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P41246

- MMP9_RABIT

UniProt

P41246 - MMP9_RABIT

Protein

Matrix metalloproteinase-9

Gene

MMP9

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments By similarity.By similarity

    Catalytic activityi

    Cleavage of gelatin types I and V and collagen types IV and V.

    Cofactori

    Binds 2 zinc ions per subunit.By similarity
    Binds 3 calcium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi99 – 991Zinc 2; in inhibited formBy similarity
    Metal bindingi131 – 1311Calcium 1By similarity
    Metal bindingi165 – 1651Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi175 – 1751Zinc 1; structuralBy similarity
    Metal bindingi177 – 1771Zinc 1; structuralBy similarity
    Metal bindingi182 – 1821Calcium 3By similarity
    Metal bindingi183 – 1831Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi185 – 1851Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi187 – 1871Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi190 – 1901Zinc 1; structuralBy similarity
    Metal bindingi197 – 1971Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi199 – 1991Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi201 – 2011Calcium 2By similarity
    Metal bindingi203 – 2031Zinc 1; structuralBy similarity
    Metal bindingi205 – 2051Calcium 3By similarity
    Metal bindingi206 – 2061Calcium 1By similarity
    Metal bindingi208 – 2081Calcium 1By similarity
    Metal bindingi208 – 2081Calcium 3By similarity
    Metal bindingi401 – 4011Zinc 2; catalyticBy similarity
    Active sitei402 – 4021PROSITE-ProRule annotation
    Metal bindingi405 – 4051Zinc 2; catalyticBy similarity
    Metal bindingi411 – 4111Zinc 2; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. collagen catabolic process Source: UniProtKB-KW
    2. leukocyte migration Source: InterPro
    3. ossification Source: InterPro
    4. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM10.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-9 (EC:3.4.24.35)
    Short name:
    MMP-9
    Alternative name(s):
    92 kDa gelatinase
    92 kDa type IV collagenase
    Gelatinase B
    Short name:
    GELB
    Gene namesi
    Name:MMP9
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Propeptidei20 – 10687Activation peptideBy similarityPRO_0000028760Add
    BLAST
    Chaini107 – 707601Matrix metalloproteinase-9PRO_0000028761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi230 ↔ 256PROSITE-ProRule annotation
    Disulfide bondi244 ↔ 271PROSITE-ProRule annotation
    Disulfide bondi288 ↔ 314PROSITE-ProRule annotation
    Disulfide bondi302 ↔ 329PROSITE-ProRule annotation
    Disulfide bondi347 ↔ 373PROSITE-ProRule annotation
    Disulfide bondi361 ↔ 388PROSITE-ProRule annotation
    Disulfide bondi516 ↔ 704PROSITE-ProRule annotation

    Post-translational modificationi

    N- and O-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Expressioni

    Tissue specificityi

    Osteoclasts.

    Interactioni

    Subunit structurei

    Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with a 25 kDa protein. Interacts with ECM1.By similarity

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000025066.

    Structurei

    3D structure databases

    ProteinModelPortaliP41246.
    SMRiP41246. Positions 29-444, 513-707.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini225 – 27349Fibronectin type-II 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 33149Fibronectin type-II 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini342 – 39049Fibronectin type-II 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati518 – 56346Hemopexin 1Add
    BLAST
    Repeati564 – 60845Hemopexin 2Add
    BLAST
    Repeati610 – 65748Hemopexin 3Add
    BLAST
    Repeati658 – 70447Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi97 – 1048Cysteine 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 3 fibronectin type-II domains.PROSITE-ProRule annotation
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG328372.
    HOGENOMiHOG000217926.
    HOVERGENiHBG052484.

    Family and domain databases

    Gene3Di2.10.10.10. 3 hits.
    2.110.10.10. 1 hit.
    3.40.390.10. 2 hits.
    InterProiIPR000562. FN_type2_col-bd.
    IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR013806. Kringle-like.
    IPR024079. MetalloPept_cat_dom.
    IPR028688. MMP9.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    IPR006970. PT.
    [Graphical view]
    PANTHERiPTHR10201:SF30. PTHR10201:SF30. 1 hit.
    PfamiPF00040. fn2. 3 hits.
    PF00045. Hemopexin. 3 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    PF04886. PT. 1 hit.
    [Graphical view]
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00059. FN2. 3 hits.
    SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    SSF57440. SSF57440. 3 hits.
    PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
    PS00023. FN2_1. 3 hits.
    PS51092. FN2_2. 3 hits.
    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.

    P41246-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPRQPLVLA LLVLGCCSAA PRRRQPTLVV FPGELRTRLT DRQLAEEYLF    50
    RYGYTRVASM HGDSQSLRLP LLLLQKHLSL PETGELDNAT LEAMRAPRCG 100
    VPDVGKFQTF EGDLKWHHHN ITYWIQNYSE DLPRDVIDDA FARAFALWSA 150
    VTPLTFTRVY SRDADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGPGIQG 200
    DAHFDDEELW SLGKGVVVPT YFGNADGAPC HFPFTFEGRS YTACTTDGRS 250
    DGMAWCSTTA DYDTDRRFGF CPSERLYTQD GNADGKPCEF PFIFQGRTYS 300
    ACTTDGRSDG HRWCATTASY DKDKLYGFCP TRADSTVVGG NSAGELCVFP 350
    FVFLGKEYSS CTSEGRRDGR LWCATTSNFD SDKKWGFCPD KGYSLFLVAA 400
    HEFGHALGLD HSSVPERLMY PMYRYLEGSP LHEDDVRGIQ HLYGPNPNPQ 450
    PPATTTPEPQ PTAPPTACPT WPATVRPSEH PTTSPTGAPS AGPTGPPTAS 500
    PSAAPTASLD PAEDVCNVNV FDAIAEIGNK LHVFKDGRYW RFSEGSGRRP 550
    QGPFLIADTW PALPAKLDSA FEEPLTKKLF FFSGRQVWVY TGASVLGPRR 600
    LDKLGLGPEV PHVTGALPRA GGKVLLFGAQ RFWRFDVKTQ TVDSRSGAPV 650
    DQMFPGVPLN THDVFQYREK AYFCQDRFFW RVSTRNEVNL VDQVGYVSFD 700
    ILHCPED 707
    Length:707
    Mass (Da):78,308
    Last modified:February 1, 1995 - v1
    Checksum:i053BCE8DC4D4758F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761K → P in AAA64358. (PubMed:7961810)Curated
    Sequence conflicti100 – 1023GVP → ASR in AAA64358. (PubMed:7961810)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26514 mRNA. Translation: BAA05520.1.
    L36050 Genomic DNA. Translation: AAA64358.1.
    PIRiA53796.
    RefSeqiNP_001075672.1. NM_001082203.1.
    UniGeneiOcu.1773.

    Genome annotation databases

    GeneIDi100008993.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26514 mRNA. Translation: BAA05520.1 .
    L36050 Genomic DNA. Translation: AAA64358.1 .
    PIRi A53796.
    RefSeqi NP_001075672.1. NM_001082203.1.
    UniGenei Ocu.1773.

    3D structure databases

    ProteinModelPortali P41246.
    SMRi P41246. Positions 29-444, 513-707.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000025066.

    Protein family/group databases

    MEROPSi M10.004.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100008993.

    Organism-specific databases

    CTDi 4318.

    Phylogenomic databases

    eggNOGi NOG328372.
    HOGENOMi HOG000217926.
    HOVERGENi HBG052484.

    Family and domain databases

    Gene3Di 2.10.10.10. 3 hits.
    2.110.10.10. 1 hit.
    3.40.390.10. 2 hits.
    InterProi IPR000562. FN_type2_col-bd.
    IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR013806. Kringle-like.
    IPR024079. MetalloPept_cat_dom.
    IPR028688. MMP9.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    IPR006970. PT.
    [Graphical view ]
    PANTHERi PTHR10201:SF30. PTHR10201:SF30. 1 hit.
    Pfami PF00040. fn2. 3 hits.
    PF00045. Hemopexin. 3 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    PF04886. PT. 1 hit.
    [Graphical view ]
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00059. FN2. 3 hits.
    SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    SSF57440. SSF57440. 3 hits.
    PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
    PS00023. FN2_1. 3 hits.
    PS51092. FN2_2. 3 hits.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of matrix metalloproteinase 9 in rabbit osteoclasts."
      Tezuka K.I., Nemoto K., Tezuka Y., Sato T., Ikeda Y., Kobori M., Kawashima H., Eguchi H., Hakeda Y., Kumegawa M.
      J. Biol. Chem. 269:15006-15009(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Japanese white.
      Tissue: Bone.
    2. "The rabbit gene for 92-kDa matrix metalloproteinase. Role of AP1 and AP2 in cell type-specific transcription."
      Fini M.E., Bartlett J.D., Matsubara M., Rinehart W.B., Mody M.K., Girard M.T., Rainville M.
      J. Biol. Chem. 269:28620-28628(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-171.
      Strain: New Zealand white.
      Tissue: Liver.

    Entry informationi

    Entry nameiMMP9_RABIT
    AccessioniPrimary (citable) accession number: P41246
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 119 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