Stromelysin-1 precursor - Mus musculus (Mouse)

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P28862 (MMP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Stromelysin-1
Short name=SL-1
EC=3.4.24.17

Alternative name(s):
EMS-2
Matrix metalloproteinase-3
Short name=MMP-3
Transin-1

Gene names

Name:

Mmp3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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.
Sequence caution	The sequence CAA44860.1 differs from that shown. Reason: Erroneous initiation.

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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to amino acid stimulus Inferred from direct assay PubMed 20548288. Source: MGI collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell migration Inferred from mutant phenotype PubMed 11869290. Source: MGI
Cellular_component	extracellular region Traceable author statement. Source: Reactome intracellular membrane-bounded organelle Inferred from electronic annotation. Source: Compara proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

Probable

Propeptide

18 – 99

Activation peptide

PRO_0000028730

Chain

100 – 477

378

Stromelysin-1

PRO_0000028731

Regions

Domain

296 – 338

Hemopexin-like 1

Domain

340 – 383

Hemopexin-like 2

Domain

388 – 435

Hemopexin-like 3

Domain

437 – 477

Hemopexin-like 4

Motif

90 – 97

Cysteine switch By similarity

Sites

Active site

219

By similarity

Metal binding

Zinc 2; in inhibited form By similarity

Metal binding

124

Calcium 1 By similarity

Metal binding

158

Calcium 2 By similarity

Metal binding

168

Zinc 1 By similarity

Metal binding

170

Zinc 1 By similarity

Metal binding

175

Calcium 3 By similarity

Metal binding

176

Calcium 3; via carbonyl oxygen By similarity

Metal binding

178

Calcium 3; via carbonyl oxygen By similarity

Metal binding

180

Calcium 3; via carbonyl oxygen By similarity

Metal binding

183

Zinc 1 By similarity

Metal binding

190

Calcium 2; via carbonyl oxygen By similarity

Metal binding

192

Calcium 2; via carbonyl oxygen By similarity

Metal binding

194

Calcium 2 By similarity

Metal binding

196

Zinc 1 By similarity

Metal binding

198

Calcium 3 By similarity

Metal binding

199

Calcium 1 By similarity

Metal binding

201

Calcium 1 By similarity

Metal binding

201

Calcium 3 By similarity

Metal binding

218

Zinc 2; catalytic By similarity

Metal binding

222

Zinc 2; catalytic By similarity

Metal binding

228

Zinc 2; catalytic By similarity

Metal binding

297

Calcium 4; via carbonyl oxygen By similarity

Metal binding

389

Calcium 4; via carbonyl oxygen By similarity

Metal binding

438

Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation

120

N-linked (GlcNAc...) Potential

Disulfide bond

290 ↔ 477

By similarity

Experimental info

Sequence conflict

468

I → T Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P28862 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 9C15594F45262D37
Show »

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

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References

[1]	"Cloning and sequencing of a cDNA encoding mouse stromelysin 1." Hammani K., Henriet P., Eeckhout Y. Gene 120:321-322(1992) [PubMed] [Europe PMC] [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] [Europe PMC] [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. NM_010809.1.
UniGene	Mm.4993.
3D structure databases
ProteinModelPortal	P28862.
SMR	P28862. Positions 32-477.
ModBase	Search...
Protein family/group databases
MEROPS	M10.005.
PTM databases
PhosphoSite	P28862.
Proteomic databases
PRIDE	P28862.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	17392.
KEGG	mmu:17392.
Organism-specific databases
CTD	4314.
MGI	MGI:97010. Mmp3.
Phylogenomic databases
eggNOG	NOG258253.
HOVERGEN	HBG052484.
InParanoid	P28862.
KO	K01394.
OrthoDB	EOG4KKZ2X.
Enzyme and pathway databases
Reactome	REACT_115202. Signal Transduction.
Gene expression databases
ArrayExpress	P28862.
Bgee	P28862.
CleanEx	MM_MMP3.
Genevestigator	P28862.
GermOnline	ENSMUSG00000043613. Mus musculus.
Family and domain databases
Gene3D	2.110.10.10. 1 hit. 3.40.390.10. 1 hit.
InterPro	IPR000585. Hemopexin-like_dom. IPR018487. Hemopexin-like_repeat. IPR018486. Hemopexin_CS. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR021190. Pept_M10A. IPR016293. Pept_M10A_Metazoans. IPR021158. Pept_M10A_Zn_BS. IPR006026. Peptidase_Metallo. IPR002477. Peptidoglycan-bd-like. [Graphical view]
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]
SUPFAM	SSF50923. Hemopexin. 1 hit. SSF47090. PGBD_like. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents