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P50282

- MMP9_RAT

UniProt

P50282 - MMP9_RAT

Protein

Matrix metalloproteinase-9

Gene

Mmp9

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 131 (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 bindingi100 – 1001Zinc 2; in inhibited formBy similarity
    Metal bindingi132 – 1321Calcium 1By similarity
    Metal bindingi166 – 1661Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi176 – 1761Zinc 1; structuralBy similarity
    Metal bindingi178 – 1781Zinc 1; structuralBy similarity
    Metal bindingi183 – 1831Calcium 3By similarity
    Metal bindingi184 – 1841Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi186 – 1861Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi188 – 1881Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi191 – 1911Zinc 1; structuralBy similarity
    Metal bindingi198 – 1981Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi200 – 2001Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi202 – 2021Calcium 2By similarity
    Metal bindingi204 – 2041Zinc 1; structuralBy similarity
    Metal bindingi206 – 2061Calcium 3By similarity
    Metal bindingi207 – 2071Calcium 1By similarity
    Metal bindingi209 – 2091Calcium 1By similarity
    Metal bindingi209 – 2091Calcium 3By similarity
    Metal bindingi402 – 4021Zinc 2; catalyticBy similarity
    Active sitei403 – 4031PROSITE-ProRule annotation
    Metal bindingi406 – 4061Zinc 2; catalyticBy similarity
    Metal bindingi412 – 4121Zinc 2; catalyticBy similarity

    GO - Molecular functioni

    1. fibronectin binding Source: RGD
    2. metalloendopeptidase activity Source: UniProtKB
    3. metallopeptidase activity Source: RGD
    4. peptidase activity Source: RGD
    5. protein binding Source: RGD
    6. protein complex binding Source: RGD
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. anatomical structure regression Source: RGD
    2. cellular response to cell-matrix adhesion Source: RGD
    3. cellular response to cytokine stimulus Source: RGD
    4. cellular response to interleukin-1 Source: RGD
    5. cellular response to iron(III) ion Source: RGD
    6. cellular response to lipopolysaccharide Source: RGD
    7. cellular response to low-density lipoprotein particle stimulus Source: RGD
    8. cellular response to tumor necrosis factor Source: RGD
    9. collagen catabolic process Source: RGD
    10. kidney development Source: RGD
    11. leukocyte migration Source: InterPro
    12. negative regulation of fibroblast proliferation Source: RGD
    13. ossification Source: RGD
    14. parturition Source: RGD
    15. positive regulation of angiogenesis Source: RGD
    16. positive regulation of synaptic plasticity Source: RGD
    17. protein oligomerization Source: RGD
    18. proteolysis Source: UniProtKB
    19. response to drug Source: RGD
    20. response to estradiol Source: RGD
    21. response to ethanol Source: RGD
    22. response to heat Source: RGD
    23. response to high light intensity Source: RGD
    24. response to hyperoxia Source: RGD
    25. response to hypoxia Source: RGD
    26. response to lipopolysaccharide Source: RGD
    27. response to mechanical stimulus Source: RGD
    28. response to nicotine Source: RGD
    29. response to nutrient Source: RGD
    30. response to organic cyclic compound Source: RGD
    31. response to organic substance Source: RGD
    32. response to oxidative stress Source: RGD
    33. response to radiation Source: RGD
    34. response to retinoic acid Source: RGD
    35. response to tumor necrosis factor Source: RGD
    36. response to vitamin A Source: RGD
    37. tissue remodeling Source: RGD
    38. transformation of host cell by virus Source: RGD

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621320. Mmp9.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    3. protein complex Source: RGD

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Propeptidei20 – 10788Activation peptideBy similarityPRO_0000028762Add
    BLAST
    Chaini108 – 708601Matrix metalloproteinase-9PRO_0000028763Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi231 ↔ 257PROSITE-ProRule annotation
    Disulfide bondi245 ↔ 272PROSITE-ProRule annotation
    Disulfide bondi289 ↔ 315PROSITE-ProRule annotation
    Disulfide bondi303 ↔ 330PROSITE-ProRule annotation
    Disulfide bondi348 ↔ 374PROSITE-ProRule annotation
    Disulfide bondi362 ↔ 389PROSITE-ProRule annotation
    Disulfide bondi519 ↔ 707PROSITE-ProRule annotation

    Post-translational modificationi

    N- and O-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP50282.
    PRIDEiP50282.

    Expressioni

    Gene expression databases

    GenevestigatoriP50282.

    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

    STRINGi10116.ENSRNOP00000023965.

    Structurei

    3D structure databases

    ProteinModelPortaliP50282.
    SMRiP50282. Positions 29-445.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini226 – 27449Fibronectin type-II 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini284 – 33249Fibronectin type-II 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini343 – 39149Fibronectin type-II 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati521 – 56646Hemopexin 1Add
    BLAST
    Repeati567 – 61145Hemopexin 2Add
    BLAST
    Repeati613 – 66048Hemopexin 3Add
    BLAST
    Repeati661 – 70747Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi98 – 1058Cysteine 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.
    InParanoidiP50282.
    KOiK01403.
    PhylomeDBiP50282.

