Reviewed, UniProtKB/Swiss-Prot P41245 (MMP9_MOUSE)

Names and origin

Protein names

Recommended name:
    Matrix metalloproteinase-9
      Short name=MMP-9
    EC=3.4.24.35
Alternative name(s):
    92 kDa type IV collagenase
    92 kDa gelatinase
    Gelatinase B
      Short name=GELB

Gene names

Name:	Mmp9
Synonyms:	Clg4b

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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.
Subunit structure	Exists as monomer or homodimer; disulfide-linked By similarity. Exists also as heterodimer with a 25 kDa protein By similarity. Interacts with ECM1 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	514	1	A → P
	Natural variant	639	1	P → L
	Natural variant	711	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	514	1	A → P in BAA02208. Ref.1
	Sequence conflict	514	1	A → P in CAA51314. Ref.3
	Sequence conflict	514	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	711	1	P → H in BAA02208. Ref.1
	Sequence conflict	711	1	P → H in CAA51314. Ref.3
	Sequence conflict	711	1	P → H in BAB23442. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P41245-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: E1911F6D5CCAC059	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

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. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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
EMBL GenBank DDBJ	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
SMR	P41245. Positions 27-729.
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
CTD	17395.
MGI	MGI:97011. Mmp9.
Phylogenomic databases
HOGENOM	HBG747685.
HOVERGEN	P41245.
InParanoid	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. IPR013806. Kringle-like. IPR001818. Pept_M10A_M12B. IPR006026. Peptidase_M. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
Pfam	PF00040. fn2. 3 hits. PF00045. Hemopexin. 3 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
PRINTS	PR00013. FNTYPEII. PR00138. MATRIXIN.
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:	February 9, 2010
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)