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P03957

- MMP3_RAT

UniProt

P03957 - MMP3_RAT

Protein

Stromelysin-1

Gene

Mmp3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (23 Oct 1986)
      Previous versions | rss
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    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 bindingi90 – 901Zinc 2; in inhibited formBy similarity
    Metal bindingi122 – 1221Calcium 1By similarity
    Metal bindingi156 – 1561Calcium 2By similarity
    Metal bindingi166 – 1661Zinc 1By similarity
    Metal bindingi168 – 1681Zinc 1By similarity
    Metal bindingi173 – 1731Calcium 3By similarity
    Metal bindingi174 – 1741Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi176 – 1761Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi178 – 1781Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi181 – 1811Zinc 1By similarity
    Metal bindingi188 – 1881Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi190 – 1901Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi192 – 1921Calcium 2By similarity
    Metal bindingi194 – 1941Zinc 1By similarity
    Metal bindingi196 – 1961Calcium 3By similarity
    Metal bindingi197 – 1971Calcium 1By similarity
    Metal bindingi199 – 1991Calcium 1By similarity
    Metal bindingi199 – 1991Calcium 3By similarity
    Metal bindingi216 – 2161Zinc 2; catalyticBy similarity
    Active sitei217 – 2171
    Metal bindingi220 – 2201Zinc 2; catalyticBy similarity
    Metal bindingi226 – 2261Zinc 2; catalyticBy similarity
    Metal bindingi295 – 2951Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi387 – 3871Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi436 – 4361Calcium 4; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: InterPro
    3. protein complex binding Source: RGD
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to cell-matrix adhesion Source: RGD
    2. cellular response to interleukin-1 Source: RGD
    3. collagen catabolic process Source: UniProtKB-KW
    4. female pregnancy Source: RGD
    5. response to amino acid Source: RGD
    6. response to cytokine Source: RGD
    7. response to estradiol Source: RGD
    8. response to hypoxia Source: RGD
    9. response to interleukin-1 Source: RGD
    10. response to lipopolysaccharide Source: RGD
    11. response to tumor necrosis factor Source: RGD
    12. wound healing Source: RGD

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    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):
    Matrix metalloproteinase-3
    Short name:
    MMP-3
    PTR1 protein
    Transin-1
    Gene namesi
    Name:Mmp3
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621317. Mmp3.

    Subcellular locationi

    GO - Cellular componenti

    1. cell body Source: RGD
    2. dendrite Source: RGD
    3. extracellular space Source: RGD
    4. nucleus Source: RGD
    5. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    6. protein complex Source: RGD

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717CuratedAdd
    BLAST
    Propeptidei18 – 9780Activation peptidePRO_0000028734Add
    BLAST
    Chaini98 – 475378Stromelysin-1PRO_0000028735Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi288 ↔ 475By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP03957.
    PRIDEiP03957.

    Expressioni

    Inductioni

    By epidermal growth factor and is increased in FR3T3 and RAT-1 fibroblasts transformed by polyoma virus, Rous sarcoma virus, or the human cellular H-Ras oncogene.

    Gene expression databases

    GenevestigatoriP03957.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000012310.

    Structurei

    3D structure databases

    ProteinModelPortaliP03957.
    SMRiP03957. Positions 31-264.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati285 – 33450Hemopexin 1Add
    BLAST
    Repeati335 – 38147Hemopexin 2Add
    BLAST
    Repeati383 – 43149Hemopexin 3Add
    BLAST
    Repeati432 – 47544Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi88 – 958Cysteine 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.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiP03957.
    PhylomeDBiP03957.

    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.

    P03957-1 [UniParc]FASTAAdd to Basket

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    MKGLPVLLWL CTAVCSSYPL HGSEEDAGME VLQKYLENYY GLEKDVKQFT    50
    KKKDSSPVVK KIQEMQKFLG LKMTGKLDSN TMELMHKPRC GVPDVGGFST 100
    FPGSPKWRKN HISYRIVNYT LDLPRESVDS AIERALKVWE EVTPLTFSRI 150
    SEGEADIMIS FAVEEHGDFI PFDGPGMVLA HAYAPGPGTN GDAHFDDDER 200
    WTDDVTGTNL FLVAAHELGH SLGLFHSANA EALMYPVYKS STDLARFHLS 250
    QDDVDGIQSL YGPPTESPDV LVVPTKSNSL DPETLPMCSS ALSFDAVSTL 300
    RGEVLFFKDR HFWRKSLRTP EPGFYLISSF WPSLPSNMDA AYEVTNRDTV 350
    FILKGNQIWA IRGHEELAGY PKSIHTLGLP ETVQKIDAAI SLKDQKKTYF 400
    FVEDKFWRFD EKKQSMDPEF PRKIAENFPG IGTKVDAVFE AFGFLYFFSG 450
    SSQLEFDPNA GKVTHILKSN SWFNC 475
    Length:475
    Mass (Da):53,428
    Last modified:October 23, 1986 - v1
    Checksum:iD81239DC3E26782E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02601 mRNA. Translation: CAA26448.1.
    PIRiA00997. KCRTIH.
    UniGeneiRn.32086.

    Genome annotation databases

    UCSCiRGD:621317. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02601 mRNA. Translation: CAA26448.1 .
    PIRi A00997. KCRTIH.
    UniGenei Rn.32086.

    3D structure databases

    ProteinModelPortali P03957.
    SMRi P03957. Positions 31-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000012310.

    Protein family/group databases

    MEROPSi M10.005.

    Proteomic databases

    PaxDbi P03957.
    PRIDEi P03957.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:621317. rat.

    Organism-specific databases

    RGDi 621317. Mmp3.

    Phylogenomic databases

    eggNOGi NOG258253.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi P03957.
    PhylomeDBi P03957.

    Miscellaneous databases

    NextBioi 13948460.
    PROi P03957.

    Gene expression databases

    Genevestigatori P03957.

    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. "Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts."
      Matrisian L.M., Glaichenhaus N., Gesnel M.-C., Breathnach R.
      EMBO J. 4:1435-1440(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Isolation of the oncogene and epidermal growth factor-induced transin gene: complex control in rat fibroblasts."
      Matrisian L.M., Gleroy P., Ruhlmann C., Gesnel M.-C., Breathnach R.
      Mol. Cell. Biol. 6:1679-1686(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Purification and properties of extracellular matrix-degrading metallo-proteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin."
      Umenishi F., Yasumitsu H., Ashida Y., Yamauti J., Umeda M., Miyazaki K.
      J. Biochem. 108:537-543(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-28; 110-119; 309-315 AND 316-325.
    4. "Structure-function relationships in the collagenase family member transin."
      Sanchez-Lopez R., Nicholson R., Gesnel M.-C., Matrisian L.M., Breathnach R.
      J. Biol. Chem. 263:11892-11899(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS, CHARACTERIZATION.

    Entry informationi

    Entry nameiMMP3_RAT
    AccessioniPrimary (citable) accession number: P03957
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 1986
    Last sequence update: October 23, 1986
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3