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0NEUL_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameNLN
DescriptionNeurolysin, mitochondrial precursor (ec 3.4.24.16) (neurotensin endopeptidase) (mitochondrial oligopeptidase m) (microsomal endopeptidase) (mep).
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 M3 (clan MA(E)).ubfamilies M3A and M3B. The protein fold of the peptidase domain for members of this family resembles that of thermolysin.he type example for clan MA.The Thimet oligopeptidase family.s a large family of archaeal.acterial and eukaryotic oligopeptidases that cleave medium sized peptides. The group contains:mitochondrial intermediate peptidase ()Neurolysin.itochondrial precursor.)Thimet oligopeptidase ()Dipeptidyl carboxypeptidase ()Oligopeptidase A ()Oligoendopeptidase F
  IPR001567:Peptidase M3A and M3B, thimet/oligopeptidase F
IPR001567:Peptidase_M3 
Evalue:-208.193817138672 
Location:251-701
SequencesProtein: NEUL_HUMAN (704 aa)
mRNA: NM_020726
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK01393
  Level 3 annotation:
    
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 53 residues, 65053840-65053997Exon2: 88 residues, 65090149-65090409Exon3: 51 residues, 65094542-65094691Exon4: 38 residues, 65109009-65109117Exon5: 36 residues, 65111761-65111864Exon6: 55 residues, 65112843-65113004Exon7: 47 residues, 65117357-65117493Exon8: 124 residues, 65119700-65120067Exon9: 69 residues, 65124036-65124238Exon10: 64 residues, 65141097-65141284Exon11: 45 residues, 65141619-65141748Exon12: 47 residues, 65143837-65143974Exon13: 261 residues, 65154364-65155143Exon14: 2 residues, -Jump to NEUL_HUMAN  
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Loci Cluster (Details)Loci: 3457 65053840-65155143 ~-101K 28898(NLN)(+)Loci: 3458 65258139-65412606 ~-154K 28902(ERBB2IP)(+)Loci: 3459 65489710-65512393 ~-23K 28906(SFRS12)(+)Loci: 4715 64921264-64955943 ~-35K 28891(TRIM23)(-)Link out to UCSC