Skip Header

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

Matrilysin

Gene

Mmp7

Organism
Rattus norvegicus (Rat)
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

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 bindingi90 – 901Zinc 2; in inhibited formBy similarity
Metal bindingi156 – 1561Calcium 1By similarity
Metal bindingi166 – 1661Zinc 1By similarity
Metal bindingi168 – 1681Zinc 1By similarity
Metal bindingi173 – 1731Calcium 2By similarity
Metal bindingi174 – 1741Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi176 – 1761Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi178 – 1781Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi181 – 1811Zinc 1By similarity
Metal bindingi188 – 1881Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi190 – 1901Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi192 – 1921Calcium 1By similarity
Metal bindingi194 – 1941Zinc 1By similarity
Metal bindingi196 – 1961Calcium 2By similarity
Metal bindingi199 – 1991Calcium 2By similarity
Metal bindingi217 – 2171Zinc 2; catalyticBy similarity
Active sitei218 – 2181PROSITE-ProRule annotation
Metal bindingi221 – 2211Zinc 2; catalyticBy similarity
Metal bindingi227 – 2271Zinc 2; catalyticBy similarity

GO - Molecular functioni

  • heparin binding Source: RGD
  • metalloendopeptidase activity Source: InterPro
  • zinc ion binding Source: InterPro

GO - Biological processi

  • aging Source: RGD
  • cellular response to mechanical stimulus Source: RGD
  • collagen catabolic process Source: UniProtKB-KW
  • estrous cycle Source: RGD
  • maternal process involved in female pregnancy Source: RGD
  • response to nutrient levels Source: RGD
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. 5301.
ReactomeiR-RNO-1442490. Collagen degradation.
R-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-1592389. Activation of Matrix Metalloproteinases.
R-RNO-2022090. Assembly of collagen fibrils and other multimeric structures.

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
Synonyms:Mmp-7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi3100. Mmp7.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • 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 – 2020By similarityAdd
BLAST
Propeptidei21 – 9777Activation peptideBy similarityPRO_0000028742Add
BLAST
Chaini98 – 267170MatrilysinPRO_0000028743Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiP50280.
PRIDEiP50280.

Expressioni

Gene expression databases

GenevisibleiP50280. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014041.

Structurei

3D structure databases

ProteinModelPortaliP50280.
SMRiP50280. Positions 98-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi88 – 958Cysteine 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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000239471.
HOVERGENiHBG052484.
InParanoidiP50280.
KOiK01397.
OMAiKRFYSYD.
OrthoDBiEOG7XPZ57.
PhylomeDBiP50280.
TreeFamiTF315428.

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: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.

P50280-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAMRLTLFR IVCLLPGCLA LPLSQEAGEV TALQWEQAQN YLRKFYLHDS
60 70 80 90 100
KTKKATSAVD KLREMQKFFG LPETGKLSPR VMEIMQKPRC GVPDVAEFSL
110 120 130 140 150
MPNSPKWHSR TVTYRIVSYT TDLPRFLVDQ IVKRALRMWS MQIPLNFKRV
160 170 180 190 200
SWGTADIIIG FARGDHGDNF PFDGPGNTLG HAFAPGPGLG GDAHFDKDEY
210 220 230 240 250
WTDGEDSGVN FLFVATHELG HSLGLGHSSV PSSVMYPTYQ GDHSEDFSLT
260
KDDIAGIQKL YGKRNKL
Length:267
Mass (Da):29,885
Last modified:October 1, 1996 - v1
Checksum:iEBA3C3D9527A4C7B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24374 mRNA. Translation: AAA99432.1.
BC064657 mRNA. Translation: AAH64657.1.
PIRiA57490.
RefSeqiNP_036996.1. NM_012864.2.
UniGeneiRn.10282.

Genome annotation databases

EnsembliENSRNOT00000014041; ENSRNOP00000014041; ENSRNOG00000010507.
GeneIDi25335.
KEGGirno:25335.
UCSCiRGD:3100. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24374 mRNA. Translation: AAA99432.1.
BC064657 mRNA. Translation: AAH64657.1.
PIRiA57490.
RefSeqiNP_036996.1. NM_012864.2.
UniGeneiRn.10282.

3D structure databases

ProteinModelPortaliP50280.
SMRiP50280. Positions 98-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014041.

Protein family/group databases

MEROPSiM10.008.

Proteomic databases

PaxDbiP50280.
PRIDEiP50280.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014041; ENSRNOP00000014041; ENSRNOG00000010507.
GeneIDi25335.
KEGGirno:25335.
UCSCiRGD:3100. rat.

Organism-specific databases

CTDi4316.
RGDi3100. Mmp7.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000239471.
HOVERGENiHBG052484.
InParanoidiP50280.
KOiK01397.
OMAiKRFYSYD.
OrthoDBiEOG7XPZ57.
PhylomeDBiP50280.
TreeFamiTF315428.

Enzyme and pathway databases

BRENDAi3.4.24.23. 5301.
ReactomeiR-RNO-1442490. Collagen degradation.
R-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-1592389. Activation of Matrix Metalloproteinases.
R-RNO-2022090. Assembly of collagen fibrils and other multimeric structures.

Miscellaneous databases

NextBioi606227.
PROiP50280.

Gene expression databases

GenevisibleiP50280. RN.

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: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...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of rat uterine matrilysin and its cDNA. Relationship to human pump-1 and activation of procollagenases."
    Abramson S.R., Conner G.E., Nagase H., Neuhaus I., Woessner J.F.
    J. Biol. Chem. 270:16016-16022(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Uterus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.

Entry informationi

Entry nameiMMP7_RAT
AccessioniPrimary (citable) accession number: P50280
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 125 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. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.