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Protein

Matrix metalloproteinase-9

Gene

Mmp9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

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

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity
  • Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi100Zinc 2; in inhibited formBy similarity1
Metal bindingi132Calcium 1By similarity1
Metal bindingi166Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi176Zinc 1; structuralBy similarity1
Metal bindingi178Zinc 1; structuralBy similarity1
Metal bindingi183Calcium 3By similarity1
Metal bindingi184Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi186Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi188Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi191Zinc 1; structuralBy similarity1
Metal bindingi198Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi200Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi202Calcium 2By similarity1
Metal bindingi204Zinc 1; structuralBy similarity1
Metal bindingi206Calcium 3By similarity1
Metal bindingi207Calcium 1By similarity1
Metal bindingi209Calcium 1By similarity1
Metal bindingi209Calcium 3By similarity1
Metal bindingi402Zinc 2; catalyticBy similarity1
Active sitei403PROSITE-ProRule annotation1
Metal bindingi406Zinc 2; catalyticBy similarity1
Metal bindingi412Zinc 2; catalyticBy similarity1

GO - Molecular functioni

  • endopeptidase activity Source: RGD
  • fibronectin binding Source: RGD
  • identical protein binding Source: RGD
  • metalloendopeptidase activity Source: UniProtKB
  • metallopeptidase activity Source: RGD
  • peptidase activity Source: RGD
  • serine-type endopeptidase activity Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • aging Source: RGD
  • cellular response to cadmium ion Source: RGD
  • cellular response to cell-matrix adhesion Source: RGD
  • cellular response to cytokine stimulus Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to iron(III) ion Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to low-density lipoprotein particle stimulus Source: RGD
  • cellular response to reactive oxygen species Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • collagen catabolic process Source: RGD
  • embryo implantation Source: RGD
  • endodermal cell differentiation Source: RGD
  • extracellular matrix organization Source: RGD
  • heart development Source: RGD
  • kidney development Source: RGD
  • leukocyte migration Source: InterPro
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of cation channel activity Source: RGD
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: RGD
  • negative regulation of fibroblast proliferation Source: RGD
  • negative regulation of intrinsic apoptotic signaling pathway Source: RGD
  • ossification Source: RGD
  • parturition Source: RGD
  • positive regulation of angiogenesis Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of DNA binding Source: RGD
  • positive regulation of epidermal growth factor receptor signaling pathway Source: RGD
  • positive regulation of keratinocyte migration Source: RGD
  • positive regulation of leukocyte migration Source: RGD
  • positive regulation of protein phosphorylation Source: RGD
  • positive regulation of receptor binding Source: RGD
  • positive regulation of release of cytochrome c from mitochondria Source: RGD
  • positive regulation of synaptic plasticity Source: RGD
  • positive regulation of vascular smooth muscle cell proliferation Source: RGD
  • protein oligomerization Source: RGD
  • proteolysis Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to heat Source: RGD
  • response to high light intensity Source: RGD
  • response to hyperoxia Source: RGD
  • response to hypoxia Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to nicotine Source: RGD
  • response to nutrient Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organic substance Source: RGD
  • response to oxidative stress Source: RGD
  • response to radiation Source: RGD
  • response to retinoic acid Source: RGD
  • response to tumor necrosis factor Source: RGD
  • response to vitamin A Source: RGD
  • skeletal system development Source: RGD
  • tissue remodeling Source: RGD
  • transformation of host cell by virus Source: RGD

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.35 5301

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621320 Mmp9

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3870

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
PropeptideiPRO_000002876220 – 107Activation peptideBy similarityAdd BLAST88
ChainiPRO_0000028763108 – 708Matrix metalloproteinase-9Add BLAST601

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi39N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi121N-linked (GlcNAc...) asparagineSequence analysis1
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

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • fibronectin binding Source: RGD
  • identical protein binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000023965

