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0PEPL1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameNPEPL1
DescriptionProbable aminopeptidase npepl1 (ec 3.4.11.-) (aminopeptidase-like 1).
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 the MEROPS peptidase family M17 (leucyl aminopeptidase family.lan MF).he type example being leucyl aminopeptidase from Bos taurus.Aminopeptidases are exopeptidases involved in the processing and regularturnover of intracellular proteins.lthough their precise role in cellularmetabolism is unclear . Leucine aminopeptidases cleave leucine residuesfrom the N-terminal of polypeptide chains.ut substantial rates are evidentfor all amino acids .The enzymes exist as homo-hexamers.omprising 2 trimers stacked on top ofone another . Each monomer binds 2 zinc ions and folds into 2 alpha/beta-type quasi-spherical globular domains.roducing a comma-like shape . The N-terminal 150 residues form a 5-stranded beta-sheet with 4 parallel and 1 anti-parallel strand sandwiched between 4 alpha-helices . An alpha-helix extends into the C-terminal domain.hich comprises a central 8-stranded saddle-shaped beta-sheet sandwiched between groups of helices.orming the monomer hydrophobic core . A 3-stranded beta-sheet resides on the surface of the monomer.here it interacts with other members of the hexamer . The 2 zinc ions and the active site are entirely located in the C-terminal catalytic domain .
  IPR000819:Peptidase M17, leucyl aminopeptidase, C-terminal
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. The majority of members of this family are zinc-dependent exopeptidases belonging to MEROPS peptidase family M17 (leucyl aminopeptidase.lan MF). This family excludes pepB aminopeptidases.hich are also members of MEROPS family M17 (see ). Leucyl aminopeptidase (LAP; ) selectively release N-terminal amino acid residues from polypeptides and proteins; in general they are involved in the processing.atabolism and degradation of intracellular proteins . Leucyl aminopeptidase forms a homohexamer containing two trimers stacked on top of one another . Each monomer binds two zinc ions. The zinc-binding and catalytic sites are located within the C-terminal catalytic domain . Leucine aminopeptidase has been shown to be identical with prolyl aminopeptidase () in mammals . Interestingly.embers of this group are also implicated in transcriptional regulation and are thought to combine catalytic and regulatory properties . The N-terminal domain of these proteins has been shown in Escherichia coli PepA to function as a DNA-binding protein in Xer site-specific recombination and in transcriptional control of the carAB operon . It is not well conserved and in some members can be found only by PSI-BLAST (after 4-6 iterations). It is not clear if the DNA binding function is preserved in all or even in most of the members.For additional information please see .
  IPR011356:Peptidase M17, leucyl aminopeptidase
IPR000819:Peptidase_M17 
Evalue:-110.327903747559 
Location:178-485
SequencesProtein: PEPL1_HUMAN (523 aa)
mRNA: AK021645
Local Annotation
Synapse Ontology
the generation of action potential at soma of neurons.
sdb:0313 generation of AP at soma  (Evidence:keywords)
KO assignmentK01269
  Level 3 annotation:
    aminopeptidase
  Level 2 annotation:
    Other amino acid metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 63 residues, 56701326-56701513Exon2: 64 residues, 56702199-56702385Exon3: 59 residues, 56702884-56703055Exon4: 32 residues, 56707146-56707236Exon5: 29 residues, 56707659-56707741Exon6: 49 residues, 56709478-56709621Exon7: 28 residues, 56715585-56715663Exon8: 35 residues, 56720941-56721042Exon9: 43 residues, 56721882-56722006Exon10: 61 residues, 56722379-56722556Exon11: 39 residues, 56723022-56723133Exon12: 83 residues, 56723630-56723873Exon13: 2 residues, -Jump to PEPL1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3271 56397650-56455367 ~-58K 23407(VAPB)(+)Loci: 3272 56659733-56687986 ~-28K 23415(STX16)(+)Loci: 3273 56701326-56723873 ~-23K 23419(NPEPL1)(+)Loci: 3274 56989705-57003581 ~-14K 23432(TH1L)(+)Loci: 3275 57027703-57035102 ~-7K 23436(TUBB1)(+)Loci: 3270 56318176-56375966 ~-58K 23405(RAB22A)(+)Link out to UCSC