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P52176

- MMP9_BOVIN

UniProt

P52176 - MMP9_BOVIN

Protein

Matrix metalloproteinase-9

Gene

MMP9

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: 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 peptidePRO_0000028750Add
    BLAST
    Chaini107 – 712606Matrix metalloproteinase-9PRO_0000028751Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-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 bondi521 ↔ 709PROSITE-ProRule annotation

    Post-translational modificationi

    N- and O-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP52176.
    PRIDEiP52176.

    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

    ProteinModelPortaliP52176.
    SMRiP52176. Positions 29-444, 518-712.
    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
    Repeati523 – 56846Hemopexin 1Add
    BLAST
    Repeati569 – 61345Hemopexin 2Add
    BLAST
    Repeati615 – 66248Hemopexin 3Add
    BLAST
    Repeati663 – 70947Hemopexin 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.
    InParanoidiP52176.
    KOiK01403.

    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.

    P52176-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPLQPLVLA LLVLACCSAV PRRRQPTVVV FPGEPRTNLT NRQLAEEYLY    50
    RYGYTPGAEL SEDGQSLQRA LLRFQRRLSL PETGELDSTT LNAMRAPRCG 100
    VPDVGRFQTF EGELKWHHHN ITYWIQNYSE DLPRAVIDDA FARAFALWSA 150
    VTPLTFTRVY GPEADIVIQF GVREHGDGYP FDGKNGLLAH AFPPGKGIQG 200
    DAHFDDEELW SLGKGVVIPT YFGNAKGAAC HFPFTFEGRS YSACTTDGRS 250
    DDMLWCSTTA DYDADRQFGF CPSERLYTQD GNADGKPCVF PFTFQGRTYS 300
    ACTSDGRSDG YRWCATTANY DQDKLYGFCP TRVDATVTGG NAAGELCVFP 350
    FTFLGKEYSA CTREGRNDGH LWCATTSNFD KDKKWGFCPD QGYSLFLVAA 400
    HEFGHALGLD HTSVPEALMY PMYRFTEEHP LHRDDVQGIQ HLYGPRPEPE 450
    PRPPTTTTTT TTEPQPTAPP TVCVTGPPTA RPSEGPTTGP TGPPAAGPTG 500
    PPTAGPSAAP TESPDPAEDV CNVDIFDAIA EIRNRLHFFK AGKYWRLSEG 550
    GGRRVQGPFL VKSKWPALPR KLDSAFEDPL TKKIFFFSGR QVWVYTGASL 600
    LGPRRLDKLG LGPEVAQVTG ALPRPEGKVL LFSGQSFWRF DVKTQKVDPQ 650
    SVTPVDQMFP GVPISTHDIF QYQEKAYFCQ DHFYWRVSSQ NEVNQVDYVG 700
    YVTFDLLKCP ED 712
    Length:712
    Mass (Da):79,088
    Last modified:October 1, 1996 - v1
    Checksum:iE7FDA28372AEE0CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78324 mRNA. Translation: CAA55127.1.
    BC142430 mRNA. Translation: AAI42431.1.
    PIRiI46031.
    RefSeqiNP_777169.1. NM_174744.2.
    UniGeneiBt.4714.

    Genome annotation databases

    GeneIDi282871.
    KEGGibta:282871.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78324 mRNA. Translation: CAA55127.1 .
    BC142430 mRNA. Translation: AAI42431.1 .
    PIRi I46031.
    RefSeqi NP_777169.1. NM_174744.2.
    UniGenei Bt.4714.

    3D structure databases

    ProteinModelPortali P52176.
    SMRi P52176. Positions 29-444, 518-712.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL5846.

    Protein family/group databases

    MEROPSi M10.004.

    Proteomic databases

    PaxDbi P52176.
    PRIDEi P52176.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 282871.
    KEGGi bta:282871.

    Organism-specific databases

    CTDi 4318.

    Phylogenomic databases

    eggNOGi NOG328372.
    HOGENOMi HOG000217926.
    HOVERGENi HBG052484.
    InParanoidi P52176.
    KOi K01403.

    Miscellaneous databases

    NextBioi 20806399.

    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. "Infection with Theileria annulata induces expression of matrix metalloproteinase 9 and transcription factor AP-1 in bovine leucocytes."
      Baylis H.A., Megson A., Hall R.
      Mol. Biochem. Parasitol. 69:211-222(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leukocyte.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.

    Entry informationi

    Entry nameiMMP9_BOVIN
    AccessioniPrimary (citable) accession number: P52176
    Secondary accession number(s): A5PKB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 117 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