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P28862 (MMP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular 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 repeats.

Sequence caution

The sequence CAA44860.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Probable
Propeptide18 – 9982Activation peptide
PRO_0000028730
Chain100 – 477378Stromelysin-1
PRO_0000028731

Regions

Repeat287 – 33650Hemopexin 1
Repeat337 – 38347Hemopexin 2
Repeat385 – 43349Hemopexin 3
Repeat434 – 47744Hemopexin 4
Motif90 – 978Cysteine switch By similarity

Sites

Active site2191 By similarity
Metal binding921Zinc 2; in inhibited form By similarity
Metal binding1241Calcium 1 By similarity
Metal binding1581Calcium 2 By similarity
Metal binding1681Zinc 1 By similarity
Metal binding1701Zinc 1 By similarity
Metal binding1751Calcium 3 By similarity
Metal binding1761Calcium 3; via carbonyl oxygen By similarity
Metal binding1781Calcium 3; via carbonyl oxygen By similarity
Metal binding1801Calcium 3; via carbonyl oxygen By similarity
Metal binding1831Zinc 1 By similarity
Metal binding1901Calcium 2; via carbonyl oxygen By similarity
Metal binding1921Calcium 2; via carbonyl oxygen By similarity
Metal binding1941Calcium 2 By similarity
Metal binding1961Zinc 1 By similarity
Metal binding1981Calcium 3 By similarity
Metal binding1991Calcium 1 By similarity
Metal binding2011Calcium 1 By similarity
Metal binding2011Calcium 3 By similarity
Metal binding2181Zinc 2; catalytic By similarity
Metal binding2221Zinc 2; catalytic By similarity
Metal binding2281Zinc 2; catalytic By similarity
Metal binding2971Calcium 4; via carbonyl oxygen By similarity
Metal binding3891Calcium 4; via carbonyl oxygen By similarity
Metal binding4381Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation1201N-linked (GlcNAc...) Potential
Disulfide bond290 ↔ 477 By similarity

Experimental info

Sequence conflict4681I → T Ref.3

Sequences

Sequence LengthMass (Da)Tools
P28862 [UniParc].

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

FASTA47753,845
        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 

« Hide

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.
PIRKCMSS1. JC1476.
RefSeqNP_034939.1. NM_010809.1.
UniGeneMm.4993.

3D structure databases

ProteinModelPortalP28862.
SMRP28862. Positions 32-477.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM10.005.

PTM databases

PhosphoSiteP28862.

Proteomic databases

PRIDEP28862.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID17392.
KEGGmmu:17392.

Organism-specific databases

CTD4314.
MGIMGI:97010. Mmp3.

Phylogenomic databases

eggNOGNOG258253.
HOVERGENHBG052484.
InParanoidP28862.
KOK01394.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_206066. Extracellular matrix organization.

Gene expression databases

ArrayExpressP28862.
BgeeP28862.
CleanExMM_MMP3.
GenevestigatorP28862.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
IPR028700. Stromelysin_1.
[Graphical view]
PANTHERPTHR10201:SF38. PTHR10201:SF38. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio292020.
PROP28862.
SOURCESearch...

Entry information

Entry nameMMP3_MOUSE
AccessionPrimary (citable) accession number: P28862
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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