    Family and domain databases

    Gene3Di1.10.101.10. 1 hit.
    2.10.10.10. 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. 1 hit.
    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. 2 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.

    P50282-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPWQPLLLV LLALGYSFAA PHQRQPTYVV FPRDLKTSNL TDTQLAEDYL    50
    YRYGYTRAAQ MMGEKQSLRP ALLMLQKQLS LPQTGELDSE TLKAIRSPRC 100
    GVPDVGKFQT FDGDLKWHHH NITYWIQSYT EDLPRDVIDD SFARAFAVWS 150
    AVTPLTFTRV YGLEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGPGIQ 200
    GDAHFDDDEL WSLGKGAVVP TYFGNANGAP CHFPFTFEGR SYLSCTTDGR 250
    NDGKPWCGTT ADYDTDRKYG FCPSENLYTE HGNGDGKPCV FPFIFEGHSY 300
    SACTTKGRSD GYRWCATTAN YDQDKADGFC PTRADVTVTG GNSAGEMCVF 350
    PFVFLGKQYS TCTSEGRSDG RLWCATTSNF DADKKWGFCP DQGYSLFLVA 400
    AHEFGHALGL DHSSVPEALM YPMYHYHEDS PLHEDDIKGI HHLYGRGSKP 450
    DPRPPATTAA EPQPTAPPTM CSTAPPMAYP TGGPTVAPTG APSPGPTGPP 500
    TAGPSEAPTE SSTPDDNPCN VDVFDAIADI QGALHFFKDG RYWKFSNHGG 550
    NQLQGPFLIA RTWPAFPSKL NSAFEDPQPK KIFFFLWAQM WVYTGQSVLG 600
    PRSLDKLGLG SEVTLVTGLL PRRGGKALLI SRERIWKFDL KSQKVDPQSV 650
    TRLDNEFSGV PWNSHNVFQY QDKAYFCHDK YFWRVSFHNR VNQVDHVAYV 700
    TYDLLQCP 708
    Length:708
    Mass (Da):78,611
    Last modified:October 1, 1996 - v1
    Checksum:iD57DC0D1B93A778C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21S → N in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti112 – 1121D → E in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti326 – 3272AD → LY in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti364 – 3641S → G in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti441 – 4411H → Q in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti472 – 4721S → P in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti515 – 5151D → V in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti551 – 5511N → S in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti566 – 5661F → L in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti568 – 5681S → A in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti579 – 5791P → S in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti586 – 5894LWAQ → SGRK in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti597 – 5971S → T in AAA90911. (PubMed:7590350)Curated
    Sequence conflicti669 – 6691Q → H in AAA90911. (PubMed:7590350)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24441 mRNA. Translation: AAA90911.1.
    U36476 mRNA. Translation: AAB01721.1.
    PIRiJC4364.
    S62907.
    RefSeqiNP_112317.1. NM_031055.1.
    UniGeneiRn.10209.

    Genome annotation databases

    GeneIDi81687.
    KEGGirno:81687.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24441 mRNA. Translation: AAA90911.1 .
    U36476 mRNA. Translation: AAB01721.1 .
    PIRi JC4364.
    S62907.
    RefSeqi NP_112317.1. NM_031055.1.
    UniGenei Rn.10209.

    3D structure databases

    ProteinModelPortali P50282.
    SMRi P50282. Positions 29-445.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000023965.

    Chemistry

    BindingDBi P50282.
    ChEMBLi CHEMBL3870.

    Protein family/group databases

    MEROPSi M10.004.

    Proteomic databases

    PaxDbi P50282.
    PRIDEi P50282.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 81687.
    KEGGi rno:81687.

    Organism-specific databases

    CTDi 4318.
    RGDi 621320. Mmp9.

    Phylogenomic databases

    eggNOGi NOG328372.
    HOGENOMi HOG000217926.
    HOVERGENi HBG052484.
    InParanoidi P50282.
    KOi K01403.
    PhylomeDBi P50282.

    Miscellaneous databases

    NextBioi 615324.
    PROi P50282.

    Gene expression databases

    Genevestigatori P50282.

    Family and domain databases

    Gene3Di 1.10.101.10. 1 hit.
    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. 1 hit.
    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. 2 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. "The cDNA cloning and expression of the gene encoding rat gelatinase B."
      Okada A., Santavicca M., Basset P.
      Gene 164:317-321(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
    2. "Cloning of rat 92-kDa type IV collagenase and expression of an active recombinant catalytic domain."
      Xia Y., Garcia G., Chen S., Wilson C.B., Feng L.
      FEBS Lett. 382:285-288(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Fischer 344.

    Entry informationi

    Entry nameiMMP9_RAT
    AccessioniPrimary (citable) accession number: P50282
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 131 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