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0MMP25_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameMMP25
DescriptionMatrix metalloproteinase-25 precursor (ec 3.4.24.-) (mmp-25) (membrane-type matrix metalloproteinase 6) (mt-mmp 6) (membrane-type-6 matrix metalloproteinase) (mt6-mmp) (leukolysin).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0009986 cell surface (IEP)
0005578 extracellular matrix (sensu Metazoa) (NAS)
0016020 membrane (NAS)
0006954 inflammatory response (NAS)
0006508 proteolysis and peptidolysis (NAS)

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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 families: Family M10 (clan MA(M)).ubfamily M10A - matrixinFamily M12 (clan MA(M)).ubfamily M12B - adamalysinThe protein fold of the peptidase domain for members of this family resembles that of thermolysin.he type example for clan MA.Sequences having this domain are extracellular metalloproteases.uch as collagenase and stromelysin.hichdegrade the extracellular matrix.re known as matrixins. They are zinc-dependent.alcium-activated proteases synthesised as inactive precursors(zymogens).hich are proteolytically cleaved to yield the active enzyme. All matrixins and related proteins possess 2 domains: an N-terminaldomain.nd a zinc-binding active site domain. The N-terminal domainpeptide.leaved during the activation step.ncludes a conserved PRCGVPDVoctapeptide.nown as the cysteine switch.hose Cys residue chelates theactive site zinc atom.endering the enzyme inactive. The active enzymedegrades components of the extracellular matrix.laying a role in theinitial steps of tissue remodelling during morphogenesis.ound healing.ngiogenesis and tumour invasion .
  IPR001818:Peptidase M10A and M12B, matrixin and adamalysin
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 zinc-dependent metallopeptidases (with the notable exceptionof the carboxypeptidases) share a common pattern of primary structure .n the part of their sequence involved in the binding of zinc.nd can begrouped together as a superfamily.nown as the metzincins.n the basis ofthis sequence similarity. They can be classified into around 40 distinct families . This signature defines the metallopeptidases associated with MEROPS peptidase families: M7.8.10 (subfamilies A. and C) and M12 (subfamily A) all of which are members of clan MA(M).
  IPR006026:Peptidase, metallopeptidases
Hemopexin () is a serum glycoprotein that binds haem and transports it to the liver for breakdown and iron recovery.fter which the free hemopexin returns to the circulation . Hemopexin prevents haem-mediated oxidative stress. Structurally hemopexin consists of two similar halves of approximately two hundred amino acid residues connected by a histidine-rich hinge region. Each half is itself formed by the repetition of a basic unit of some 35 to 45 residues. Hemopexin-like domains have been found in two other types of proteins.itronectin . cell adhesion and spreading factor found in plasma and tissues.nd matrixins MMP-1.MP-2.MP-3.MP-9.MP-10.MP-11.MP-12.MP-14.MP-15 and MMP-16.embers of the matrix metalloproteinase family that cleave extracellular matrix constituents . These zinc endopeptidases.hich belong to MEROPS peptidase subfamily M10A.ave a single hemopexin-like domain in their C-terminal section. It is suggested that the hemopexin domain facilitates binding to a variety of molecules and proteins.or example the HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).
  IPR000585:Hemopexin
This domain.eptidoglycan binding domain 1.ay have a general peptidoglycan binding function. It is composed of three alpha helices and is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation . Examples are:Muramoyl-pentapeptide carboxypeptidase ()N-acetylmuramoyl-L-alanine amidase cwlA precursor (cell wall hydrolase.utolysin.Autolytic lysozyme (1.-beta-N-acetylmuramidase.utolysin.Membrane-bound lytic murein transglycosylase BMany of the proteins having this domain are as yet uncharacterised. Those that are.re metallopeptidases belonging to MEROPS peptidase family M15 (clan MD).ubfamily M15A. A number of the proteins belonging to subfamily M15A are non-peptidase homologues as they 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.
  IPR002477:Peptidoglycan-binding domain 1
The peptidoglycan-binding domain (PGBD).hich may have a general peptidoglycan-binding function.as a core structure consisting of a closed.hree-helical bundle with a left-handed twist. It is found at the N or C terminus of a variety of enzymes involved in bacterial cell degradation. For example.he zinc-containing D-alanyl-D-alanine-cleaving carboxypeptidase.anX.ontains an N-terminal PGBD .Eukaryotic enzymes can contain structurally similar PGBD-like domains. Matrix metalloproteinases (MMP).hich catalyse extracellular matrix degradation.ave N-terminal domains that resemble PGBD. Examples are gelatinase A (MMP-2).hich degrades type IV collagen .tromelysin-1 (MMP-3).hich plays a role in arthritis and tumour invasion and gelatinase B (MMP-9) secreted by neutrophils as part of the innate immune defence mechanism . Several MMPs are implicated in cancer progression.ince degradation of the extracellular matrix is an essential step in the cascade of metastasis .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009070:Peptidoglycan binding-like
IPR001818:Peptidase_M10 
Evalue:-80.5686340332031 
Location:114-280IPR000585:Hemopexin 
Evalue:-15.1366767883301 
Location:416-462IPR002477:PG_binding_1 
Evalue:-13.5376024246216 
Location:25-89IPR000585:Hemopexin 
Evalue:-10.6777811050415 
Location:321-365IPR000585:Hemopexin 
Evalue:-7.36653137207031 
Location:370-412IPR000585:Hemopexin 
Evalue:-3 
Location:464-508IPR000585:HEMOPEXIN 
Evalue:0 
Location:0-0
SequencesProtein: MMP25_HUMAN (562 aa)
mRNA: NM_022468
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 assignmentK08003
  Level 3 annotation:
    matrix metalloproteinase 25 (membrane-inserted)
  Level 2 annotation:
    Cell motility and secretion
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 113 residues, 3036682-3037018Exon2: 46 residues, 3037416-3037549Exon3: 47 residues, 3040010-3040146Exon4: 99 residues, 3040255-3040548Exon5: 61 residues, 3047034-3047211Exon6: 30 residues, 3047311-3047396Exon7: 29 residues, 3047532-3047615Exon8: 53 residues, 3048182-3048335Exon9: 88 residues, 3048413-3048671Exon10: 633 residues, 3048828-3050723Exon11: 2 residues, -Jump to MMP25_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 2919 3036682-3050723 ~-14K 13385(MMP25)(+)Loci: 4203 3232028-3246628 ~-15K 13403(MEFV)(-)Loci: 2920 3273487-3281456 ~-8K 13405(ZNF263)(+)Loci: 4204 3571183-3601586 ~-30K 13423(BTBD12)(-)Loci: 4205 3648039-3707514 ~-59K 13426(TRAP1)(-)Loci: 4206 3717719-3870723 ~-153K 13429(CREBBP)(-)Loci: 4202 2962794-2970475 ~-8K 13372(PKMYT1)(-)Link out to UCSC