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Reviewed, UniProtKB/Swiss-Prot P50280 (MMP7_RAT)

Last modified November 3, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Matrilysin
    EC=3.4.24.23
Alternative name(s):
    Pump-1 protease
    Uterine metalloproteinase
    Matrix metalloproteinase-7
      Short name=MMP-7
    Matrin
Gene names
Name: Mmp7
Synonyms: Mmp-7
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase By similarity.

Catalytic activity

Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).

Cofactor

Binds 2 calcium ions per subunit By similarity.

Binds 2 zinc ions per subunit By similarity.

Subcellular location

Secreted › extracellular space › extracellular matrix Probable.

Domain

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Sequence similarities

Belongs to the peptidase M10A family.

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Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
Gene Ontology (GO)
   Biological processcollagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Propeptide21 – 9777Activation peptide By similarity
PRO_0000028742
Chain98 – 267170Matrilysin
PRO_0000028743

Regions

Motif88 – 958Cysteine switch By similarity

Sites

Active site2181 By similarity
Metal binding901Zinc 2; in inhibited form By similarity
Metal binding1561Calcium 1 By similarity
Metal binding1661Zinc 1 By similarity
Metal binding1681Zinc 1 By similarity
Metal binding1731Calcium 2 By similarity
Metal binding1741Calcium 2; via carbonyl oxygen By similarity
Metal binding1761Calcium 2; via carbonyl oxygen By similarity
Metal binding1781Calcium 2; via carbonyl oxygen By similarity
Metal binding1811Zinc 1 By similarity
Metal binding1881Calcium 1; via carbonyl oxygen By similarity
Metal binding1901Calcium 1; via carbonyl oxygen By similarity
Metal binding1921Calcium 1 By similarity
Metal binding1941Zinc 1 By similarity
Metal binding1961Calcium 2 By similarity
Metal binding1991Calcium 2 By similarity
Metal binding2171Zinc 2; catalytic By similarity
Metal binding2211Zinc 2; catalytic By similarity
Metal binding2271Zinc 2; catalytic By similarity

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Sequences

Sequence LengthMass (Da)Tools
P50280-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EBA3C3D9527A4C7B

FASTA26729,885
        10         20         30         40         50         60 
MAAMRLTLFR IVCLLPGCLA LPLSQEAGEV TALQWEQAQN YLRKFYLHDS KTKKATSAVD 

        70         80         90        100        110        120 
KLREMQKFFG LPETGKLSPR VMEIMQKPRC GVPDVAEFSL MPNSPKWHSR TVTYRIVSYT 

       130        140        150        160        170        180 
TDLPRFLVDQ IVKRALRMWS MQIPLNFKRV SWGTADIIIG FARGDHGDNF PFDGPGNTLG 

       190        200        210        220        230        240 
HAFAPGPGLG GDAHFDKDEY WTDGEDSGVN FLFVATHELG HSLGLGHSSV PSSVMYPTYQ 

       250        260 
GDHSEDFSLT KDDIAGIQKL YGKRNKL

« Hide

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References

« Hide 'large scale' references
[1]"Characterization of rat uterine matrilysin and its cDNA. Relationship to human pump-1 and activation of procollagenases."
Abramson S.R., Conner G.E., Nagase H., Neuhaus I., Woessner J.F.
J. Biol. Chem. 270:16016-16022(1995) [PubMed: 7608162] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Uterus.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
+Additional computationally mapped references.

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Cross-references

Sequence databases

L24374 mRNA. Translation: AAA99432.1.
BC064657 mRNA. Translation: AAH64657.1.
IPIIPI00196590.
PIRA57490.
RefSeqNP_036996.1.
UniGeneRn.10282

3D structure databases

HSSPHSSP built from PDB template 1MMR based on UniProtKB P09237.
SMRP50280. Positions 98-264.
ModBaseSearch...

Protein-protein interaction databases

STRINGP50280.

Protein family/group databases

MEROPSM10.008.

Genome annotation databases

EnsemblENSRNOT00000014041; ENSRNOP00000014041; ENSRNOG00000010507; Rattus norvegicus. [Genome view]
GeneID25335.
KEGGrno:25335.
UCSCNM_012864. rat.

Organism-specific databases

CTD25335.
RGD3100. Mmp7.

Phylogenomic databases

HOVERGENP50280.
OMADERWTDG.

Enzyme and pathway databases

BRENDA3.4.24.23. 248.

Gene expression databases

ArrayExpressP50280.
GenevestigatorP50280.
GermOnlineENSRNOG00000010507. Rattus norvegicus.

Family and domain databases

InterProIPR001818. Pept_M10A_M12B.
IPR006025. Pept_M_Zn_BS.
IPR006026. Peptidase_M.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PfamPF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio606227.

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Entry information

Entry nameMMP7_RAT
AccessionPrimary (citable) accession number: P50280
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 3, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents