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P33435

- MMP13_MOUSE

UniProt

P33435 - MMP13_MOUSE

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Protein
Collagenase 3
Gene
Mmp13
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CTGF. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CTGF. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.5 Publications

Cofactori

Calcium. Can bind about 5 calcium ions per subunit.1 Publication
Binds 2 zinc ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi97 – 971Zinc 2; in inhibited form By similarity
Metal bindingi129 – 1291Calcium 1 By similarity
Metal bindingi163 – 1631Calcium 2; via carbonyl oxygen
Metal bindingi173 – 1731Zinc 1; via tele nitrogen
Metal bindingi175 – 1751Zinc 1
Metal bindingi180 – 1801Calcium 3
Metal bindingi181 – 1811Calcium 3; via carbonyl oxygen
Metal bindingi183 – 1831Calcium 3; via carbonyl oxygen
Metal bindingi185 – 1851Calcium 3; via carbonyl oxygen
Metal bindingi188 – 1881Zinc 1; via tele nitrogen
Metal bindingi195 – 1951Calcium 2; via carbonyl oxygen By similarity
Metal bindingi197 – 1971Calcium 2; via carbonyl oxygen
Metal bindingi199 – 1991Calcium 2 By similarity
Metal bindingi201 – 2011Zinc 1; via pros nitrogen
Metal bindingi203 – 2031Calcium 3
Metal bindingi204 – 2041Calcium 1 By similarity
Metal bindingi206 – 2061Calcium 1; via carbonyl oxygen By similarity
Metal bindingi206 – 2061Calcium 3
Metal bindingi223 – 2231Zinc 2; via tele nitrogen; catalytic
Active sitei224 – 2241
Metal bindingi227 – 2271Zinc 2; via tele nitrogen; catalytic
Metal bindingi233 – 2331Zinc 2; via tele nitrogen; catalytic
Metal bindingi241 – 2411Zinc 2; via carbonyl oxygen; catalytic By similarity
Metal bindingi292 – 2921Calcium 4; via carbonyl oxygen By similarity
Metal bindingi294 – 2941Calcium 5; via carbonyl oxygen By similarity
Metal bindingi336 – 3361Calcium 4; via carbonyl oxygen By similarity
Metal bindingi338 – 3381Calcium 5; via carbonyl oxygen By similarity
Metal bindingi384 – 3841Calcium 4; via carbonyl oxygen By similarity
Metal bindingi386 – 3861Calcium 5; via carbonyl oxygen By similarity
Metal bindingi433 – 4331Calcium 4; via carbonyl oxygen By similarity
Metal bindingi435 – 4351Calcium 5; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. collagen binding Source: UniProtKB
  3. metalloendopeptidase activity Source: MGI
  4. peptidase activity Source: MGI
  5. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. bone mineralization Source: UniProtKB
  2. bone morphogenesis Source: UniProtKB
  3. cartilage development Source: MGI
  4. cellular protein metabolic process Source: MGI
  5. collagen catabolic process Source: UniProtKB
  6. endochondral ossification Source: UniProtKB
  7. extracellular matrix disassembly Source: UniProtKB
  8. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Protein family/group databases

MEROPSiM10.013.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagenase 3 (EC:3.4.24.-)
Alternative name(s):
Matrix metalloproteinase-13
Short name:
MMP-13
Gene namesi
Name:Mmp13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1340026. Mmp13.

Subcellular locationi

Secretedextracellular spaceextracellular matrix Inferred. Secreted 2 Publications

