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P09237

- MMP7_HUMAN

UniProt

P09237 - MMP7_HUMAN

Protein

Matrilysin

Gene

MMP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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 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

    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

    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

    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 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

    ArrayExpressiP09237.
    BgeeiP09237.
    CleanExiHS_MMP7.
    GenevestigatoriP09237.

    Organism-specific databases

    HPAiCAB025869.

    Interactioni

    Protein-protein interaction databases

    BioGridi110459. 4 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 – 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.
    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.
    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. 2 interactions.
    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

    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: October 1, 2014
    This is version 160 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