Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P28862

- MMP3_MOUSE

UniProt

P28862 - MMP3_MOUSE

Protein

Stromelysin-1

Gene

Mmp3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (01 Feb 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.

    Catalytic activityi

    Preferential cleavage where P1', P2' and P3' are hydrophobic residues.

    Cofactori

    Binds 4 calcium ions per subunit.By similarity
    Binds 2 zinc ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi92 – 921Zinc 2; in inhibited formBy similarity
    Metal bindingi124 – 1241Calcium 1By similarity
    Metal bindingi158 – 1581Calcium 2By similarity
    Metal bindingi168 – 1681Zinc 1By similarity
    Metal bindingi170 – 1701Zinc 1By similarity
    Metal bindingi175 – 1751Calcium 3By similarity
    Metal bindingi176 – 1761Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi178 – 1781Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi180 – 1801Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi183 – 1831Zinc 1By similarity
    Metal bindingi190 – 1901Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi192 – 1921Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi194 – 1941Calcium 2By similarity
    Metal bindingi196 – 1961Zinc 1By similarity
    Metal bindingi198 – 1981Calcium 3By similarity
    Metal bindingi199 – 1991Calcium 1By similarity
    Metal bindingi201 – 2011Calcium 1By similarity
    Metal bindingi201 – 2011Calcium 3By similarity
    Metal bindingi218 – 2181Zinc 2; catalyticBy similarity
    Active sitei219 – 2191PROSITE-ProRule annotation
    Metal bindingi222 – 2221Zinc 2; catalyticBy similarity
    Metal bindingi228 – 2281Zinc 2; catalyticBy similarity
    Metal bindingi297 – 2971Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi389 – 3891Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi438 – 4381Calcium 4; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to amino acid stimulus Source: MGI
    2. cellular response to oxidative stress Source: ParkinsonsUK-UCL
    3. collagen catabolic process Source: UniProtKB-KW
    4. negative regulation of protein kinase B signaling Source: ParkinsonsUK-UCL
    5. protein catabolic process Source: ParkinsonsUK-UCL
    6. proteolysis Source: ParkinsonsUK-UCL
    7. regulation of cell migration Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198350. EGFR Transactivation by Gastrin.
    REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stromelysin-1 (EC:3.4.24.17)
    Short name:
    SL-1
    Alternative name(s):
    EMS-2
    Matrix metalloproteinase-3
    Short name:
    MMP-3
    Transin-1
    Gene namesi
    Name:Mmp3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:97010. Mmp3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: ParkinsonsUK-UCL
    2. extracellular region Source: Reactome
    3. mitochondrion Source: ParkinsonsUK-UCL
    4. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717CuratedAdd
    BLAST
    Propeptidei18 – 9982Activation peptidePRO_0000028730Add
    BLAST
    Chaini100 – 477378Stromelysin-1PRO_0000028731Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi290 ↔ 477By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRIDEiP28862.

    PTM databases

    PhosphoSiteiP28862.

    Expressioni

    Developmental stagei

    Present in unfertilized eggs and at the zygote and cleavage stages. Levels increase at the blastocyst stage and with endoderm differentiation.1 Publication

    Gene expression databases

    ArrayExpressiP28862.
    BgeeiP28862.
    CleanExiMM_MMP3.
    GenevestigatoriP28862.

    Structurei

    3D structure databases

    ProteinModelPortaliP28862.
    SMRiP28862. Positions 32-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati287 – 33650Hemopexin 1Add
    BLAST
    Repeati337 – 38347Hemopexin 2Add
    BLAST
    Repeati385 – 43349Hemopexin 3Add
    BLAST
    Repeati434 – 47744Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi90 – 978Cysteine 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
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG258253.
    HOVERGENiHBG052484.
    InParanoidiP28862.
    KOiK01394.