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice are born at the expected Mendelian rate, are fertile and have a normal life span. Mutant embryos show a delay in the development of the primary ossification centers. Besides, they display an increased length of the growth plates of the long bones from the hind limbs (1 Publication). Three week old mutant mice display an increased trabecular bone volume due to an increase in the length of the hypertrophic chondrocyte zone of the growth plate. This phenotype persists during several months (1 Publication and 1 Publication), but one year old mutant mice display no longer any difference relative to wild-type (1 Publication). After bone fractures, mutant mice show delays in carticage remodeling and resorption, as well as an increased volume of spongy bone mass. In addition, mutant mice show delayed healing of cutaneous wounds that is most evident three to seven days after wounding. The delay in wound healing and in re-epithelialization is exacerbated in mice lacking both Mmp13 and Mmp9.5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed prediction
Add
BLAST
Propeptidei20 – 10485Activation peptide
PRO_0000028790Add
BLAST
Chaini105 – 472368Collagenase 3
PRO_0000028791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi118 – 1181N-linked (GlcNAc...) Reviewed prediction
Glycosylationi153 – 1531N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi285 ↔ 472 By similarity
Glycosylationi410 – 4101N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) By similarity.
N-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP33435.

PTM databases

PhosphoSiteiP33435.

Expressioni

Tissue specificityi

Detected in epidermal cells and stromal fibroblasts in wounded skin, but not in normal skin (at protein level). Detected in embryonic hypertrophic chondrocytes and newly recruited bone cells at primary ossification centers. After adult bone fracture, detected in periosteum and in chondrocytes in the cartilage. Detected in immature and mature osteoblasts in the fracture callus. Detected in calvaria from neonates. Detected in wounded skin, but not in normal skin.3 Publications

Gene expression databases

ArrayExpressiP33435.
BgeeiP33435.
CleanExiMM_MMP13.
GenevestigatoriP33435.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi117 – 1237
Helixi132 – 14716
Beta strandi153 – 1564
Beta strandi158 – 1603
Beta strandi163 – 1697
Beta strandi174 – 1763
Beta strandi181 – 1844
Beta strandi187 – 1893
Beta strandi192 – 1943
Turni195 – 1984
Beta strandi200 – 2034
Beta strandi208 – 2169
Helixi217 – 22913
Beta strandi242 – 2443
Helixi257 – 26711

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CXVX-ray2.00A/B105-268[»]
ProteinModelPortaliP33435.
SMRiP33435. Positions 36-472.

Miscellaneous databases

EvolutionaryTraceiP33435.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati282 – 33150Hemopexin 1
Add
BLAST
Repeati332 – 37847Hemopexin 2
Add
BLAST
Repeati380 – 42849Hemopexin 3
Add
BLAST
Repeati429 – 47244Hemopexin 4
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 24771Interaction with TIMP2 By similarity
Add
BLAST
Regioni269 – 472204Interaction with collagen By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi95 – 1028Cysteine switch By similarity

Domaini

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 By similarity.
The C-terminal region binds to collagen By similarity.

Sequence similaritiesi

Belongs to the peptidase M10A family.
Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG299356.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiP33435.
KOiK07994.
OMAiNQVWSYD.
OrthoDBiEOG7XPZ57.
PhylomeDBiP33435.
TreeFamiTF315428.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR028711. Collagenase_3.
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]
PANTHERiPTHR10201:SF130. PTHR10201:SF130. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33435-1 [UniParc]FASTAAdd to Basket

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MHSAILATFF LLSWTPCWSL PLPYGDDDDD DLSEEDLVFA EHYLKSYYHP    50
ATLAGILKKS TVTSTVDRLR EMQSFFGLEV TGKLDDPTLD IMRKPRCGVP 100
DVGEYNVFPR TLKWSQTNLT YRIVNYTPDM SHSEVEKAFR KAFKVWSDVT 150
PLNFTRIYDG TADIMISFGT KEHGDFYPFD GPSGLLAHAF PPGPNYGGDA 200
HFDDDETWTS SSKGYNLFIV AAHELGHSLG LDHSKDPGAL MFPIYTYTGK 250
SHFMLPDDDV QGIQFLYGPG DEDPNPKHPK TPEKCDPALS LDAITSLRGE 300
TMIFKDRFFW RLHPQQVEAE LFLTKSFWPE LPNHVDAAYE HPSRDLMFIF 350
RGRKFWALNG YDILEGYPRK ISDLGFPKEV KRLSAAVHFE NTGKTLFFSE 400
NHVWSYDDVN QTMDKDYPRL IEEEFPGIGN KVDAVYEKNG YIYFFNGPIQ 450
FEYSIWSNRI VRVMPTNSIL WC 472
Length:472
Mass (Da):54,182
Last modified:February 1, 1994 - v1
Checksum:i67F437B89B4D0DBD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66473 mRNA. Translation: CAA47102.1.
CCDSiCCDS22803.1.
PIRiS29243.
RefSeqiNP_032633.1. NM_008607.2.
UniGeneiMm.5022.

