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Protein

Matrilysin

Gene

Mmp7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase (By similarity).By similarity
May play a role in tissue reorganization.

Catalytic activityi

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).

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871Zinc 2; in inhibited formBy similarity
Metal bindingi153 – 1531Calcium 1By similarity
Metal bindingi163 – 1631Zinc 1By similarity
Metal bindingi165 – 1651Zinc 1By similarity
Metal bindingi170 – 1701Calcium 2By similarity
Metal bindingi171 – 1711Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi173 – 1731Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi175 – 1751Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi178 – 1781Zinc 1By similarity
Metal bindingi185 – 1851Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi187 – 1871Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi189 – 1891Calcium 1By similarity
Metal bindingi191 – 1911Zinc 1By similarity
Metal bindingi193 – 1931Calcium 2By similarity
Metal bindingi196 – 1961Calcium 2By similarity
Metal bindingi214 – 2141Zinc 2; catalyticBy similarity
Active sitei215 – 2151PROSITE-ProRule annotation
Metal bindingi218 – 2181Zinc 2; catalyticBy similarity
Metal bindingi224 – 2241Zinc 2; catalyticBy similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. peptidase activity Source: MGI
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. antibacterial peptide biosynthetic process Source: MGI
  2. antibacterial peptide secretion Source: MGI
  3. collagen catabolic process Source: UniProtKB-KW
  4. defense response to bacterium Source: MGI
  5. defense response to Gram-negative bacterium Source: MGI
  6. defense response to Gram-positive bacterium Source: MGI
  7. proteolysis Source: MGI
  8. regulation of cell proliferation Source: MGI
  9. response to drug Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.23. 3474.
ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Protein family/group databases

MEROPSiM10.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrilysin (EC:3.4.24.23)
Alternative name(s):
Matrin
Matrix metalloproteinase-7
Short name:
MMP-7
Pump-1 protease
Uterine metalloproteinase
Gene namesi
Name:Mmp7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:103189. Mmp7.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Propeptidei18 – 9477Activation peptideBy similarityPRO_0000028740Add
BLAST
Chaini95 – 264170MatrilysinPRO_0000028741Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiQ10738.

PTM databases

PhosphoSiteiQ10738.

Expressioni

Gene expression databases

BgeeiQ10738.
CleanExiMM_MMP7.
ExpressionAtlasiQ10738. baseline and differential.
GenevestigatoriQ10738.

Structurei

3D structure databases

ProteinModelPortaliQ10738.
SMRiQ10738. Positions 36-260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi85 – 928Cysteine switchBy 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.

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG312228.
HOVERGENiHBG052484.
InParanoidiQ10738.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR028707. Matrilysin.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF128. PTHR10201:SF128. 1 hit.
PfamiPF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q10738-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLTLFCFVC LLPGHLALPL SQEAGDVSAH QWEQAQNYLR KFYPHDSKTK
60 70 80 90 100
KVNSLVDNLK EMQKFFGLPM TGKLSPYIME IMQKPRCGVP DVAEYSLMPN
110 120 130 140 150
SPKWHSRIVT YRIVSYTSDL PRIVVDQIVK KALRMWSMQI PLNFKRVSWG
160 170 180 190 200
TADIIIGFAR RDHGDSFPFD GPGNTLGHAF APGPGLGGDA HFDKDEYWTD
210 220 230 240 250
GEDAGVNFLF AATHEFGHSL GLSHSSVPGT VMYPTYQRDY SEDFSLTKDD
260
IAGIQKLYGK RNTL
Length:264
Mass (Da):29,755
Last modified:October 1, 1996 - v1
Checksum:iEDA31A5EBAC63342
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011G → D in AAA99983. (PubMed:7579699)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36238
, L36243, L36242, L36241, L36240, L36239 Genomic DNA. Translation: AAA99984.1.
L36244 mRNA. Translation: AAA99983.1.
UniGeneiMm.4825.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L36238
, L36243, L36242, L36241, L36240, L36239 Genomic DNA. Translation: AAA99984.1.
L36244 mRNA. Translation: AAA99983.1.
UniGeneiMm.4825.

3D structure databases

ProteinModelPortaliQ10738.
SMRiQ10738. Positions 36-260.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM10.008.

PTM databases

PhosphoSiteiQ10738.

Proteomic databases

PRIDEiQ10738.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:103189. Mmp7.

Phylogenomic databases

eggNOGiNOG312228.
HOVERGENiHBG052484.
InParanoidiQ10738.

Enzyme and pathway databases

BRENDAi3.4.24.23. 3474.
ReactomeiREACT_199000. Activation of Matrix Metalloproteinases.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

PROiQ10738.
SOURCEiSearch...

Gene expression databases

BgeeiQ10738.
CleanExiMM_MMP7.
ExpressionAtlasiQ10738. baseline and differential.
GenevestigatoriQ10738.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR028707. Matrilysin.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF128. PTHR10201:SF128. 1 hit.
PfamiPF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: ICR.
    Tissue: Uterus.

Entry informationi

Entry nameiMMP7_MOUSE
AccessioniPrimary (citable) accession number: Q10738
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 121 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.