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O18733

- MMP9_CANFA

UniProt

O18733 - MMP9_CANFA

Protein

Matrix metalloproteinase-9

Gene

MMP9

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (11 Jul 2001)
      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 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
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: 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_0000028752Add
    BLAST
    Chaini107 – 704598Matrix metalloproteinase-9PRO_0000028753Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-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 bondi513 ↔ 701PROSITE-ProRule annotation

    Post-translational modificationi

    N- and O-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliO18733.
    SMRiO18733. Positions 29-444, 510-704.
    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
    Repeati515 – 56046Hemopexin 1Add
    BLAST
    Repeati561 – 60545Hemopexin 2Add
    BLAST
    Repeati607 – 65448Hemopexin 3Add
    BLAST
    Repeati655 – 70147Hemopexin 4Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi445 – 50864Pro-richAdd
    BLAST

    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.
    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.
    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.

    O18733-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPRQPLVLV FLVLGCCSAA PRPHKPTVVV FPGDLRTNLT DKQLAEEYLF    50
    RYGYTQVAEL SNDKQSLSRG LRLLQRRLAL PETGELDKTT LEAMRAPRCG 100
    VPDLGKFQTF EGDLKWHHND ITYWIQNYSE DLPRDVIDDA FARAFAVWSA 150
    VTPLTFTRVY GPEADIIIQF GVREHGDGYP FDGKNGLLAH AFPPGPGIQG 200
    DAHFDDEELW TLGKGVVVPT HFGNADGAPC HFPFTFEGRS YSACTTDGRS 250
    DDTPWCSTTA DYDTDRRFGF CPSEKLYAQD GNGDGKPCVF PFTFEGRSYS 300
    TCTTDGRSDG YRWCSTTADY DQDKLYGFCP TRVDSAVTGG NSAGEPCVFP 350
    FIFLGKQYST CTREGRGDGH LWCATTSNFD RDKKWGFCPD QGYSLFLVAA 400
    HEFGHALGLD HSSVPEALMY PMYSFTEGPP LHEDDVRGIQ HLYGPRPEPE 450
    PQPPTAPPTA PPTVCATGPP TTRPSERPTA GPTGPPAAGP TGPPTAGPSE 500
    APTVPVDPAE DICKVNIFDA IAEIRNYLHF FKEGKYWRFS KGKGRRVQGP 550
    FLSPSTWPAL PRKLDSAFED GLTKKTFFFS GRQVWVYTGT SVVGPRRLDK 600
    LGLGPEVTQV TGALPQGGGK VLLFSRQRFW SFDVKTQTVD PRSAGSVEQM 650
    YPGVPLNTHD IFQYQEKAYF CQDRFYWRVN SRNEVNQVDE VGYVTFDILQ 700
    CPED 704
    Length:704
    Mass (Da):78,123
    Last modified:July 11, 2001 - v2
    Checksum:i0DB394D2D6256B91
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311D → E in AAB81681. (PubMed:9325284)Curated
    Sequence conflicti276 – 2783LYA → FYT in AAB81681. (PubMed:9325284)Curated
    Sequence conflicti553 – 5553SPS → ITD in AAB81681. (PubMed:9325284)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006421 mRNA. Translation: BAA22087.3.
    U89842 mRNA. Translation: AAB81681.1.
    UniGeneiCfa.3470.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006421 mRNA. Translation: BAA22087.3 .
    U89842 mRNA. Translation: AAB81681.1 .
    UniGenei Cfa.3470.

    3D structure databases

    ProteinModelPortali O18733.
    SMRi O18733. Positions 29-444, 510-704.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M10.004.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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.
    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.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dog mast cell alpha-chymase activates progelatinase B by cleaving the Phe88-Gln89 and Phe91-Glu92 bonds of the catalytic domain."
      Fang K.C., Raymond W.W., Blount J.L., Caughey G.H.
      J. Biol. Chem. 272:25628-25635(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "High expression of 92 kDa type IV collagenase (matrix metalloproteinase-9) in canine mammary adenocarcinoma."
      Yokota H., Kumata T., Taketaba S., Kobayashi T., Moue H., Taniyama H., Hirayama K., Kagawa Y., Itoh N., Fujita O., Nakade T., Yuasa A.
      Biochim. Biophys. Acta 1568:7-12(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Mongrel.

    Entry informationi

    Entry nameiMMP9_CANFA
    AccessioniPrimary (citable) accession number: O18733
    Secondary accession number(s): O19130
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 11, 2001
    Last modified: October 1, 2014
    This is version 116 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3