UniProtKB - P50282 (MMP9_RAT)
Protein
Matrix metalloproteinase-9
Gene
Mmp9
Organism
Rattus norvegicus (Rat)
Status
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. EC:3.4.24.35
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 100 | Zinc 2; in inhibited formBy similarity | 1 | |
Metal bindingi | 132 | Calcium 1By similarity | 1 | |
Metal bindingi | 166 | Calcium 2; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 176 | Zinc 1; structuralBy similarity | 1 | |
Metal bindingi | 178 | Zinc 1; structuralBy similarity | 1 | |
Metal bindingi | 183 | Calcium 3By similarity | 1 | |
Metal bindingi | 184 | Calcium 3; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 186 | Calcium 3; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 188 | Calcium 3; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 191 | Zinc 1; structuralBy similarity | 1 | |
Metal bindingi | 198 | Calcium 2; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 200 | Calcium 2; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 202 | Calcium 2By similarity | 1 | |
Metal bindingi | 204 | Zinc 1; structuralBy similarity | 1 | |
Metal bindingi | 206 | Calcium 3By similarity | 1 | |
Metal bindingi | 207 | Calcium 1By similarity | 1 | |
Metal bindingi | 209 | Calcium 1By similarity | 1 | |
Metal bindingi | 209 | Calcium 3By similarity | 1 | |
Metal bindingi | 402 | Zinc 2; catalyticBy similarity | 1 | |
Active sitei | 403 | PROSITE-ProRule annotation | 1 | |
Metal bindingi | 406 | Zinc 2; catalyticBy similarity | 1 | |
Metal bindingi | 412 | Zinc 2; catalyticBy similarity | 1 |
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
- protein-containing complex binding 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 epithelial cell differentiation involved in kidney development 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 cell migration 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 associated smooth muscle cell proliferation Source: RGD
- proteolysis Source: RGD
- response to amyloid-beta 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 function | Hydrolase, Metalloprotease, Protease |
Biological process | Collagen degradation |
Ligand | Calcium, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.4.24.35, 5301 |
Reactomei | R-RNO-1433557, Signaling by SCF-KIT R-RNO-1442490, Collagen degradation R-RNO-1474228, Degradation of the extracellular matrix R-RNO-1592389, Activation of Matrix Metalloproteinases R-RNO-2022090, Assembly of collagen fibrils and other multimeric structures R-RNO-3928665, EPH-ephrin mediated repulsion of cells R-RNO-6798695, Neutrophil degranulation R-RNO-9009391, Extra-nuclear estrogen signaling |
Protein family/group databases
MEROPSi | M10.004 |
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 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 621320, Mmp9 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix Curated
Extracellular region or secreted
- extracellular matrix Source: InterPro
- extracellular space Source: RGD
Other locations
- protein-containing complex Source: RGD
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 19 | By similarityAdd BLAST | 19 | |
PropeptideiPRO_0000028762 | 20 – 107 | Activation peptideBy similarityAdd BLAST | 88 | |
ChainiPRO_0000028763 | 108 – 708 | Matrix metalloproteinase-9Add BLAST | 601 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 39 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 121 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 231 ↔ 257 | PROSITE-ProRule annotation | ||
Disulfide bondi | 245 ↔ 272 | PROSITE-ProRule annotation | ||
Disulfide bondi | 289 ↔ 315 | PROSITE-ProRule annotation | ||
Disulfide bondi | 303 ↔ 330 | PROSITE-ProRule annotation | ||
Disulfide bondi | 348 ↔ 374 | PROSITE-ProRule annotation | ||
Disulfide bondi | 362 ↔ 389 | PROSITE-ProRule annotation | ||
Disulfide bondi | 519 ↔ 707 | PROSITE-ProRule annotation |
Post-translational modificationi
N- and O-glycosylated.By similarity
Keywords - PTMi
Disulfide bond, Glycoprotein, ZymogenProteomic databases
PaxDbi | P50282 |
PRIDEi | P50282 |
PTM databases
GlyGeni | P50282, 2 sites |
Interactioni
Subunit structurei
Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with LCN2.
Interacts with ECM1.
