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P33435 (MMP13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. 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:
Collagenase 3

EC=3.4.24.-
Alternative name(s):
Matrix metalloproteinase-13
Short name=MMP-13
Gene names
Name:Mmp13
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades collagen type I.

Cofactor

Binds 4 calcium ions per subunit.

Binds 2 zinc ions per subunit.

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.

Contains 4 hemopexin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 10485Activation peptide Potential
PRO_0000028790
Chain105 – 472368Collagenase 3
PRO_0000028791

Regions

Repeat282 – 33150Hemopexin 1
Repeat332 – 37847Hemopexin 2
Repeat380 – 42849Hemopexin 3
Repeat429 – 47244Hemopexin 4
Motif95 – 1028Cysteine switch By similarity

Sites

Active site2241
Metal binding971Zinc 2; in inhibited form By similarity
Metal binding1631Calcium 1
Metal binding1731Zinc 1
Metal binding1751Zinc 1
Metal binding1801Calcium 2
Metal binding1811Calcium 2; via carbonyl oxygen
Metal binding1881Zinc 1
Metal binding1951Calcium 1; via carbonyl oxygen
Metal binding1971Calcium 1; via carbonyl oxygen
Metal binding1991Calcium 1
Metal binding2011Zinc 1
Metal binding2061Calcium 2
Metal binding2231Zinc 2; catalytic
Metal binding2271Zinc 2; catalytic
Metal binding2331Zinc 2; catalytic
Metal binding2921Calcium 3; via carbonyl oxygen By similarity
Metal binding2941Calcium 4; via carbonyl oxygen By similarity
Metal binding3361Calcium 3; via carbonyl oxygen By similarity
Metal binding3381Calcium 4; via carbonyl oxygen By similarity
Metal binding3841Calcium 3; via carbonyl oxygen By similarity
Metal binding3861Calcium 4; via carbonyl oxygen By similarity
Metal binding4331Calcium 3; via carbonyl oxygen By similarity
Metal binding4351Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Disulfide bond285 ↔ 472 By similarity

Secondary structure

............................. 472
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33435 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 67F437B89B4D0DBD

FASTA47254,182
        10         20         30         40         50         60 
MHSAILATFF LLSWTPCWSL PLPYGDDDDD DLSEEDLVFA EHYLKSYYHP ATLAGILKKS 

        70         80         90        100        110        120 
TVTSTVDRLR EMQSFFGLEV TGKLDDPTLD IMRKPRCGVP DVGEYNVFPR TLKWSQTNLT 

       130        140        150        160        170        180 
YRIVNYTPDM SHSEVEKAFR KAFKVWSDVT PLNFTRIYDG TADIMISFGT KEHGDFYPFD 

       190        200        210        220        230        240 
GPSGLLAHAF PPGPNYGGDA HFDDDETWTS SSKGYNLFIV AAHELGHSLG LDHSKDPGAL 

       250        260        270        280        290        300 
MFPIYTYTGK SHFMLPDDDV QGIQFLYGPG DEDPNPKHPK TPEKCDPALS LDAITSLRGE 

       310        320        330        340        350        360 
TMIFKDRFFW RLHPQQVEAE LFLTKSFWPE LPNHVDAAYE HPSRDLMFIF RGRKFWALNG 

       370        380        390        400        410        420 
YDILEGYPRK ISDLGFPKEV KRLSAAVHFE NTGKTLFFSE NHVWSYDDVN QTMDKDYPRL 

       430        440        450        460        470 
IEEEFPGIGN KVDAVYEKNG YIYFFNGPIQ FEYSIWSNRI VRVMPTNSIL WC 

« Hide

References

[1]"Cloning and sequencing of mouse collagenase cDNA. Divergence of mouse and rat collagenases from the other mammalian collagenases."
Henriet P., Rousseau G.G., Eeckhout Y.
FEBS Lett. 310:175-178(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 105-119 AND 266-275.
Strain: NMRI.
Tissue: Calvaria.
[2]"Structure of recombinant mouse collagenase-3 (MMP-13)."
Botos I., Meyer E., Swanson S.M., Lemaitre V., Eeckhout Y., Meyer E.F.
J. Mol. Biol. 292:837-844(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 105-268.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66473 mRNA. Translation: CAA47102.1.
PIRS29243.
RefSeqNP_032633.1. NM_008607.2.
UniGeneMm.5022.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CXVX-ray2.00A/B105-268[»]
ProteinModelPortalP33435.
SMRP33435. Positions 36-472.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM10.013.

PTM databases

PhosphoSiteP33435.

Proteomic databases

PRIDEP33435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015394; ENSMUSP00000015394; ENSMUSG00000050578.
GeneID17386.
KEGGmmu:17386.
UCSCuc009ocg.2. mouse.

Organism-specific databases

CTD4322.
MGIMGI:1340026. Mmp13.

Phylogenomic databases

eggNOGNOG299356.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidP33435.
KOK07994.
OMANQVWSYD.
OrthoDBEOG7XPZ57.
PhylomeDBP33435.
TreeFamTF315428.

Gene expression databases

ArrayExpressP33435.
BgeeP33435.
CleanExMM_MMP13.
GenevestigatorP33435.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR028711. Collagenase_3/4.
IPR000585. 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.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF77. PTHR10201:SF77. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMMP13. mouse.
EvolutionaryTraceP33435.
NextBio291996.
PROP33435.
SOURCESearch...

Entry information

Entry nameMMP13_MOUSE
AccessionPrimary (citable) accession number: P33435
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 130 of the entry and version 1 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