Reviewed, UniProtKB/Swiss-Prot P28862 (MMP3_MOUSE)

Names and origin

Protein names

Recommended name:
    Stromelysin-1
      Short name=SL-1
    EC=3.4.24.17
Alternative name(s):
    Matrix metalloproteinase-3
      Short name=MMP-3
    Transin-1
    EMS-2

Gene names

Name:

Mmp3

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	477 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	Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.
Catalytic activity	Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
Cofactor	Binds 4 calcium ions per subunit By similarity. Binds 2 zinc ions per subunit By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix Probable.
Developmental stage	Present in unfertilized eggs and at the zygote and cleavage stages. Levels increase at the blastocyst stage and with endoderm differentiation. Ref.3
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.
Sequence similarities	Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.

Ontologies

Keywords
Biological process	Collagen degradation
Cellular component	Extracellular matrix Secreted
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 electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	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 electronic annotation. Source: InterPro 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 – 17	17	Probable
	Propeptide	18 – 99	82	Activation peptide		PRO_0000028730
	Chain	100 – 477	378	Stromelysin-1		PRO_0000028731
Regions
	Domain	296 – 338	43	Hemopexin-like 1
	Domain	340 – 383	44	Hemopexin-like 2
	Domain	388 – 435	48	Hemopexin-like 3
	Domain	437 – 477	41	Hemopexin-like 4
	Motif	90 – 97	8	Cysteine switch By similarity
Sites
	Active site	219	1	By similarity
	Metal binding	92	1	Zinc 2; in inhibited form By similarity
	Metal binding	124	1	Calcium 1 By similarity
	Metal binding	158	1	Calcium 2 By similarity
	Metal binding	168	1	Zinc 1 By similarity
	Metal binding	170	1	Zinc 1 By similarity
	Metal binding	175	1	Calcium 3 By similarity
	Metal binding	176	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	178	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	180	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	183	1	Zinc 1 By similarity
	Metal binding	190	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	192	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	194	1	Calcium 2 By similarity
	Metal binding	196	1	Zinc 1 By similarity
	Metal binding	198	1	Calcium 3 By similarity
	Metal binding	199	1	Calcium 1 By similarity
	Metal binding	201	1	Calcium 1 By similarity
	Metal binding	201	1	Calcium 3 By similarity
	Metal binding	218	1	Zinc 2; catalytic By similarity
	Metal binding	222	1	Zinc 2; catalytic By similarity
	Metal binding	228	1	Zinc 2; catalytic By similarity
	Metal binding	297	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	389	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	438	1	Calcium 4; via carbonyl oxygen By similarity
Amino acid modifications
	Glycosylation	120	1	N-linked (GlcNAc...) Potential
	Disulfide bond	290 ↔ 477		By similarity
Experimental info
	Sequence conflict	468	1	I → T Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P28862-1 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 9C15594F45262D37	FASTA	477	53,845
	10 20 30 40 50 60 MKGLPVLLWL CVVVCSSYPL HDSARDDDAG MELLQKYLEN YYGLAKDVKQ FIKKKDSSLI 70 80 90 100 110 120 VKKIQEMQKF LGLEMTGKLD SNTMELMHKP RCGVPDVGGF STFPGSPKWR KSHITYRIVN 130 140 150 160 170 180 YTPDLPRQSV DSAIEKALKV WEEVTPLTFS RISEGEADIM ISFAVGEHGD FVPFDGPGTV 190 200 210 220 230 240 LAHAYAPGPG INGDAHFDDD ERWTEDVTGT NLFLVAAHEL GHSLGLYHSA KAEALMYPVY 250 260 270 280 290 300 KSSTDLSRFH LSQDDVDGIQ SLYGTPTASP DVLVVPTKSN SLEPETSPMC SSTLFFDAVS 310 320 330 340 350 360 TLRGEVLFFK DRHFWRKSLR TPEPEFYLIS SFWPSLPSNM DAAYEVTNRD TVFIFKGNQF 370 380 390 400 410 420 WAIRGHEELA GYPKSIHTLG LPATVKKIDA AISNKEKRKT YFFVEDKYWR FDEKKQSMEP 430 440 450 460 470 GFPRKIAEDF PGVDSRVDAV FEAFGFLYFF SGSSQLEFDP NAKKVTHILK SNSWFNC

References

[1]	"Cloning and sequencing of a cDNA encoding mouse stromelysin 1." Hammani K., Henriet P., Eeckhout Y. Gene 120:321-322(1992) [PubMed: 1398148] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: NMRI. Tissue: Calvaria.
[2]	Li F., Strange R., Saurer S., Niemann H., Friis R.R. Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss.
[3]	"Genes for extracellular-matrix-degrading metalloproteinases and their inhibitor, TIMP, are expressed during early mammalian development." Brenner C.A., Adler R.R., Rappolee D.A., Pedersen R.A., Werb Z. Genes Dev. 3:848-859(1989) [PubMed: 2744464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 415-469, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X66402 mRNA. Translation: CAA47029.1. X63162 mRNA. Translation: CAA44860.1. Different initiation.
IPI	IPI00123511.
PIR	KCMSS1. JC1476.
RefSeq	NP_034939.1.
UniGene	Mm.4993
3D structure databases
SMR	P28862. Positions 33-266, 287-477.
ModBase	Search...
Protein-protein interaction databases
STRING	P28862.
Protein family/group databases
MEROPS	M10.005.
PTM databases
PhosphoSite	P28862.
Proteomic databases
PRIDE	P28862.
Genome annotation databases
Ensembl	ENSMUST00000034497; ENSMUSP00000034497; ENSMUSG00000043613; Mus musculus. [Genome view]
GeneID	17392.
KEGG	mmu:17392.
UCSC	uc009oco.1. mouse.
Organism-specific databases
CTD	17392.
MGI	MGI:97010. Mmp3.
Phylogenomic databases
eggNOG	roNOG10274.
HOVERGEN	P28862.
InParanoid	P28862.
OrthoDB	EOG9NP9NP.
PhylomeDB	P28862.
Enzyme and pathway databases
BRENDA	3.4.24.17. 244.
Gene expression databases
ArrayExpress	P28862.
Bgee	P28862.
CleanEx	MM_MMP3.
Genevestigator	P28862.
GermOnline	ENSMUSG00000043613. Mus musculus.
Family and domain databases
InterPro	IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR001818. Pept_M10A_M12B. IPR016293. Pept_M10A_matrix. IPR006026. Peptidase_M. IPR002477. Peptidoglycan-bd-like. [Graphical view]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
Pfam	PF00045. Hemopexin. 4 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTS	PR00138. MATRIXIN.
SMART	SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	292020.
SOURCE	Search...

Entry information

Entry name

MMP3_MOUSE

Accession

Primary (citable) accession number: P28862

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	February 1, 1994
Last modified:	January 19, 2010
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)