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P09237

- MMP7_HUMAN

UniProt

P09237 - MMP7_HUMAN

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Protein
Matrilysin
Gene
MMP7, MPSL1, PUMP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.1 Publication

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.
Binds 2 zinc ions per subunit.

Sites

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

GO - Molecular functioni

  1. metalloendopeptidase activity Source: ProtInc
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. antibacterial peptide secretion Source: Ensembl
  2. collagen catabolic process Source: Reactome
  3. defense response to Gram-negative bacterium Source: Ensembl
  4. defense response to Gram-positive bacterium Source: Ensembl
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. proteolysis Source: ProtInc
  8. regulation of cell proliferation Source: Ensembl
  9. response to drug Source: Ensembl
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. 2681.
ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
SABIO-RKP09237.

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:MPSL1, PUMP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:7174. MMP7.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: ProtInc
  3. extracellular vesicular exosome Source: UniProt
  4. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30887.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 Publication
Add
BLAST
Propeptidei18 – 9477Activation peptide
PRO_0000028738Add
BLAST
Chaini95 – 267173Matrilysin
PRO_0000028739Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiP09237.
PRIDEiP09237.

PTM databases

PhosphoSiteiP09237.

Miscellaneous databases

PMAP-CutDBP09237.

Expressioni

Gene expression databases

ArrayExpressiP09237.
BgeeiP09237.
CleanExiHS_MMP7.
GenevestigatoriP09237.

Organism-specific databases

HPAiCAB025869.

Interactioni

Protein-protein interaction databases

BioGridi110459. 4 interactions.
IntActiP09237. 1 interaction.
MINTiMINT-7709639.
STRINGi9606.ENSP00000260227.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi106 – 1138
Beta strandi118 – 1203
Helixi122 – 13716
Beta strandi143 – 1464
Beta strandi148 – 1503
Beta strandi153 – 1597
Beta strandi164 – 1663
Beta strandi171 – 1744
Beta strandi177 – 1793
Beta strandi182 – 1843
Turni185 – 1884
Beta strandi190 – 1934
Beta strandi198 – 20710
Helixi208 – 21912
Beta strandi233 – 2364
Beta strandi241 – 2433
Helixi248 – 25710

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP09237.
SMRiP09237. Positions 33-263.

Miscellaneous databases

EvolutionaryTraceiP09237.

Family & Domainsi

Motif

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG312228.
HOGENOMiHOG000239471.
HOVERGENiHBG052484.
InParanoidiP09237.
KOiK01397.
OMAiYPTYGNG.
OrthoDBiEOG7XPZ57.
PhylomeDBiP09237.
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: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.

P09237-1 [UniParc]FASTAAdd to Basket

« Hide

MRLTVLCAVC LLPGSLALPL PQEAGGMSEL QWEQAQDYLK RFYLYDSETK    50
NANSLEAKLK EMQKFFGLPI TGMLNSRVIE IMQKPRCGVP DVAEYSLFPN 100
SPKWTSKVVT YRIVSYTRDL PHITVDRLVS KALNMWGKEI PLHFRKVVWG 150
TADIMIGFAR GAHGDSYPFD GPGNTLAHAF APGTGLGGDA HFDEDERWTD 200
GSSLGINFLY AATHELGHSL GMGHSSDPNA VMYPTYGNGD PQNFKLSQDD 250
IKGIQKLYGK RSNSRKK 267
Length:267
Mass (Da):29,677
Last modified:July 1, 1989 - v1
Checksum:iF6BD1FC0ADA23603
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771R → H.1 Publication
Corresponds to variant rs10502001 [ dbSNP | Ensembl ].
VAR_006729
Natural varianti137 – 1371G → D.1 Publication
Corresponds to variant rs17884789 [ dbSNP | Ensembl ].
VAR_021027
Natural varianti241 – 2411P → L.1 Publication
Corresponds to variant rs17886506 [ dbSNP | Ensembl ].
VAR_021028

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07819 mRNA. Translation: CAA30678.1.
Z11887 mRNA. Translation: CAA77942.1.
L22524
, L22519, L22520, L22521, L22522, L22523 Genomic DNA. Translation: AAC37543.1.
AY795972 Genomic DNA. Translation: AAV40839.1.
BC003635 mRNA. Translation: AAH03635.1.
CCDSiCCDS8317.1.
PIRiB28816. KCHUM.
RefSeqiNP_002414.1. NM_002423.3.
UniGeneiHs.2256.

Genome annotation databases

EnsembliENST00000260227; ENSP00000260227; ENSG00000137673.
GeneIDi4316.
KEGGihsa:4316.
UCSCiuc001phb.3. human.

Polymorphism databases

DMDMi116861.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07819 mRNA. Translation: CAA30678.1 .
Z11887 mRNA. Translation: CAA77942.1 .
L22524
, L22519 , L22520 , L22521 , L22522 , L22523 Genomic DNA. Translation: AAC37543.1 .
AY795972 Genomic DNA. Translation: AAV40839.1 .
BC003635 mRNA. Translation: AAH03635.1 .
CCDSi CCDS8317.1.
PIRi B28816. KCHUM.
RefSeqi NP_002414.1. NM_002423.3.
UniGenei Hs.2256.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MMP X-ray 2.30 A/B 95-264 [» ]
1MMQ X-ray 1.90 A 95-264 [» ]
1MMR X-ray 2.40 A 95-264 [» ]
2DDY NMR - A 95-267 [» ]
2Y6C X-ray 1.70 A 95-258 [» ]
2Y6D X-ray 1.60 A 95-267 [» ]
ProteinModelPortali P09237.
SMRi P09237. Positions 33-263.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110459. 4 interactions.
IntActi P09237. 1 interaction.
MINTi MINT-7709639.
STRINGi 9606.ENSP00000260227.

Chemistry

BindingDBi P09237.
ChEMBLi CHEMBL4073.

Protein family/group databases

MEROPSi M10.008.

PTM databases

PhosphoSitei P09237.

Polymorphism databases

DMDMi 116861.

Proteomic databases

PaxDbi P09237.
PRIDEi P09237.

Protocols and materials databases

DNASUi 4316.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260227 ; ENSP00000260227 ; ENSG00000137673 .
GeneIDi 4316.
KEGGi hsa:4316.
UCSCi uc001phb.3. human.

Organism-specific databases

CTDi 4316.
GeneCardsi GC11M102425.
HGNCi HGNC:7174. MMP7.
HPAi CAB025869.
MIMi 178990. gene.
neXtProti NX_P09237.
PharmGKBi PA30887.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG312228.
HOGENOMi HOG000239471.
HOVERGENi HBG052484.
InParanoidi P09237.
KOi K01397.
OMAi YPTYGNG.
OrthoDBi EOG7XPZ57.
PhylomeDBi P09237.
TreeFami TF315428.

Enzyme and pathway databases

BRENDAi 3.4.24.23. 2681.
Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
SABIO-RK P09237.

Miscellaneous databases

EvolutionaryTracei P09237.
GeneWikii MMP7.
GenomeRNAii 4316.
NextBioi 16981.
PMAP-CutDB P09237.
PROi P09237.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09237.
Bgeei P09237.
CleanExi HS_MMP7.
Genevestigatori P09237.

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

« Hide 'large scale' publications
  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).

Entry informationi

Entry nameiMMP7_HUMAN
AccessioniPrimary (citable) accession number: P09237
Secondary accession number(s): Q9BTK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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