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0LONM_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NamePRSS15
DescriptionLon protease homolog, mitochondrial precursor (ec 3.4.21.-) (lon protease-like protein) (lonp) (lonhs).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (TAS)
0004176 ATP-dependent peptidase activity (TAS)
0006508 proteolysis and peptidolysis (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:
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .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 signature defines the N-terminal domain of the archael.acterial and eukaryotic lon proteases.hich are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family.lan SF). In the eukaryotes the majority of the proteins are located in the mitochondrial matrix . In yeast.im1.s located in the mitochondrial matrix.s required for mitochondrial function.s constitutively expressed but is increased after thermal stress.uggesting that Pim1 may play a role in the heat shock response .
  IPR003111:Peptidase S16, lon N-terminal
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .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 signature defines the C-terminal proteolytic domain of the archael.acterial and eukaryotic lon proteases.hich are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family.lan SF). In the eukaryotes the majority of the proteins are located in the mitochondrial matrix . In yeast.im1.s located in the mitochondrial matrix.s required for mitochondrial function.s constitutively expressed but is increased after thermal stress.uggesting that Pim1 may play a role in the heat shock response .
  IPR008269:Peptidase S16, lon C-terminal
A large family of ATPases has been described whose key feature is that they share a conserved region of about 220 amino acids that contains an ATP-binding site. This family is now called AAA.or ATPases Associated with diverse cellular Activities. The proteins that belong to this family either contain one or two AAA domains.It is proposed that.n general.he AAA domains in these proteins act as ATP-dependent protein clamps .In addition to the ATP-binding A and B motifs (see the relevant entry ).hich are located in the N-terminal half of this domain.here is a highly conserved region located in the central part of the domain.
  IPR003959:AAA ATPase, central region
AAA ATPases form a large.unctionally diverse protein family belonging to the AAA+ superfamily of ring-shaped P-loop NTPases.hich exert their activity through the energy-dependent unfolding of macromolecules. AAA ATPases contain a P-loop NTPase domain.hich is the most abundant class of NTP-binding protein fold.nd is found throughout all kingdoms of life . P-loop NTPase domains act to hydrolyse the beta-gamma phosphate bond of bound nucleoside triphosphate. There are two classes of P-loop domains: the KG (kinase-GTPase) division.nd the ASCE division.he latter including the AAA+ group as well as several other ATPases.There are at least six major clades of AAA domains (metalloproteases.eiotic proteins.1 and D2 domains of ATPases with two AAA domains.roteasome subunits.nd BSC1).s well as several minor clades.ome of which consist of hypothetical proteins . The domain organisation of AAA ATPases consists of a non-ATPase N-terminal domain that acts in substrate recognition.ollowed by one or two AAA domains (D1 and D2).ne of which may be degenerate.
  IPR003593:AAA ATPase
A group of ATP-binding proteins that includes the regulatory subunit of the ATP-dependent protease clpA; heat shock proteins clpB.04 and 78; and chloroplastproteins CD4a (ClpC) and CD4b belong to this family . The proteins are thought to protect cells from stress by controlling the aggregation and denaturation of vital cellular structures. They vary in size.ut share a domainwhich contains an ATP-binding site.These signatures which span the ATP binding region also identify the bacterial DNA polymerase III subunit tau ().TP-dependent protease La () and the mitochondrial lon protease homolog ().oth of which belong to MEROPS peptidase family S16.
  IPR001270:Chaperonin clpA/B
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .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 serine peptidases belong to the MEROPS peptidase family S16 (lon protease family.lan SF). The type example being the lon protease of Escherichia coli.Lon (La) protease was the first ATP-dependent protease to be purified fromE. coli . The enzyme is a homotetramer of 87kDa subunits.ith one proteolytic and one ATP-binding site per monomer.aking it structurally less complex than other known ATP-dependent proteases . Despite this relative structural simplicity.on recognises its substrates directly.ithout delegating the task of substrate recognition to other enzymes . By contrast.lpP endopeptidases (S14.lan SK) are multimeric assemblies of two different types of subunit.ne of which has ATPase activity.nd the other has proteolytic activity .Other members of this group include:Bacterial and archaeal La homologsEukaryotic ATP-dependent protease La ()Cell division protein ftsH homologsDNA repair protein radA homologsHolliday junction DNA helicase RuvBThe family also include proteins classified as non-peptidase homologues that either have been found experimentally to be without peptidase activity.r lack amino acid residues that are believed to be essential for the catalytic activity. A significant number of the non-peptidase homologues of S16 are found in .hich are described as Mg chelatase-related proteins.
  IPR001984:Peptidase S16, lon protease
Proteolytic enzymes that exploit serine in their catalytic activity areubiquitous.eing found in viruses.acteria and eukaryotes . Theyinclude a wide range of peptidase activity.ncluding exopeptidase.ndopeptidase.ligopeptidase and omega-peptidase activity. Over 20 families(denoted S1 - S27) of serine protease have been identified.hese beinggrouped into 6 clans (SA.B.C.E.F and SG) on the basis of structuralsimilarity and other functional evidence . Structures are known for fourof the clans (SA.B.C and SE): these appear to be totally unrelated.uggesting at least four evolutionary origins of serine peptidases andpossibly many more .Notwithstanding their different evolutionary origins.here are similaritiesin the reaction mechanisms of several peptidases. Chymotrypsin.ubtilisinand carboxypeptidase C clans have a catalytic triad of serine.spartate andhistidine in common: serine acts as a nucleophile.spartate as anelectrophile.nd histidine as a base . The geometric orientations ofthe catalytic residues are similar between families.espite differentprotein folds . The linear arrangements of the catalytic residuescommonly reflect clan relationships. For example the catalytic triad inthe chymotrypsin clan (SA) is ordered HDS.ut is ordered DHS in thesubtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) .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 signature defines the bacterial and eukaryotic lon proteases.hich are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family.lan SF). This family of sequences does not include the archaeal lon homologs. In the eukaryotes the majority of the proteins are located in the mitochondrial matrix . In yeast.im1.s located in the mitochondrial matrix.s required for mitochondrial function.s constitutively expressed but is increased after thermal stress.uggesting that Pim1 may play a role in the heat shock response .
  IPR004815:Peptidase S16, ATP-dependent protease La
IPR003111:LON 
Evalue:-130.301025390625 
Location:123-368IPR008269:Lon_C 
Evalue:-94.6575775146484 
Location:736-949IPR003959:AAA 
Evalue:-57.4685211181641 
Location:518-713
SequencesProtein: LONM_HUMAN (959 aa)
mRNA: NM_004793 X76040
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 assignmentK01362
  Level 3 annotation:
    
  Level 2 annotation:
    Other amino acid metabolism
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 125 residues, 5642845-5643219Exon2: 57 residues, 5644308-5644473Exon3: 74 residues, 5644562-5644780Exon4: 57 residues, 5645397-5645563Exon5: 49 residues, 5645771-5645912Exon6: 41 residues, 5647064-5647181Exon7: 43 residues, 5647259-5647382Exon8: 31 residues, 5647680-5647768Exon9: 61 residues, 5650037-5650216Exon10: 48 residues, 5651799-5651938Exon11: 75 residues, 5656782-5657003Exon12: 30 residues, 5658070-5658154Exon13: 45 residues, 5658707-5658837Exon14: 22 residues, 5659352-5659414Exon15: 79 residues, 5662781-5663013Exon16: 42 residues, 5664144-5664264Exon17: 31 residues, 5665193-5665282Exon18: 143 residues, 5670714-5671138Exon19: 2 residues, -Jump to LONM_HUMANExon1: 125 residues, 5642845-5643219Exon2: 57 residues, 5644308-5644473Exon3: 74 residues, 5644562-5644780Exon4: 57 residues, 5645397-5645563Exon5: 49 residues, 5645771-5645912Exon6: 41 residues, 5647064-5647181Exon7: 43 residues, 5647259-5647382Exon8: 31 residues, 5647680-5647768Exon9: 61 residues, 5650037-5650216Exon10: 48 residues, 5651799-5651938Exon11: 75 residues, 5656782-5657003Exon12: 30 residues, 5658070-5658154Exon13: 45 residues, 5658707-5658837Exon14: 22 residues, 5659352-5659414Exon15: 79 residues, 5662781-5663013Exon16: 42 residues, 5664144-5664264Exon17: 31 residues, 5665193-5665282Exon18: 156 residues, 5670714-5671176Exon19: 2 residues, -Jump to LONM_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3082 5774817-5779334 ~-5K 17769(NRTN)(+)Loci: 4357 5642845-5671176 ~-28K 17762(PRSS15)(-)Link out to UCSC