Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q10738

- MMP7_MOUSE

UniProt

Q10738 - MMP7_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Matrilysin

Gene

Mmp7

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Binds 2 calcium ions per subunit.By similarity
Binds 2 zinc 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. zinc ion binding Source: InterPro

GO - Biological processi

  1. antibacterial peptide secretion Source: MGI
  2. collagen catabolic process Source: UniProtKB-KW
  3. defense response to bacterium Source: MGI
  4. defense response to Gram-negative bacterium Source: MGI
  5. defense response to Gram-positive bacterium Source: MGI
  6. regulation of cell proliferation Source: MGI
  7. 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_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: Ensembl
  3. proteinaceous extracellular matrix Source: UniProtKB-KW
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. 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L36238
, L36243 , L36242 , L36241 , L36240 , L36239 Genomic DNA. Translation: AAA99984.1 .
L36244 mRNA. Translation: AAA99983.1 .
UniGenei Mm.4825.

3D structure databases

ProteinModelPortali Q10738.
SMRi Q10738. Positions 36-260.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M10.008.

PTM databases

PhosphoSitei Q10738.

Proteomic databases

PRIDEi Q10738.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:103189. Mmp7.

Phylogenomic databases

eggNOGi NOG312228.
HOVERGENi HBG052484.
InParanoidi Q10738.

Enzyme and pathway databases

BRENDAi 3.4.24.23. 3474.
Reactomei REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.

Miscellaneous databases

PROi Q10738.
SOURCEi Search...

Gene expression databases

Bgeei Q10738.
CleanExi MM_MMP7.
ExpressionAtlasi Q10738. differential.
Genevestigatori Q10738.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR10201:SF128. PTHR10201:SF128. 1 hit.
Pfami PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PRINTSi PR00138. MATRIXIN.
SMARTi SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 118 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