Matrix metalloproteinase-9 precursor

Protein attributes

Sequence length	730 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	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.
Catalytic activity	Cleavage of gelatin types I and V and collagen types IV and V.
Cofactor	Binds 2 zinc ions per subunit By similarity. Binds 3 calcium ions per subunit By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix Probable.
Domain	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.
Post-translational modification	N- and O-glycosylated By similarity.
Sequence similarities	Belongs to the peptidase M10A family. Contains 3 fibronectin type-II domains. Contains 4 hemopexin-like domains.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from direct assay. Source: MGI extracellular matrix organization Inferred from genetic interaction. Source: MGI positive regulation of apoptosis Inferred from mutant phenotype. Source: MGI proteolysis Inferred from sequence or structural similarity. Source: UniProtKB skeletal system development Inferred from genetic interaction. Source: MGI
Cellular component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

By similarity

Propeptide

20 – 107

88

Activation peptide By similarity

PRO_0000028758

Chain

108 – 730

623

Matrix metalloproteinase-9

PRO_0000028759

Regions

Domain

225 – 273

49

Fibronectin type-II 1

Domain

283 – 331

49

Fibronectin type-II 2

Domain

342 – 390

49

Fibronectin type-II 3

Domain

539 – 583

45

Hemopexin-like 1

Domain

585 – 626

42

Hemopexin-like 2

Domain

631 – 677

47

Hemopexin-like 3

Domain

679 – 723

45

Hemopexin-like 4

Motif

98 – 105

8

Cysteine switch By similarity

Sites

Active site

402

1

By similarity

Metal binding

100

1

Zinc 2; in inhibited form By similarity

Metal binding

131

1

Calcium 1 By similarity

Metal binding

165

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

175

1

Zinc 1; structural By similarity

Metal binding

177

1

Zinc 1; structural By similarity

Metal binding

182

1

Calcium 3 By similarity

Metal binding

183

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

185

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

187

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

190

1

Zinc 1; structural By similarity

Metal binding

197

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

199

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

201

1

Calcium 2 By similarity

Metal binding

203

1

Zinc 1; structural By similarity

Metal binding

205

1

Calcium 3 By similarity

Metal binding

206

1

Calcium 1 By similarity

Metal binding

208

1

Calcium 1 By similarity

Metal binding

208

1

Calcium 3 By similarity

Metal binding

401

1

Zinc 2; catalytic By similarity

Metal binding

405

1

Zinc 2; catalytic By similarity

Metal binding

411

1

Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation

39

1

N-linked (GlcNAc...) Potential

Glycosylation

120

1

N-linked (GlcNAc...) Potential

Glycosylation

127

1

N-linked (GlcNAc...) Potential

Disulfide bond

230 ↔ 256

By similarity

Disulfide bond

244 ↔ 271

By similarity

Disulfide bond

288 ↔ 314

By similarity

Disulfide bond

302 ↔ 329

By similarity

Disulfide bond

347 ↔ 373

By similarity

Disulfide bond

361 ↔ 388

By similarity

Disulfide bond

534 ↔ 729

By similarity

Natural variations

Natural variant

1

A → P

Natural variant

639

1

P → L

Natural variant

1

P → H

Experimental info

Sequence conflict

20

1

A → C in AAB28942. Ref.2

Sequence conflict

25 – 26

2

QP → HA in AAB28942. Ref.2

Sequence conflict

466

1

P → T in BAB23442. Ref.5

Sequence conflict

1

A → P in BAA02208. Ref.1

Sequence conflict

1

A → P in CAA51314. Ref.3

Sequence conflict

1

A → P in BAB23442. Ref.5

Sequence conflict

639

1

P → L in CAA51314. Ref.3

Sequence conflict

639

1

P → L in BAB23442. Ref.5

Sequence conflict

1

P → H in BAA02208. Ref.1

Sequence conflict

1

P → H in CAA51314. Ref.3

Sequence conflict

1

P → H in BAB23442. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P41245-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: E1911F6D5CCAC059
Show »

FASTA

730

80,453

        10         20         30         40         50         60 
MSPWQPLLLA LLAFGCSSAA PYQRQPTFVV FPKDLKTSNL TDTQLAEAYL YRYGYTRAAQ 

        70         80         90        100        110        120 
MMGEKQSLRP ALLMLQKQLS LPQTGELDSQ TLKAIRTPRC GVPDVGRFQT FKGLKWDHHN 

       130        140        150        160        170        180 
ITYWIQNYSE DLPRDMIDDA FARAFAVWGE VAPLTFTRVY GPEADIVIQF GVAEHGDGYP 

       190        200        210        220        230        240 
FDGKDGLLAH AFPPGAGVQG DAHFDDDELW SLGKGVVIPT YYGNSNGAPC HFPFTFEGRS 