    Family and domain databases

    Gene3Di2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    IPR028700. Stromelysin_1.
    [Graphical view]
    PANTHERiPTHR10201:SF38. PTHR10201:SF38. 1 hit.
    PfamiPF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P28862-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGLPVLLWL CVVVCSSYPL HDSARDDDAG MELLQKYLEN YYGLAKDVKQ    50
    FIKKKDSSLI VKKIQEMQKF LGLEMTGKLD SNTMELMHKP RCGVPDVGGF 100
    STFPGSPKWR KSHITYRIVN YTPDLPRQSV DSAIEKALKV WEEVTPLTFS 150
    RISEGEADIM ISFAVGEHGD FVPFDGPGTV LAHAYAPGPG INGDAHFDDD 200
    ERWTEDVTGT NLFLVAAHEL GHSLGLYHSA KAEALMYPVY KSSTDLSRFH 250
    LSQDDVDGIQ SLYGTPTASP DVLVVPTKSN SLEPETSPMC SSTLFFDAVS 300
    TLRGEVLFFK DRHFWRKSLR TPEPEFYLIS SFWPSLPSNM DAAYEVTNRD 350
    TVFIFKGNQF WAIRGHEELA GYPKSIHTLG LPATVKKIDA AISNKEKRKT 400
    YFFVEDKYWR FDEKKQSMEP GFPRKIAEDF PGVDSRVDAV FEAFGFLYFF 450
    SGSSQLEFDP NAKKVTHILK SNSWFNC 477
    Length:477
    Mass (Da):53,845
    Last modified:February 1, 1994 - v2
    Checksum:i9C15594F45262D37
    GO

    Sequence cautioni

    The sequence CAA44860.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti468 – 4681I → T(PubMed:2744464)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66402 mRNA. Translation: CAA47029.1.
    X63162 mRNA. Translation: CAA44860.1. Different initiation.
    PIRiJC1476. KCMSS1.
    RefSeqiNP_034939.1. NM_010809.1.
    UniGeneiMm.4993.

    Genome annotation databases

    GeneIDi17392.
    KEGGimmu:17392.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66402 mRNA. Translation: CAA47029.1 .
    X63162 mRNA. Translation: CAA44860.1 . Different initiation.
    PIRi JC1476. KCMSS1.
    RefSeqi NP_034939.1. NM_010809.1.
    UniGenei Mm.4993.

    3D structure databases

    ProteinModelPortali P28862.
    SMRi P28862. Positions 32-477.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M10.005.

    PTM databases

    PhosphoSitei P28862.

    Proteomic databases

    PRIDEi P28862.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 17392.
    KEGGi mmu:17392.

    Organism-specific databases

    CTDi 4314.
    MGIi MGI:97010. Mmp3.

    Phylogenomic databases

    eggNOGi NOG258253.
    HOVERGENi HBG052484.
    InParanoidi P28862.
    KOi K01394.

    Enzyme and pathway databases

    Reactomei REACT_198350. EGFR Transactivation by Gastrin.
    REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    NextBioi 292020.
    PROi P28862.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28862.
    Bgeei P28862.
    CleanExi MM_MMP3.
    Genevestigatori P28862.

    Family and domain databases

    Gene3Di 2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    IPR028700. Stromelysin_1.
    [Graphical view ]
    PANTHERi PTHR10201:SF38. PTHR10201:SF38. 1 hit.
    Pfami PF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a cDNA encoding mouse stromelysin 1."
      Hammani K., Henriet P., Eeckhout Y.
      Gene 120:321-322(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NMRI.
      Tissue: Calvaria.
    2. Li F., Strange R., Saurer S., Niemann H., Friis R.R.
      Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Swiss.
    3. "Genes for extracellular-matrix-degrading metalloproteinases and their inhibitor, TIMP, are expressed during early mammalian development."
      Brenner C.A., Adler R.R., Rappolee D.A., Pedersen R.A., Werb Z.
      Genes Dev. 3:848-859(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 415-469, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiMMP3_MOUSE
    AccessioniPrimary (citable) accession number: P28862
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3