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Protein

Matrix metalloproteinase-9

Gene

Mmp9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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 bindingi131Calcium 1By similarity1
Metal bindingi165Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi175Zinc 1; structuralBy similarity1
Metal bindingi177Zinc 1; structuralBy similarity1
Metal bindingi182Calcium 3By similarity1
Metal bindingi183Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi185Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi187Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi190Zinc 1; structuralBy similarity1
Metal bindingi197Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi199Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi201Calcium 2By similarity1
Metal bindingi203Zinc 1; structuralBy similarity1
Metal bindingi205Calcium 3By similarity1
Metal bindingi206Calcium 1By similarity1
Metal bindingi208Calcium 1By similarity1
Metal bindingi208Calcium 3By similarity1
Metal bindingi401Zinc 2; catalyticBy similarity1
Active sitei402PROSITE-ProRule annotation1
Metal bindingi405Zinc 2; catalyticBy similarity1
Metal bindingi411Zinc 2; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi3.4.24.35 3474
ReactomeiR-MMU-1433557 Signaling by SCF-KIT
R-MMU-1442490 Collagen degradation
R-MMU-1474228 Degradation of the extracellular matrix
R-MMU-1592389 Activation of Matrix Metalloproteinases
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-3928665 EPH-ephrin mediated repulsion of cells
R-MMU-6798695 Neutrophil degranulation

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
Synonyms:Clg4b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97011 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

ChEMBLiCHEMBL2214

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
PropeptideiPRO_000002875820 – 107Activation peptideBy similarityAdd BLAST88
ChainiPRO_0000028759108 – 730Matrix metalloproteinase-9Add BLAST623

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi39N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi120N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi127N-linked (GlcNAc...) asparagineSequence analysis1
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 bondi534 ↔ 729PROSITE-ProRule annotation

Post-translational modificationi

N- and O-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP41245
PaxDbiP41245
PeptideAtlasiP41245
PRIDEiP41245

PTM databases

CarbonylDBiP41245
PhosphoSitePlusiP41245

Expressioni

Inductioni

Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells.1 Publication
(Microbial infection) Induced in macrophages as well as in whole animals (spleen, lung and liver) by incubation or infection with M.bovis BCG and M.tuberculosis H37Rv (at protein level) (PubMed:11500442).1 Publication

Gene expression databases

BgeeiENSMUSG00000017737 Expressed in 182 organ(s), highest expression level in hindlimb long bone
CleanExiMM_MMP9
ExpressionAtlasiP41245 baseline and differential
GenevisibleiP41245 MM

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

Protein-protein interaction databases

BioGridi201454, 1 interactor
STRINGi10090.ENSMUSP00000017881

Chemistry databases

BindingDBiP41245

Structurei

3D structure databases

ProteinModelPortaliP41245
SMRiP41245
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini225 – 273Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini283 – 331Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini342 – 390Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST49
Repeati536 – 581Hemopexin 1Add BLAST46
Repeati582 – 626Hemopexin 2Add BLAST45
Repeati628 – 675Hemopexin 3Add BLAST48
Repeati676 – 729Hemopexin 4Add BLAST54

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
GeneTreeiENSGT00910000144034
HOGENOMiHOG000217926
HOVERGENiHBG052484
InParanoidiP41245
KOiK01403
OMAiGFCPSER
OrthoDBiEOG091G02JB
TreeFamiTF315428

Family and domain databases

CDDicd00062 FN2, 2 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, 2 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PF04886 PT, 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, 3 hits
PS51092 FN2_2, 3 hits
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P41245-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSPWQPLLLA LLAFGCSSAA PYQRQPTFVV FPKDLKTSNL TDTQLAEAYL
60 70 80 90 100
YRYGYTRAAQ MMGEKQSLRP ALLMLQKQLS LPQTGELDSQ TLKAIRTPRC
110 120 130 140 150
GVPDVGRFQT FKGLKWDHHN ITYWIQNYSE DLPRDMIDDA FARAFAVWGE
160 170 180 190 200
VAPLTFTRVY GPEADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGAGVQG
210 220 230 240 250
DAHFDDDELW SLGKGVVIPT YYGNSNGAPC HFPFTFEGRS YSACTTDGRN
260 270 280 290 300
DGTPWCSTTA DYDKDGKFGF CPSERLYTEH GNGEGKPCVF PFIFEGRSYS
310 320 330 340 350
ACTTKGRSDG YRWCATTANY DQDKLYGFCP TRVDATVVGG NSAGELCVFP
360 370 380 390 400
FVFLGKQYSS CTSDGRRDGR LWCATTSNFD TDKKWGFCPD QGYSLFLVAA
410 420 430 440 450
HEFGHALGLD HSSVPEALMY PLYSYLEGFP LNKDDIDGIQ YLYGRGSKPD
460 470 480 490 500
PRPPATTTTE PQPTAPPTMC PTIPPTAYPT VGPTVGPTGA PSPGPTSSPS
510 520 530 540 550
PGPTGAPSPG PTAPPTAGSS EASTESLSPA DNPCNVDVFD AIAEIQGALH
560 570 580 590 600
FFKDGWYWKF LNHRGSPLQG PFLTARTWPA LPATLDSAFE DPQTKRVFFF
610 620 630 640 650
SGRQMWVYTG KTVLGPRSLD KLGLGPEVTH VSGLLPRRLG KALLFSKGRV
660 670 680 690 700
WRFDLKSQKV DPQSVIRVDK EFSGVPWNSH DIFQYQDKAY FCHGKFFWRV
710 720 730
SFQNEVNKVD HEVNQVDDVG YVTYDLLQCP
Length:730
Mass (Da):80,535
Last modified:July 27, 2011 - v2
Checksum:iE16F45C24D4D1024
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2A5K8A2A5K8_MOUSE
Matrix metalloproteinase-9
Mmp9
67Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20A → C in AAB28942 (PubMed:8219207).Curated1
Sequence conflicti25 – 26QP → HA in AAB28942 (PubMed:8219207).Curated2
Sequence conflicti466P → T in BAB23442 (PubMed:16141072).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti514P → A1 Publication1
Natural varianti639L → P1 Publication1
Natural varianti711H → P1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12712 mRNA Translation: BAA02208.1
S67830 mRNA Translation: AAB28942.1
X72794 Genomic DNA Translation: CAA51314.1
X72795 mRNA Translation: CAA51315.1
Z27231 mRNA Translation: CAA81745.1
AK004651 mRNA Translation: BAB23442.1
AK159292 mRNA Translation: BAE34968.1
AL591495 Genomic DNA Translation: CAM26465.1
BC046991 mRNA Translation: AAH46991.1
CCDSiCCDS17066.1
PIRiI52580
JC1456
RefSeqiNP_038627.1, NM_013599.4
UniGeneiMm.4406

Genome annotation databases

EnsembliENSMUST00000017881; ENSMUSP00000017881; ENSMUSG00000017737
GeneIDi17395
KEGGimmu:17395
UCSCiuc008nwt.2 mouse

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D12712 mRNA Translation: BAA02208.1
S67830 mRNA Translation: AAB28942.1
X72794 Genomic DNA Translation: CAA51314.1
X72795 mRNA Translation: CAA51315.1
Z27231 mRNA Translation: CAA81745.1
AK004651 mRNA Translation: BAB23442.1
AK159292 mRNA Translation: BAE34968.1
AL591495 Genomic DNA Translation: CAM26465.1
BC046991 mRNA Translation: AAH46991.1
CCDSiCCDS17066.1
PIRiI52580
JC1456
RefSeqiNP_038627.1, NM_013599.4
UniGeneiMm.4406

3D structure databases

ProteinModelPortaliP41245
SMRiP41245
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201454, 1 interactor
STRINGi10090.ENSMUSP00000017881

Chemistry databases

BindingDBiP41245
ChEMBLiCHEMBL2214

Protein family/group databases

MEROPSiM10.004

PTM databases

CarbonylDBiP41245
PhosphoSitePlusiP41245

Proteomic databases

MaxQBiP41245
PaxDbiP41245
PeptideAtlasiP41245
PRIDEiP41245

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017881; ENSMUSP00000017881; ENSMUSG00000017737
GeneIDi17395
KEGGimmu:17395
UCSCiuc008nwt.2 mouse

Organism-specific databases

CTDi4318
MGIiMGI:97011 Mmp9

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00910000144034
HOGENOMiHOG000217926
HOVERGENiHBG052484
InParanoidiP41245
KOiK01403
OMAiGFCPSER
OrthoDBiEOG091G02JB
TreeFamiTF315428

Enzyme and pathway databases

BRENDAi3.4.24.35 3474
ReactomeiR-MMU-1433557 Signaling by SCF-KIT
R-MMU-1442490 Collagen degradation
R-MMU-1474228 Degradation of the extracellular matrix
R-MMU-1592389 Activation of Matrix Metalloproteinases
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-3928665 EPH-ephrin mediated repulsion of cells
R-MMU-6798695 Neutrophil degranulation

Miscellaneous databases

PROiPR:P41245
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000017737 Expressed in 182 organ(s), highest expression level in hindlimb long bone
CleanExiMM_MMP9
ExpressionAtlasiP41245 baseline and differential
GenevisibleiP41245 MM

Family and domain databases

CDDicd00062 FN2, 2 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, 2 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PF04886 PT, 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, 3 hits
PS51092 FN2_2, 3 hits
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMMP9_MOUSE
AccessioniPrimary (citable) accession number: P41245
Secondary accession number(s): Q06788, Q80XI8, Q9DC02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: September 12, 2018
This is version 185 of the entry and version 2 of the sequence. See 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
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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