By similarityGO - Molecular functioni
- fibronectin binding Source: RGD
- identical protein binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000023965 |
Chemistry databases
BindingDBi | P50282 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 226 – 274 | Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST | 49 | |
Domaini | 284 – 332 | Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST | 49 | |
Domaini | 343 – 391 | Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST | 49 | |
Repeati | 521 – 566 | Hemopexin 1Add BLAST | 46 | |
Repeati | 567 – 611 | Hemopexin 2Add BLAST | 45 | |
Repeati | 613 – 660 | Hemopexin 3Add BLAST | 48 | |
Repeati | 661 – 707 | Hemopexin 4Add BLAST | 47 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 98 – 105 | Cysteine switchBy similarity | 8 |
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, SignalPhylogenomic databases
eggNOGi | KOG1565, Eukaryota |
InParanoidi | P50282 |
OrthoDBi | 1075463at2759 |
PhylomeDBi | P50282 |
Family and domain databases
CDDi | cd00062, FN2, 3 hits cd00094, HX, 1 hit cd04278, ZnMc_MMP, 1 hit |
Gene3Di | 1.10.101.10, 1 hit 2.10.10.10, 3 hits 2.110.10.10, 1 hit 3.40.390.10, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR10201:SF30, PTHR10201:SF30, 1 hit |
Pfami | View 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 |
PIRSFi | PIRSF001191, Peptidase_M10A_matrix, 1 hit |
PRINTSi | PR00138, MATRIXIN |
SMARTi | View protein in SMART SM00059, FN2, 3 hits SM00120, HX, 4 hits SM00235, ZnMc, 1 hit |
SUPFAMi | SSF47090, SSF47090, 1 hit SSF50923, SSF50923, 1 hit SSF57440, SSF57440, 3 hits |
PROSITEi | View 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 |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
P50282-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketD3ZYK8 | D3ZYK8_RAT | 92 kDa gelatinase | Mmp9 rCG_32078 | 708 | Annotation score: | ||
A0A0G2JUD9 | A0A0G2JUD9_RAT | 92 kDa gelatinase | Mmp9 | 708 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 2 | S → N in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 112 | D → E in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 326 – 327 | AD → LY in AAA90911 (PubMed:7590350).Curated | 2 | |
Sequence conflicti | 364 | S → G in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 441 | H → Q in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 472 | S → P in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 515 | D → V in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 551 | N → S in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 566 | F → L in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 568 | S → A in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 579 | P → S in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 586 – 589 | LWAQ → SGRK in AAA90911 (PubMed:7590350).Curated | 4 | |
Sequence conflicti | 597 | S → T in AAA90911 (PubMed:7590350).Curated | 1 | |
Sequence conflicti | 669 | Q → H in AAA90911 (PubMed:7590350).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U24441 mRNA Translation: AAA90911.1 U36476 mRNA Translation: AAB01721.1 |
PIRi | JC4364 S62907 |
RefSeqi | NP_112317.1, NM_031055.1 |
Genome annotation databases
GeneIDi | 81687 |
KEGGi | rno:81687 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U24441 mRNA Translation: AAA90911.1 U36476 mRNA Translation: AAB01721.1 |
PIRi | JC4364 S62907 |
RefSeqi | NP_112317.1, NM_031055.1 |
3D structure databases
SMRi | P50282 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000023965 |
Chemistry databases
BindingDBi | P50282 |
ChEMBLi | CHEMBL3870 |
Protein family/group databases
MEROPSi | M10.004 |
PTM databases
GlyGeni | P50282, 2 sites |
Proteomic databases
PaxDbi | P50282 |
PRIDEi | P50282 |
Protocols and materials databases
ABCDi | P50282, 2 sequenced antibodies |
Genome annotation databases
GeneIDi | 81687 |
KEGGi | rno:81687 |
Organism-specific databases
CTDi | 4318 |
RGDi | 621320, Mmp9 |
Phylogenomic databases
eggNOGi | KOG1565, Eukaryota |
InParanoidi | P50282 |
OrthoDBi | 1075463at2759 |
PhylomeDBi | P50282 |
Enzyme and pathway databases
BRENDAi | 3.4.24.35, 5301 |
Reactomei | R-RNO-1433557, Signaling by SCF-KIT R-RNO-1442490, Collagen degradation R-RNO-1474228, Degradation of the extracellular matrix R-RNO-1592389, Activation of Matrix Metalloproteinases R-RNO-2022090, Assembly of collagen fibrils and other multimeric structures R-RNO-3928665, EPH-ephrin mediated repulsion of cells R-RNO-6798695, Neutrophil degranulation R-RNO-9009391, Extra-nuclear estrogen signaling |
Miscellaneous databases
PROi | PR:P50282 |
Family and domain databases
CDDi | cd00062, FN2, 3 hits cd00094, HX, 1 hit cd04278, ZnMc_MMP, 1 hit |
Gene3Di | 1.10.101.10, 1 hit 2.10.10.10, 3 hits 2.110.10.10, 1 hit 3.40.390.10, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR10201:SF30, PTHR10201:SF30, 1 hit |
Pfami | View 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 |
PIRSFi | PIRSF001191, Peptidase_M10A_matrix, 1 hit |
PRINTSi | PR00138, MATRIXIN |
SMARTi | View protein in SMART SM00059, FN2, 3 hits SM00120, HX, 4 hits SM00235, ZnMc, 1 hit |
SUPFAMi | SSF47090, SSF47090, 1 hit SSF50923, SSF50923, 1 hit SSF57440, SSF57440, 3 hits |
PROSITEi | View 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MMP9_RAT | |
Accessioni | P50282Primary (citable) accession number: P50282 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | October 1, 1996 | |
Last modified: | February 10, 2021 | |
This is version 170 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Peptidase families
Classification of peptidase families and list of entries