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Q499S5

- MMP11_RAT

UniProt

Q499S5 - MMP11_RAT

Protein

Stromelysin-3

Gene

Mmp11

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (13 Sep 2005)
      Previous versions | rss
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    Functioni

    May play an important role in the progression of epithelial malignancies.By similarity

    Cofactori

    Binds 1 calcium ion per subunit.
    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi84 – 841Zinc 2; in inhibited formBy similarity
    Metal bindingi168 – 1681Zinc 1By similarity
    Metal bindingi170 – 1701Zinc 1By similarity
    Metal bindingi175 – 1751CalciumBy similarity
    Metal bindingi176 – 1761Calcium; via carbonyl oxygenBy similarity
    Metal bindingi178 – 1781Calcium; via carbonyl oxygenBy similarity
    Metal bindingi180 – 1801Calcium; via carbonyl oxygenBy similarity
    Metal bindingi183 – 1831Zinc 1By similarity
    Metal bindingi196 – 1961Zinc 1By similarity
    Metal bindingi218 – 2181Zinc 2; catalyticBy similarity
    Active sitei219 – 2191PROSITE-ProRule annotation
    Metal bindingi222 – 2221Zinc 2; catalyticBy similarity
    Metal bindingi228 – 2281Zinc 2; catalyticBy 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. basement membrane organization Source: Ensembl
    2. collagen catabolic process Source: UniProtKB-KW
    3. collagen fibril organization Source: Ensembl
    4. multicellular organismal development Source: InterPro
    5. negative regulation of fat cell differentiation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198590. Activation of Matrix Metalloproteinases.
    REACT_199177. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stromelysin-3 (EC:3.4.24.-)
    Short name:
    SL-3
    Short name:
    ST3
    Alternative name(s):
    Matrix metalloproteinase-11
    Short name:
    MMP-11
    Gene namesi
    Name:Mmp11
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 20

    Organism-specific databases

    RGDi3099. Mmp11.

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Sequence AnalysisAdd
    BLAST
    Propeptidei36 – 10166Activation peptideBy similarityPRO_0000042649Add
    BLAST
    Chaini102 – 491390Stromelysin-3PRO_0000042650Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi297 ↔ 483By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.1 Publication

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiQ499S5.
    PRIDEiQ499S5.

    PTM databases

    PhosphoSiteiQ499S5.

    Expressioni

    Tissue specificityi

    Highly expressed in ovary and uterus.1 Publication

    Inductioni

    In skin fibroblasts of superficial dermis upon skin lesion with highest level between days 5-10.1 Publication

    Gene expression databases

    GenevestigatoriQ499S5.

    Interactioni

    Protein-protein interaction databases

    BioGridi247514. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ499S5.
    SMRiQ499S5. Positions 102-264.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati298 – 34245Hemopexin 1Add
    BLAST
    Repeati343 – 38543Hemopexin 2Add
    BLAST
    Repeati387 – 43549Hemopexin 3Add
    BLAST
    Repeati436 – 48348Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi82 – 898Cysteine 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

    eggNOGiNOG236137.
    GeneTreeiENSGT00750000117332.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiQ499S5.
    KOiK07993.
    OMAiVDTNEIA.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiQ499S5.

    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.
    IPR006026. Peptidase_Metallo.
    IPR028705. Stromelysin-3.
    [Graphical view]
    PANTHERiPTHR10201:SF20. PTHR10201:SF20. 1 hit.
    PfamiPF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50923. SSF50923. 1 hit.
    PROSITEiPS00024. 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.

    Q499S5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARAACLLRA ISRALLLPLP LLLLLLLLLP PQLMARARPP ENHRHRPVKR    50
    VPQLLPAALP NSLPSVPASH WVPGPASSSR PLRCGVPDPP DVLNARNRQK 100
    RFVLSGGRWE KTDLTYRILR FPWQLVREQV RQTVAEALRV WSEVTPLTFT 150
    EVHEGRADIM IDFTRYWHGD NLPFDGPGGI LAHAFFPKTH REGDVHFDYD 200
    ETWTIGDKGT DLLQVAAHEF GHVLGLQHTT AAKALMSPFY TFRYPLSLSP 250
    DDRRGIQHLY GRPQLTPTSP TPTLSSQAGT DTNEIALQEP EVPPEVCETS 300
    FDAVSTIRGE LFFFKAGFVW RLRSGQLQPG YPALASRHWQ GLPSPVDAAF 350
    EDAQGQIWFF QGAQYWVYDG EKPVLGPAPL SKLGLQGSPV HAALVWGPEK 400
    NKIYFFRGGD YWRFHPRTQR VDNPVPRRTT DWRGVPSEID AAFQDAEGYA 450
    YFLRGHLYWK FDPVKVKVLE SFPRPIGPDF FDCAEPANTF R 491
    Length:491
    Mass (Da):55,511
    Last modified:September 13, 2005 - v1
    Checksum:iB0C5B191A623FD41
    GO

    Sequence cautioni

    The sequence AAC53061.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH99781.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46034 mRNA. Translation: AAC53061.1. Different initiation.
    BC099781 mRNA. Translation: AAH99781.2. Different initiation.
    RefSeqiNP_037112.2. NM_012980.2.
    UniGeneiRn.11123.

    Genome annotation databases

    EnsembliENSRNOT00000031400; ENSRNOP00000035334; ENSRNOG00000028344.
    GeneIDi25481.
    KEGGirno:25481.
    UCSCiRGD:3099. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46034 mRNA. Translation: AAC53061.1 . Different initiation.
    BC099781 mRNA. Translation: AAH99781.2 . Different initiation.
    RefSeqi NP_037112.2. NM_012980.2.
    UniGenei Rn.11123.

    3D structure databases

    ProteinModelPortali Q499S5.
    SMRi Q499S5. Positions 102-264.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247514. 2 interactions.

    Protein family/group databases

    MEROPSi M10.007.

    PTM databases

    PhosphoSitei Q499S5.

    Proteomic databases

    PaxDbi Q499S5.
    PRIDEi Q499S5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000031400 ; ENSRNOP00000035334 ; ENSRNOG00000028344 .
    GeneIDi 25481.
    KEGGi rno:25481.
    UCSCi RGD:3099. rat.

    Organism-specific databases

    CTDi 4320.
    RGDi 3099. Mmp11.

    Phylogenomic databases

    eggNOGi NOG236137.
    GeneTreei ENSGT00750000117332.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi Q499S5.
    KOi K07993.
    OMAi VDTNEIA.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi Q499S5.

    Enzyme and pathway databases

    Reactomei REACT_198590. Activation of Matrix Metalloproteinases.
    REACT_199177. Collagen degradation.

    Miscellaneous databases

    NextBioi 606819.
    PROi Q499S5.

    Gene expression databases

    Genevestigatori Q499S5.

    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.
    IPR006026. Peptidase_Metallo.
    IPR028705. Stromelysin-3.
    [Graphical view ]
    PANTHERi PTHR10201:SF20. PTHR10201:SF20. 1 hit.
    Pfami PF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 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 SSF50923. SSF50923. 1 hit.
    PROSITEi PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rat stromelysin 3: cDNA cloning from healing skin wound, activation by furin and expression in rat tissues."
      Okada A., Saez S., Misumi Y., Basset P.
      Gene 185:187-193(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, PROTEOLYTIC PROCESSING.
      Strain: Wistar.
    2. "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: Prostate.

    Entry informationi

    Entry nameiMMP11_RAT
    AccessioniPrimary (citable) accession number: Q499S5
    Secondary accession number(s): P97568
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 76 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, 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