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P09237 (MMP7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrilysin

EC=3.4.24.23
Alternative name(s):
Matrin
Matrix metalloproteinase-7
Short name=MMP-7
Pump-1 protease
Uterine metalloproteinase
Gene names
Name:MMP7
Synonyms:MPSL1, PUMP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. Ref.7

Catalytic activity

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).

Cofactor

Binds 2 calcium ions per subunit.

Binds 2 zinc ions per subunit.

Subcellular location

Secretedextracellular spaceextracellular matrix Probable.

Domain

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 similarities

Belongs to the peptidase M10A family.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processantibacterial peptide secretion

Inferred from electronic annotation. Source: Ensembl

collagen catabolic process

Traceable author statement. Source: Reactome

defense response to Gram-negative bacterium

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-positive bacterium

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

proteolysis

Traceable author statement Ref.2. Source: ProtInc

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement Ref.2. Source: ProtInc

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetalloendopeptidase activity

Traceable author statement Ref.2. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.6
Propeptide18 – 9477Activation peptide
PRO_0000028738
Chain95 – 267173Matrilysin
PRO_0000028739

Regions

Motif85 – 928Cysteine switch By similarity

Sites

Active site2151
Metal binding871Zinc 2; in inhibited form By similarity
Metal binding1531Calcium 1
Metal binding1631Zinc 1
Metal binding1651Zinc 1
Metal binding1701Calcium 2
Metal binding1711Calcium 2; via carbonyl oxygen
Metal binding1731Calcium 2; via carbonyl oxygen
Metal binding1751Calcium 2; via carbonyl oxygen
Metal binding1781Zinc 1
Metal binding1851Calcium 1; via carbonyl oxygen
Metal binding1871Calcium 1; via carbonyl oxygen
Metal binding1891Calcium 1
Metal binding1911Zinc 1
Metal binding1931Calcium 2
Metal binding1961Calcium 2
Metal binding2141Zinc 2; catalytic
Metal binding2181Zinc 2; catalytic
Metal binding2241Zinc 2; catalytic

Natural variations

Natural variant771R → H. Ref.4
Corresponds to variant rs10502001 [ dbSNP | Ensembl ].
VAR_006729
Natural variant1371G → D. Ref.4
Corresponds to variant rs17884789 [ dbSNP | Ensembl ].
VAR_021027
Natural variant2411P → L. Ref.4
Corresponds to variant rs17886506 [ dbSNP | Ensembl ].
VAR_021028

Secondary structure

................................. 267
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09237 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: F6BD1FC0ADA23603

FASTA26729,677
        10         20         30         40         50         60 
MRLTVLCAVC LLPGSLALPL PQEAGGMSEL QWEQAQDYLK RFYLYDSETK NANSLEAKLK 

        70         80         90        100        110        120 
EMQKFFGLPI TGMLNSRVIE IMQKPRCGVP DVAEYSLFPN SPKWTSKVVT YRIVSYTRDL 

       130        140        150        160        170        180 
PHITVDRLVS KALNMWGKEI PLHFRKVVWG TADIMIGFAR GAHGDSYPFD GPGNTLAHAF 

       190        200        210        220        230        240 
APGTGLGGDA HFDEDERWTD GSSLGINFLY AATHELGHSL GMGHSSDPNA VMYPTYGNGD 

       250        260 
PQNFKLSQDD IKGIQKLYGK RSNSRKK 

« Hide

References

« Hide 'large scale' references
[1]"The collagenase gene family in humans consists of at least four members."
Muller D., Quantin B., Gesnel M.-C., Millon-Collard R., Abecassis J., Breathnach R.
Biochem. J. 253:187-192(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular characterization of a low-molecular-mass matrix metalloproteinase secreted by glomerular mesangial cells as PUMP-1."
Marti H.P., McNeil L., Thomas G., Davies M., Lovett D.H.
Biochem. J. 285:899-905(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[3]"Structure and expression of the human gene for the matrix metalloproteinase matrilysin."
Gaire M., Magbanua Z., McDonnell S., McNeil L.B., Lovett D.H., Matrisian L.M.
J. Biol. Chem. 269:2032-2040(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[4]NIEHS SNPs program
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-77; ASP-137 AND LEU-241.
[5]"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: Colon.
[6]"Purification and characterization of extracellular matrix-degrading metalloproteinase, matrin (pump-1), secreted from human rectal carcinoma cell line."
Miyazaki K., Hattori Y., Umenishi F., Yasumitsu H., Umeda M.
Cancer Res. 50:7758-7764(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-42.
[7]"Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members."
Quantin B., Murphy G., Breathnach R.
Biochemistry 28:5327-5334(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Matrilysin-inhibitor complexes: common themes among metalloproteases."
Browner M.F., Smith W.W., Castelhano A.L.
Biochemistry 34:6602-6610(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07819 mRNA. Translation: CAA30678.1.
Z11887 mRNA. Translation: CAA77942.1.
L22524 expand/collapse EMBL AC list , L22519, L22520, L22521, L22522, L22523 Genomic DNA. Translation: AAC37543.1.
AY795972 Genomic DNA. Translation: AAV40839.1.
BC003635 mRNA. Translation: AAH03635.1.
PIRKCHUM. B28816.
RefSeqNP_002414.1. NM_002423.3.
UniGeneHs.2256.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MMPX-ray2.30A/B95-264[»]
1MMQX-ray1.90A95-264[»]
1MMRX-ray2.40A95-264[»]
2DDYNMR-A95-267[»]
2Y6CX-ray1.70A95-258[»]
2Y6DX-ray1.60A95-267[»]
ProteinModelPortalP09237.
SMRP09237. Positions 33-262.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110459. 4 interactions.
IntActP09237. 1 interaction.
MINTMINT-7709639.
STRING9606.ENSP00000260227.

Chemistry

BindingDBP09237.
ChEMBLCHEMBL4073.

Protein family/group databases

MEROPSM10.008.

PTM databases

PhosphoSiteP09237.

Polymorphism databases

DMDM116861.

Proteomic databases

PaxDbP09237.
PRIDEP09237.

Protocols and materials databases

DNASU4316.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260227; ENSP00000260227; ENSG00000137673.
GeneID4316.
KEGGhsa:4316.
UCSCuc001phb.3. human.

Organism-specific databases

CTD4316.
GeneCardsGC11M102425.
HGNCHGNC:7174. MMP7.
HPACAB025869.
MIM178990. gene.
neXtProtNX_P09237.
PharmGKBPA30887.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG312228.
HOGENOMHOG000239471.
HOVERGENHBG052484.
InParanoidP09237.
KOK01397.
OMAYPTYGNG.
OrthoDBEOG7XPZ57.
PhylomeDBP09237.
TreeFamTF315428.

Enzyme and pathway databases

BRENDA3.4.24.23. 2681.
ReactomeREACT_118779. Extracellular matrix organization.
SABIO-RKP09237.

Gene expression databases

ArrayExpressP09237.
BgeeP09237.
CleanExHS_MMP7.
GenevestigatorP09237.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR028707. 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]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF34. PTHR10201:SF34. 1 hit.
PfamPF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09237.
GeneWikiMMP7.
GenomeRNAi4316.
NextBio16981.
PMAP-CutDBP09237.
PROP09237.
SOURCESearch...

Entry information

Entry nameMMP7_HUMAN
AccessionPrimary (citable) accession number: P09237
Secondary accession number(s): Q9BTK9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM