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Q02853 (MMP11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Stromelysin-3

Short name=SL-3
Short name=ST3
EC=3.4.24.-
Alternative name(s):
Matrix metalloproteinase-11
Short name=MMP-11
Gene names
Name:Mmp11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play an important role in the progression of epithelial malignancies.

Cofactor

Binds 1 calcium ion per subunit.

Binds 2 zinc ions per subunit.

Subcellular location

Secretedextracellular spaceextracellular matrix Probable.

Tissue specificity

Specifically expressed in the mammary gland during apoptosis.

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.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbasement membrane organization

Inferred from mutant phenotype PubMed 18622425. Source: MGI

collagen catabolic process

Inferred from direct assay PubMed 18622425. Source: MGI

collagen fibril organization

Inferred from mutant phenotype PubMed 18622425. Source: MGI

extracellular matrix organization

Inferred from mutant phenotype PubMed 18622425. Source: MGI

multicellular organismal development

Inferred from electronic annotation. Source: InterPro

negative regulation of fat cell differentiation

Inferred from direct assay PubMed 18622425. Source: MGI

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular matrix

Inferred from sequence orthology PubMed 18622425. Source: MGI

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

metallopeptidase activity

Inferred from direct assay PubMed 18622425. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Propeptide36 – 10166Activation peptide By similarity
PRO_0000028772
Chain102 – 492391Stromelysin-3
PRO_0000028773

Regions

Repeat295 – 34349Hemopexin 1
Repeat344 – 38643Hemopexin 2
Repeat388 – 43649Hemopexin 3
Repeat437 – 48448Hemopexin 4
Motif82 – 898Cysteine switch By similarity

Sites

Active site2201
Metal binding841Zinc 2; in inhibited form By similarity
Metal binding1681Zinc 1
Metal binding1701Zinc 1
Metal binding1751Calcium
Metal binding1761Calcium; via carbonyl oxygen
Metal binding1781Calcium; via carbonyl oxygen
Metal binding1801Calcium; via carbonyl oxygen
Metal binding1831Zinc 1
Metal binding1961Zinc 1
Metal binding2191Zinc 2; catalytic
Metal binding2231Zinc 2; catalytic
Metal binding2291Zinc 2; catalytic

Amino acid modifications

Disulfide bond298 ↔ 484 By similarity

Secondary structure

.............................. 492
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02853 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: B54E260E4AB3D7C3

FASTA49255,441
        10         20         30         40         50         60 
MARAACLLRA ISRVLLLPLP LLLLLLLLLP SPLMARARPP ESHRHHPVKK GPRLLHAALP 

        70         80         90        100        110        120 
NTLTSVPASH WVPSPAGSSR PLRCGVPDLP DVLNARNRQK RFVLSGGRWE KTDLTYRILR 

       130        140        150        160        170        180 
FPWQLVREQV RQTVAEALQV WSEVTPLTFT EVHEGRADIM IDFARYWHGD NLPFDGPGGI 

       190        200        210        220        230        240 
LAHAFFPKTH REGDVHFDYD ETWTIGDNQG TDLLQVAAHE FGHVLGLQHT TAAKALMSPF 

       250        260        270        280        290        300 
YTFRYPLSLS PDDRRGIQHL YGRPQMAPTS PAPTLSSQAG TDTNEIALLE PETPPDVCET 

       310        320        330        340        350        360 
SFDAVSTIRG ELFFFKAGFV WRLRSGRLQP GYPALASRHW QGLPSPVDAA FEDAQGQIWF 

       370        380        390        400        410        420 
FQGAQYWVYD GEKPVLGPAP LSKLGLQGSP VHAALVWGPE KNKIYFFRGG DYWRFHPRTQ 

       430        440        450        460        470        480 
RVDNPVPRRS TDWRGVPSEI DAAFQDAEGY AYFLRGHLYW KFDPVKVKVL EGFPRPVGPD 

       490 
FFDCAEPANT FR 

« Hide

References

[1]"The breast cancer-associated stromelysin-3 gene is expressed during mouse mammary gland apoptosis."
Lefebvre O., Wolf C., Limacher J.-M., Hutin P., Wendling C., Lemeur M., Basset P., Rio M.C.
J. Cell Biol. 119:997-1002(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Lefebvre O.
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed with a phosphinic inhibitor mimicking the transition-state."
Gall A.-L., Ruff M., Kannan R., Cuniasse P., Yiotakis A., Dive V., Rio M.-C., Basset P., Moras D.
J. Mol. Biol. 307:577-586(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 102-265.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z12604 mRNA. Translation: CAA78248.1.
PIRA44399.
RefSeqNP_032632.1. NM_008606.2.
XP_006513381.1. XM_006513318.1.
UniGeneMm.4561.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HV5X-ray2.60A/B/C/D/E/F102-265[»]
ProteinModelPortalQ02853.
SMRQ02853. Positions 61-470.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBQ02853.
ChEMBLCHEMBL3412.

Protein family/group databases

MEROPSM10.007.

PTM databases

PhosphoSiteQ02853.

Proteomic databases

PRIDEQ02853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000924; ENSMUSP00000000924; ENSMUSG00000000901.
ENSMUST00000120281; ENSMUSP00000112940; ENSMUSG00000000901.
GeneID17385.
KEGGmmu:17385.
UCSCuc007fto.1. mouse.

Organism-specific databases

CTD4320.
MGIMGI:97008. Mmp11.

Phylogenomic databases

eggNOGNOG236137.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidQ02853.
KOK07993.
OMAVDTNEIA.
OrthoDBEOG7XPZ57.
PhylomeDBQ02853.
TreeFamTF315428.

Gene expression databases

ArrayExpressQ02853.
BgeeQ02853.
CleanExMM_MMP11.
GenevestigatorQ02853.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR028705. Stromelysin-3.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF20. PTHR10201:SF20. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. SSF50923. 1 hit.
PROSITEPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ02853.
NextBio291992.
PMAP-CutDBQ02853.
PROQ02853.
SOURCESearch...

Entry information

Entry nameMMP11_MOUSE
AccessionPrimary (citable) accession number: Q02853
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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