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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)DescriptionActionsGraphical viewLength
Metal bindingi87Zinc 2; in inhibited formBy similarity1
Metal bindingi153Calcium 11
Metal bindingi163Zinc 11
Metal bindingi165Zinc 11
Metal bindingi170Calcium 21
Metal bindingi171Calcium 2; via carbonyl oxygen1
Metal bindingi173Calcium 2; via carbonyl oxygen1
Metal bindingi175Calcium 2; via carbonyl oxygen1
Metal bindingi178Zinc 11
Metal bindingi185Calcium 1; via carbonyl oxygen1
Metal bindingi187Calcium 1; via carbonyl oxygen1
Metal bindingi189Calcium 11
Metal bindingi191Zinc 11
Metal bindingi193Calcium 21
Metal bindingi196Calcium 21
Metal bindingi214Zinc 2; catalytic1
Active sitei2151
Metal bindingi218Zinc 2; catalytic1
Metal bindingi224Zinc 2; catalytic1

GO - Molecular functioni

  • heparin binding Source: Ensembl
  • metalloendopeptidase activity Source: ProtInc
  • serine-type endopeptidase activity Source: Reactome
  • 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

BioCyciZFISH:HS06371-MONOMER.
BRENDAi3.4.24.23. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
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
Proteomesi
  • UP000005640 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

DisGeNETi4316.
OpenTargetsiENSG00000137673.
PharmGKBiPA30887.

Chemistry databases

ChEMBLiCHEMBL4073.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1631.

Polymorphism and mutation databases

BioMutaiMMP7.
DMDMi116861.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
PropeptideiPRO_000002873818 – 94Activation peptideAdd BLAST77
ChainiPRO_000002873995 – 267MatrilysinAdd BLAST173

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiP09237.
PeptideAtlasiP09237.
PRIDEiP09237.

PTM databases

iPTMnetiP09237.
PhosphoSitePlusiP09237.

Miscellaneous databases

PMAP-CutDBP09237.

Expressioni

Gene expression databases

BgeeiENSG00000137673.
CleanExiHS_MMP7.
GenevisibleiP09237. HS.

Organism-specific databases

HPAiCAB025869.
HPA051358.

Interactioni

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP09237.

Structurei

Secondary structure

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi24 – 26Combined sources3
Helixi29 – 41Combined sources13
Turni47 – 49Combined sources3
Helixi53 – 66Combined sources14
Helixi77 – 83Combined sources7
Beta strandi99 – 103Combined sources5
Beta strandi106 – 113Combined sources8
Beta strandi118 – 120Combined sources3
Helixi122 – 137Combined sources16
Beta strandi143 – 146Combined sources4
Beta strandi148 – 150Combined sources3
Beta strandi153 – 159Combined sources7
Beta strandi164 – 166Combined sources3
Beta strandi171 – 174Combined sources4
Beta strandi177 – 179Combined sources3
Beta strandi182 – 184Combined sources3
Turni185 – 188Combined sources4
Beta strandi190 – 193Combined sources4
Beta strandi198 – 207Combined sources10
Helixi208 – 219Combined sources12
Beta strandi233 – 236Combined sources4
Beta strandi241 – 243Combined sources3
Helixi248 – 257Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MMPX-ray2.30A/B95-264[»]
1MMQX-ray1.90A95-264[»]
1MMRX-ray2.40A95-264[»]
2DDYNMR-A95-267[»]
2MZENMR-A18-267[»]
2MZHNMR-A20-267[»]
2MZINMR-A18-267[»]
2Y6CX-ray1.70A95-258[»]
2Y6DX-ray1.60A95-267[»]
ProteinModelPortaliP09237.
SMRiP09237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09237.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi85 – 92Cysteine switchBy similarity8

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.
GeneTreeiENSGT00860000133713.
HOGENOMiHOG000239471.
HOVERGENiHBG052484.
InParanoidiP09237.
KOiK01397.
OMAiGAHGDSY.
OrthoDBiEOG091G03DP.
PhylomeDBiP09237.
TreeFamiTF315428.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di3.40.390.10. 1 hit.
InterProiIPR033739. M10A_MMP.
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]
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.

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_00672977R → H.1 PublicationCorresponds to variant rs10502001dbSNPEnsembl.1
Natural variantiVAR_021027137G → D.1 PublicationCorresponds to variant rs17884789dbSNPEnsembl.1
Natural variantiVAR_021028241P → L.1 PublicationCorresponds to variant rs17886506dbSNPEnsembl.1

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_002423.4.
UniGeneiHs.2256.

Genome annotation databases

EnsembliENST00000260227; ENSP00000260227; ENSG00000137673.
GeneIDi4316.
KEGGihsa:4316.
UCSCiuc001phb.4. 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_002423.4.
UniGeneiHs.2256.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MMPX-ray2.30A/B95-264[»]
1MMQX-ray1.90A95-264[»]
1MMRX-ray2.40A95-264[»]
2DDYNMR-A95-267[»]
2MZENMR-A18-267[»]
2MZHNMR-A20-267[»]
2MZINMR-A18-267[»]
2Y6CX-ray1.70A95-258[»]
2Y6DX-ray1.60A95-267[»]
ProteinModelPortaliP09237.
SMRiP09237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP09237.
ChEMBLiCHEMBL4073.
DrugBankiDB00786. Marimastat.
GuidetoPHARMACOLOGYi1631.

Protein family/group databases

MEROPSiM10.008.

PTM databases

iPTMnetiP09237.
PhosphoSitePlusiP09237.

Polymorphism and mutation databases

BioMutaiMMP7.
DMDMi116861.

Proteomic databases

PaxDbiP09237.
PeptideAtlasiP09237.
PRIDEiP09237.

Protocols and materials databases

DNASUi4316.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260227; ENSP00000260227; ENSG00000137673.
GeneIDi4316.
KEGGihsa:4316.
UCSCiuc001phb.4. human.

Organism-specific databases

CTDi4316.
DisGeNETi4316.
GeneCardsiMMP7.
HGNCiHGNC:7174. MMP7.
HPAiCAB025869.
HPA051358.
MIMi178990. gene.
neXtProtiNX_P09237.
OpenTargetsiENSG00000137673.
PharmGKBiPA30887.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00860000133713.
HOGENOMiHOG000239471.
HOVERGENiHBG052484.
InParanoidiP09237.
KOiK01397.
OMAiGAHGDSY.
OrthoDBiEOG091G03DP.
PhylomeDBiP09237.
TreeFamiTF315428.

Enzyme and pathway databases

BioCyciZFISH:HS06371-MONOMER.
BRENDAi3.4.24.23. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
SABIO-RKP09237.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000137673.
CleanExiHS_MMP7.
GenevisibleiP09237. HS.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di3.40.390.10. 1 hit.
InterProiIPR033739. M10A_MMP.
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]
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...

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: November 30, 2016
This is version 181 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

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.