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Protein

Matrilysin

Gene

MMP7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 2 calcium ions per subunit.
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871Zinc 2; in inhibited formBy 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

  • heparin binding Source: Ensembl
  • metalloendopeptidase activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

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 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7174. MMP7.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: ProtInc
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30887.

Chemistry

DrugBankiDB00786. Marimastat.

Polymorphism and mutation databases

BioMutaiMMP7.
DMDMi116861.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17171 PublicationAdd
BLAST
Propeptidei18 – 9477Activation peptidePRO_0000028738Add
BLAST
Chaini95 – 267173MatrilysinPRO_0000028739Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiP09237.
PRIDEiP09237.

PTM databases

PhosphoSiteiP09237.

Miscellaneous databases

PMAP-CutDBP09237.

Expressioni

Gene expression databases

BgeeiP09237.
CleanExiHS_MMP7.
GenevisibleiP09237. HS.

Organism-specific databases

HPAiCAB025869.
HPA051358.

Interactioni

Protein-protein interaction databases

BioGridi110459. 23 interactions.
IntActiP09237. 2 interactions.
MINTiMINT-7709639.
STRINGi9606.ENSP00000260227.

Structurei

Secondary structure

1
267
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi106 – 1138Combined sources
Beta strandi118 – 1203Combined sources
Helixi122 – 13716Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi153 – 1597Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi171 – 1744Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi182 – 1843Combined sources
Turni185 – 1884Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi198 – 20710Combined sources
Helixi208 – 21912Combined sources
Beta strandi233 – 2364Combined sources
Beta strandi241 – 2433Combined sources
Helixi248 – 25710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09237.

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.
GeneTreeiENSGT00760000119132.
HOGENOMiHOG000239471.
HOVERGENiHBG052484.
InParanoidiP09237.
KOiK01397.
OMAiGAHGDSY.
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

        10         20         30         40         50
MRLTVLCAVC LLPGSLALPL PQEAGGMSEL QWEQAQDYLK RFYLYDSETK
60 70 80 90 100
NANSLEAKLK EMQKFFGLPI TGMLNSRVIE IMQKPRCGVP DVAEYSLFPN
110 120 130 140 150
SPKWTSKVVT YRIVSYTRDL PHITVDRLVS KALNMWGKEI PLHFRKVVWG
160 170 180 190 200
TADIMIGFAR GAHGDSYPFD GPGNTLAHAF APGTGLGGDA HFDEDERWTD
210 220 230 240 250
GSSLGINFLY AATHELGHSL GMGHSSDPNA VMYPTYGNGD PQNFKLSQDD
260
IKGIQKLYGK RSNSRKK
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110459. 23 interactions.
IntActiP09237. 2 interactions.
MINTiMINT-7709639.
STRINGi9606.ENSP00000260227.

Chemistry

BindingDBiP09237.
ChEMBLiCHEMBL4073.
DrugBankiDB00786. Marimastat.

Protein family/group databases

MEROPSiM10.008.

PTM databases

PhosphoSiteiP09237.

Polymorphism and mutation databases

BioMutaiMMP7.
DMDMi116861.

Proteomic databases

PaxDbiP09237.
PRIDEiP09237.

Protocols and materials databases

DNASUi4316.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4316.
GeneCardsiGC11M102425.
HGNCiHGNC:7174. MMP7.
HPAiCAB025869.
HPA051358.
MIMi178990. gene.
neXtProtiNX_P09237.
PharmGKBiPA30887.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG312228.
GeneTreeiENSGT00760000119132.
HOGENOMiHOG000239471.
HOVERGENiHBG052484.
InParanoidiP09237.
KOiK01397.
OMAiGAHGDSY.
OrthoDBiEOG7XPZ57.
PhylomeDBiP09237.
TreeFamiTF315428.

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.

Miscellaneous databases

ChiTaRSiMMP7. human.
EvolutionaryTraceiP09237.
GeneWikiiMMP7.
GenomeRNAii4316.
NextBioi16981.
PMAP-CutDBP09237.
PROiP09237.
SOURCEiSearch...

Gene expression databases

BgeeiP09237.
CleanExiHS_MMP7.
GenevisibleiP09237. HS.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 168 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

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 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.