Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Matrix metalloproteinase-9

Gene

Mmp9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, 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-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97011. Mmp9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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...)Sequence analysis1
Glycosylationi120N-linked (GlcNAc...)Sequence analysis1
Glycosylationi127N-linked (GlcNAc...)Sequence 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

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.
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

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
Contains 3 fibronectin type-II domains.PROSITE-ProRule annotation
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiP41245.
KOiK01403.
OMAiGFCPSER.
OrthoDBiEOG091G02JB.
TreeFamiTF315428.

Family and domain databases

CDDicd00062. FN2. 2 hits.
cd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
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.
IPR018486. Hemopexin_CS.
IPR013806. Kringle-like.
IPR033739. M10A_MMP.
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. 3 hits.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 2 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.
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.

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

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 → A.1 Publication1
Natural varianti639L → P.1 Publication1
Natural varianti711H → P.1 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

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

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.
GeneTreeiENSGT00760000118870.
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-3928665. EPH-ephrin mediated repulsion of cells.
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiP41245.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000017737.
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.
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.
IPR018486. Hemopexin_CS.
IPR013806. Kringle-like.
IPR033739. M10A_MMP.
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. 3 hits.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 2 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.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP9_MOUSE
AccessioniPrimary (citable) accession number: P41245
Secondary accession number(s): Q06788, Q80XI8, Q9DC02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 172 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.