Chemistry databases

BindingDBiP50282

Structurei

3D structure databases

ProteinModelPortaliP50282
SMRiP50282
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini226 – 274Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini284 – 332Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini343 – 391Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST49
Repeati521 – 566Hemopexin 1Add BLAST46
Repeati567 – 611Hemopexin 2Add BLAST45
Repeati613 – 660Hemopexin 3Add BLAST48
Repeati661 – 707Hemopexin 4Add BLAST47

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi98 – 105Cysteine switchBy similarity8

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
HOGENOMiHOG000217926
HOVERGENiHBG052484
InParanoidiP50282
KOiK01403
PhylomeDBiP50282

Family and domain databases

CDDicd00062 FN2, 3 hits
cd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.10.10.10, 3 hits
2.110.10.10, 1 hit
3.40.390.10, 2 hits
InterProiView protein in InterPro
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR013806 Kringle-like
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028688 MMP9
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf
IPR006970 PT
PANTHERiPTHR10201:SF30 PTHR10201:SF30, 1 hit
PfamiView protein in Pfam
PF00040 fn2, 3 hits
PF00045 Hemopexin, 1 hit
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PF04886 PT, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00059 FN2, 3 hits
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
SSF57440 SSF57440, 3 hits
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P50282-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPWQPLLLV LLALGYSFAA PHQRQPTYVV FPRDLKTSNL TDTQLAEDYL
60 70 80 90 100
YRYGYTRAAQ MMGEKQSLRP ALLMLQKQLS LPQTGELDSE TLKAIRSPRC
110 120 130 140 150
GVPDVGKFQT FDGDLKWHHH NITYWIQSYT EDLPRDVIDD SFARAFAVWS
160 170 180 190 200
AVTPLTFTRV YGLEADIVIQ FGVAEHGDGY PFDGKDGLLA HAFPPGPGIQ
210 220 230 240 250
GDAHFDDDEL WSLGKGAVVP TYFGNANGAP CHFPFTFEGR SYLSCTTDGR
260 270 280 290 300
NDGKPWCGTT ADYDTDRKYG FCPSENLYTE HGNGDGKPCV FPFIFEGHSY
310 320 330 340 350
SACTTKGRSD GYRWCATTAN YDQDKADGFC PTRADVTVTG GNSAGEMCVF
360 370 380 390 400
PFVFLGKQYS TCTSEGRSDG RLWCATTSNF DADKKWGFCP DQGYSLFLVA
410 420 430 440 450
AHEFGHALGL DHSSVPEALM YPMYHYHEDS PLHEDDIKGI HHLYGRGSKP
460 470 480 490 500
DPRPPATTAA EPQPTAPPTM CSTAPPMAYP TGGPTVAPTG APSPGPTGPP
510 520 530 540 550
TAGPSEAPTE SSTPDDNPCN VDVFDAIADI QGALHFFKDG RYWKFSNHGG
560 570 580 590 600
NQLQGPFLIA RTWPAFPSKL NSAFEDPQPK KIFFFLWAQM WVYTGQSVLG
610 620 630 640 650
PRSLDKLGLG SEVTLVTGLL PRRGGKALLI SRERIWKFDL KSQKVDPQSV
660 670 680 690 700
TRLDNEFSGV PWNSHNVFQY QDKAYFCHDK YFWRVSFHNR VNQVDHVAYV

TYDLLQCP
Length:708
Mass (Da):78,611
Last modified:October 1, 1996 - v1
Checksum:iD57DC0D1B93A778C
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2S → N in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti112D → E in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti326 – 327AD → LY in AAA90911 (PubMed:7590350).Curated2
Sequence conflicti364S → G in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti441H → Q in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti472S → P in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti515D → V in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti551N → S in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti566F → L in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti568S → A in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti579P → S in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti586 – 589LWAQ → SGRK in AAA90911 (PubMed:7590350).Curated4
Sequence conflicti597S → T in AAA90911 (PubMed:7590350).Curated1
Sequence conflicti669Q → H in AAA90911 (PubMed:7590350).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiMMP9_RAT
AccessioniPrimary (citable) accession number: P50282
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 25, 2018
This is version 154 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health