Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q10738 (MMP7_MOUSE)

Last modified October 13, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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

May play a role in tissue reorganization.

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

Secretedextracellular spaceextracellular 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 9477Activation peptide By similarity
PRO_0000028740
Chain95 – 264170Matrilysin
PRO_0000028741

Regions

Motif85 – 928Cysteine switch By similarity

Sites

Active site2151 By similarity
Metal binding871Zinc 2; in inhibited form By similarity
Metal binding1531Calcium 1 By similarity
Metal binding1631Zinc 1 By similarity
Metal binding1651Zinc 1 By similarity
Metal binding1701Calcium 2 By similarity
Metal binding1711Calcium 2; via carbonyl oxygen By similarity
Metal binding1731Calcium 2; via carbonyl oxygen By similarity
Metal binding1751Calcium 2; via carbonyl oxygen By similarity
Metal binding1781Zinc 1 By similarity
Metal binding1851Calcium 1; via carbonyl oxygen By similarity
Metal binding1871Calcium 1; via carbonyl oxygen By similarity
Metal binding1891Calcium 1 By similarity
Metal binding1911Zinc 1 By similarity
Metal binding1931Calcium 2 By similarity
Metal binding1961Calcium 2 By similarity
Metal binding2141Zinc 2; catalytic By similarity
Metal binding2181Zinc 2; catalytic By similarity
Metal binding2241Zinc 2; catalytic By similarity

Experimental info

Sequence conflict2011G → D in AAA99983. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q10738-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EDA31A5EBAC63342

FASTA26429,755
        10         20         30         40         50         60 
MQLTLFCFVC LLPGHLALPL SQEAGDVSAH QWEQAQNYLR KFYPHDSKTK KVNSLVDNLK 

        70         80         90        100        110        120 
EMQKFFGLPM TGKLSPYIME IMQKPRCGVP DVAEYSLMPN SPKWHSRIVT YRIVSYTSDL 

       130        140        150        160        170        180 
PRIVVDQIVK KALRMWSMQI PLNFKRVSWG TADIIIGFAR RDHGDSFPFD GPGNTLGHAF 

       190        200        210        220        230        240 
APGPGLGGDA HFDKDEYWTD GEDAGVNFLF AATHEFGHSL GLSHSSVPGT VMYPTYQRDY 

       250        260 
SEDFSLTKDD IAGIQKLYGK RNTL 

« Hide

References

[1]"The metalloproteinase matrilysin is preferentially expressed by epithelial cells in a tissue-restricted pattern in the mouse."
Wilson C.L., Heppner K.J., Rudolph L.A., Matrisian L.M.
Mol. Biol. Cell 6:851-869(1995) [PubMed: 7579699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: ICR.
Tissue: Uterus.
+Additional computationally mapped references.

Cross-references

Sequence databases

L36238 expand/collapse EMBL AC list , L36243, L36242, L36241, L36240, L36239 Genomic DNA. Translation: AAA99984.1.
L36244 mRNA. Translation: AAA99983.1.
IPIIPI00275232.
UniGeneMm.4825

3D structure databases

HSSPHSSP built from PDB template 1MMR based on UniProtKB P09237.
SMRQ10738. Positions 95-261.
ModBaseSearch...

Protein family/group databases

MEROPSM10.008.

Proteomic databases

PRIDEQ10738.

Genome annotation databases

EnsemblENSMUST00000018767; ENSMUSP00000018767; ENSMUSG00000018623; Mus musculus. [Genome view]
UCSCuc009ocv.1. mouse.

Organism-specific databases

MGIMGI:103189. Mmp7.

Phylogenomic databases

HOVERGENQ10738.

Enzyme and pathway databases

BRENDA3.4.24.23. 244.

Gene expression databases

ArrayExpressQ10738.
BgeeQ10738.
CleanExMM_MMP7.
GenevestigatorQ10738.

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

SOURCESearch...

Entry information

Entry nameMMP7_MOUSE
AccessionPrimary (citable) accession number: Q10738
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 13, 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)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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