       250        260        270        280        290        300 
YSACTTDGRN DGTPWCSTTA DYDKDGKFGF CPSERLYTEH GNGEGKPCVF PFIFEGRSYS 

       310        320        330        340        350        360 
ACTTKGRSDG YRWCATTANY DQDKLYGFCP TRVDATVVGG NSAGELCVFP FVFLGKQYSS 

       370        380        390        400        410        420 
CTSDGRRDGR LWCATTSNFD TDKKWGFCPD QGYSLFLVAA HEFGHALGLD HSSVPEALMY 

       430        440        450        460        470        480 
PLYSYLEGFP LNKDDIDGIQ YLYGRGSKPD PRPPATTTTE PQPTAPPTMC PTIPPTAYPT 

       490        500        510        520        530        540 
VGPTVGPTGA PSPGPTSSPS PGPTGAPSPG PTAAPTAGSS EASTESLSPA DNPCNVDVFD 

       550        560        570        580        590        600 
AIAEIQGALH FFKDGWYWKF LNHRGSPLQG PFLTARTWPA LPATLDSAFE DPQTKRVFFF 

       610        620        630        640        650        660 
SGRQMWVYTG KTVLGPRSLD KLGLGPEVTH VSGLLPRRPG KALLFSKGRV WRFDLKSQKV 

       670        680        690        700        710        720 
DPQSVIRVDK EFSGVPWNSH DIFQYQDKAY FCHGKFFWRV SFQNEVNKVD PEVNQVDDVG 

       730 
YVTYDLLQCP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of the mouse 105-kDa gelatinase cDNA." Tanaka H., Hojo K., Yoshida H., Yoshioka T., Sugita K. Biochem. Biophys. Res. Commun. 190:732-740(1993) [PubMed: 8382489] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning and expression of the cDNA encoding mouse neutrophil gelatinase: demonstration of coordinate secondary granule protein gene expression during terminal neutrophil maturation." Graubert T., Johnston J., Berliner N. Blood 82:3192-3197(1993) [PubMed: 8219207] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Mouse gelatinase B. cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation." Masure S., Nys G., Fiten P., van Damme J., Opdenakker G. Eur. J. Biochem. 218:129-141(1993) [PubMed: 8243459] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: C57BL/6. Tissue: Liver.
[4]	"High expression of 92-kD type IV collagenase (gelatinase B) in the osteoclast lineage during mouse development." Reponen P., Sahlberg C., Munaut C., Thesleff I., Tryggvason K. J. Cell Biol. 124:1091-1102(1994) [PubMed: 8132709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Bone.
[5]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Lung.
+	Additional computationally mapped references.

Cross-references

Sequence databases
	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.
IPI	IPI00319200.
PIR	I52580. JC1456.
RefSeq	NP_038627.1.
UniGene	Mm.4406
3D structure databases
HSSP	HSSP built from PDB template 1GKC based on UniProtKB P14780.
SMR	P41245. Positions 29-444, 531-730.
ModBase	Search...
Protein-protein interaction databases
STRING	P41245.
Protein family/group databases
MEROPS	M10.004.
Proteomic databases
PRIDE	P41245.
Genome annotation databases
Ensembl	ENSMUST00000017881; ENSMUSP00000017881; ENSMUSG00000017737; Mus musculus. [Genome view]
GeneID	17395.
KEGG	mmu:17395.
Organism-specific databases
MGI	MGI:97011. Mmp9.
Phylogenomic databases
HOGENOM	P41245.
HOVERGEN	P41245.
Enzyme and pathway databases
BRENDA	3.4.24.35. 244.
Gene expression databases
ArrayExpress	P41245.
Bgee	P41245.
CleanEx	MM_MMP9.
Genevestigator	P41245.
GermOnline	ENSMUSG00000017737. Mus musculus.
Family and domain databases
InterPro	IPR000562. FN_type2_col_bd. IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR001818. Pept_M10A_M12B. IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR002477. Peptidoglycan-bd-like. IPR006970. PT. [Graphical view]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
Pfam	PF00040. fn2. 3 hits. PF00045. Hemopexin. 4 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. PF04886. PT. 1 hit. [Graphical view]
PRINTS	PR00013. FNTYPEII. PR00138. MATRIXIN.
ProDom	PD000995. FN_Type_II. 2 hits. [Graphical view] [Entries sharing at least one domain]
SMART	SM00059. FN2. 3 hits. SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00023. FN2_1. 3 hits. PS51092. FN2_2. 3 hits. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

MMP9_MOUSE

Accession

Primary (citable) accession number: P41245
Secondary accession number(s): Q06788, Q9DC02

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	October 13, 2009
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)