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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)DescriptionActionsGraphical viewLength
Metal bindingi87Zinc 2; in inhibited formBy similarity1
Metal bindingi153Calcium 1By similarity1
Metal bindingi163Zinc 1By similarity1
Metal bindingi165Zinc 1By similarity1
Metal bindingi170Calcium 2By similarity1
Metal bindingi171Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi173Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi175Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi178Zinc 1By similarity1
Metal bindingi185Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi187Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi189Calcium 1By similarity1
Metal bindingi191Zinc 1By similarity1
Metal bindingi193Calcium 2By similarity1
Metal bindingi196Calcium 2By similarity1
Metal bindingi214Zinc 2; catalyticBy similarity1
Active sitei215PROSITE-ProRule annotation1
Metal bindingi218Zinc 2; catalyticBy similarity1
Metal bindingi224Zinc 2; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

  • antibacterial peptide biosynthetic process Source: MGI
  • antibacterial peptide secretion Source: MGI
  • collagen catabolic process Source: UniProtKB-KW
  • defense response to bacterium Source: MGI
  • defense response to Gram-negative bacterium Source: MGI
  • defense response to Gram-positive bacterium Source: MGI
  • extracellular matrix disassembly Source: Reactome
  • proteolysis Source: MGI
  • regulation of cell proliferation Source: MGI
  • 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.
ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.

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
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:103189. Mmp7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
PropeptideiPRO_000002874018 – 94Activation peptideBy similarityAdd BLAST77
ChainiPRO_000002874195 – 264MatrilysinAdd BLAST170

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiQ10738.
PeptideAtlasiQ10738.
PRIDEiQ10738.

PTM databases

PhosphoSitePlusiQ10738.

Expressioni

Gene expression databases

BgeeiENSMUSG00000018623.
CleanExiMM_MMP7.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000018767.

Structurei

3D structure databases

ProteinModelPortaliQ10738.
SMRiQ10738.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi85 – 92Cysteine switchBy similarity8

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOVERGENiHBG052484.
InParanoidiQ10738.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di3.40.390.10. 1 hit.
InterProiIPR033739. M10A_MMP.
IPR028707. 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:SF143. PTHR10201:SF143. 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)DescriptionActionsGraphical viewLength
Sequence conflicti201G → D in AAA99983 (PubMed:7579699).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000018767.

Protein family/group databases

MEROPSiM10.008.

PTM databases

PhosphoSitePlusiQ10738.

Proteomic databases

PaxDbiQ10738.
PeptideAtlasiQ10738.
PRIDEiQ10738.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:103189. Mmp7.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
HOVERGENiHBG052484.
InParanoidiQ10738.

Enzyme and pathway databases

BRENDAi3.4.24.23. 3474.
ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.

Miscellaneous databases

PROiQ10738.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000018623.
CleanExiMM_MMP7.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di3.40.390.10. 1 hit.
InterProiIPR033739. M10A_MMP.
IPR028707. 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:SF143. PTHR10201:SF143. 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...

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: November 2, 2016
This is version 132 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

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 one 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.