Genome annotation databases

EnsembliENSMUST00000015394; ENSMUSP00000015394; ENSMUSG00000050578.
GeneIDi17386.
KEGGimmu:17386.
UCSCiuc009ocg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66473 mRNA. Translation: CAA47102.1 .
CCDSi CCDS22803.1.
PIRi S29243.
RefSeqi NP_032633.1. NM_008607.2.
UniGenei Mm.5022.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CXV X-ray 2.00 A/B 105-268 [» ]
ProteinModelPortali P33435.
SMRi P33435. Positions 36-472.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M10.013.

PTM databases

PhosphoSitei P33435.

Proteomic databases

PRIDEi P33435.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000015394 ; ENSMUSP00000015394 ; ENSMUSG00000050578 .
GeneIDi 17386.
KEGGi mmu:17386.
UCSCi uc009ocg.2. mouse.

Organism-specific databases

CTDi 4322.
MGIi MGI:1340026. Mmp13.

Phylogenomic databases

eggNOGi NOG299356.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi P33435.
KOi K07994.
OMAi NQVWSYD.
OrthoDBi EOG7XPZ57.
PhylomeDBi P33435.
TreeFami TF315428.

Enzyme and pathway databases

Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

ChiTaRSi MMP13. mouse.
EvolutionaryTracei P33435.
NextBioi 291996.
PROi P33435.
SOURCEi Search...

Gene expression databases

ArrayExpressi P33435.
Bgeei P33435.
CleanExi MM_MMP13.
Genevestigatori P33435.

Family and domain databases

Gene3Di 2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR028711. Collagenase_3.
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 ]
PANTHERi PTHR10201:SF130. PTHR10201:SF130. 1 hit.
Pfami PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. "Altered endochondral bone development in matrix metalloproteinase 13-deficient mice."
    Stickens D., Behonick D.J., Ortega N., Heyer B., Hartenstein B., Yu Y., Fosang A.J., Schorpp-Kistner M., Angel P., Werb Z.
    Development 131:5883-5895(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
  3. "Critical roles for collagenase-3 (Mmp13) in development of growth plate cartilage and in endochondral ossification."
    Inada M., Wang Y., Byrne M.H., Rahman M.U., Miyaura C., Lopez-Otin C., Krane S.M.
    Proc. Natl. Acad. Sci. U.S.A. 101:17192-17197(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Role of matrix metalloproteinase 13 in both endochondral and intramembranous ossification during skeletal regeneration."
    Behonick D.J., Xing Z., Lieu S., Buckley J.M., Lotz J.C., Marcucio R.S., Werb Z., Miclau T., Colnot C.
    PLoS ONE 2:E1150-E1150(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  5. "MMP-13 plays a role in keratinocyte migration, angiogenesis, and contraction in mouse skin wound healing."
    Hattori N., Mochizuki S., Kishi K., Nakajima T., Takaishi H., D'Armiento J., Okada Y.
    Am. J. Pathol. 175:533-546(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  6. "MMP-13 regulates growth of wound granulation tissue and modulates gene expression signatures involved in inflammation, proteolysis, and cell viability."
    Toriseva M., Laato M., Carpen O., Ruohonen S.T., Savontaus E., Inada M., Krane S.M., Kahari V.M.
    PLoS ONE 7:E42596-E42596(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 105-268 IN COMPLEX WITH ZINC AND CALCIUM IONS, COFACTOR.

Entry informationi

Entry nameiMMP13_MOUSE
AccessioniPrimary (citable) accession number: P33435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 3, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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