evalue:-64.5376052856445 
Location:23-301IPR000905:OSIALOPTASE 
Evalue:0 
Location:5-18
SequencesProtein: GCP_HUMAN (335 aa)
mRNA: NM_017807
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK01409
  Level 3 annotation:
    O-sialoglycoprotein endopeptidase
  Level 2 annotation:
    Protein folding and associated processing
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 75 residues, 19985056-19985278Exon2: 35 residues, 19985420-19985519Exon3: 27 residues, 19985613-19985689Exon4: 32 residues, 19985902-19985993Exon5: 24 residues, 19986104-19986170Exon6: 28 residues, 19986731-19986810Exon7: 18 residues, 19986962-19987012Exon8: 34 residues, 19987169-19987265Exon9: 60 residues, 19989972-19990148Exon10: 42 residues, 19990327-19990447Exon11: 159 residues, 19992567-19993038Exon12: 2 residues, -Jump to GCP_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2822 19598043-19598982 ~-1K 10739(OR4L1)(+)Loci: 4110 19849367-19871297 ~-22K 10743(CCNB1IP1)(-)Loci: 4111 19905765-19951420 ~-46K 10749(TEP1)(-)Loci: 4112 19985056-19993038 ~-8K 10750(OSGEP)(-)Loci: 2823 19993129-19995765 ~-3K 10751(APEX1)(+)Loci: 2821 19414266-19415211 ~-1K 10737(OR4K2)(+)Link out to UCSC