Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P03957 (MMP3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Matrix metalloproteinase-3
Short name=MMP-3
PTR1 protein
Transin-1
Gene names
Name:Mmp3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Induction

By epidermal growth factor and is increased in FR3T3 and RAT-1 fibroblasts transformed by polyoma virus, Rous sarcoma virus, or the human cellular H-Ras oncogene.

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.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to cell-matrix adhesion

Inferred from expression pattern PubMed 12963432. Source: RGD

cellular response to interleukin-1

Inferred from expression pattern PubMed 16046515. Source: RGD

collagen catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

female pregnancy

Inferred from expression pattern PubMed 15672041. Source: RGD

response to amino acid

Inferred from expression pattern PubMed 17083784. Source: RGD

response to cytokine

Inferred from expression pattern PubMed 10435007. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 19889233. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 15099024. Source: RGD

response to interleukin-1

Inferred from expression pattern PubMed 16290189. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 19345799. Source: RGD

response to tumor necrosis factor

Inferred from expression pattern PubMed 17704356. Source: RGD

wound healing

Inferred from expression pattern PubMed 19834065. Source: RGD

   Cellular_componentcell body

Inferred from direct assay PubMed 18629001. Source: RGD

dendrite

Inferred from direct assay PubMed 18629001. Source: RGD

extracellular space

Inferred from direct assay PubMed 18439420. Source: RGD

nucleus

Inferred from direct assay PubMed 18629001. Source: RGD

protein complex

Inferred from direct assay PubMed 16935996. Source: RGD

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

protein complex binding

Inferred from direct assay PubMed 16935996. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Probable
Propeptide18 – 9780Activation peptide
PRO_0000028734
Chain98 – 475378Stromelysin-1
PRO_0000028735

Regions

Repeat285 – 33450Hemopexin 1
Repeat335 – 38147Hemopexin 2
Repeat383 – 43149Hemopexin 3
Repeat432 – 47544Hemopexin 4
Motif88 – 958Cysteine switch By similarity

Sites

Active site2171
Metal binding901Zinc 2; in inhibited form By similarity
Metal binding1221Calcium 1 By similarity
Metal binding1561Calcium 2 By similarity
Metal binding1661Zinc 1 By similarity
Metal binding1681Zinc 1 By similarity
Metal binding1731Calcium 3 By similarity
Metal binding1741Calcium 3; via carbonyl oxygen By similarity
Metal binding1761Calcium 3; via carbonyl oxygen By similarity
Metal binding1781Calcium 3; via carbonyl oxygen By similarity
Metal binding1811Zinc 1 By similarity
Metal binding1881Calcium 2; via carbonyl oxygen By similarity
Metal binding1901Calcium 2; via carbonyl oxygen By similarity
Metal binding1921Calcium 2 By similarity
Metal binding1941Zinc 1 By similarity
Metal binding1961Calcium 3 By similarity
Metal binding1971Calcium 1 By similarity
Metal binding1991Calcium 1 By similarity
Metal binding1991Calcium 3 By similarity
Metal binding2161Zinc 2; catalytic By similarity
Metal binding2201Zinc 2; catalytic By similarity
Metal binding2261Zinc 2; catalytic By similarity
Metal binding2951Calcium 4; via carbonyl oxygen By similarity
Metal binding3871Calcium 4; via carbonyl oxygen By similarity
Metal binding4361Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation1181N-linked (GlcNAc...) Potential
Disulfide bond288 ↔ 475 By similarity

Sequences

Sequence LengthMass (Da)Tools
P03957 [UniParc].

Last modified October 23, 1986. Version 1.
Checksum: D81239DC3E26782E

FASTA47553,428
        10         20         30         40         50         60 
MKGLPVLLWL CTAVCSSYPL HGSEEDAGME VLQKYLENYY GLEKDVKQFT KKKDSSPVVK 

        70         80         90        100        110        120 
KIQEMQKFLG LKMTGKLDSN TMELMHKPRC GVPDVGGFST FPGSPKWRKN HISYRIVNYT 

       130        140        150        160        170        180 
LDLPRESVDS AIERALKVWE EVTPLTFSRI SEGEADIMIS FAVEEHGDFI PFDGPGMVLA 

       190        200        210        220        230        240 
HAYAPGPGTN GDAHFDDDER WTDDVTGTNL FLVAAHELGH SLGLFHSANA EALMYPVYKS 

       250        260        270        280        290        300 
STDLARFHLS QDDVDGIQSL YGPPTESPDV LVVPTKSNSL DPETLPMCSS ALSFDAVSTL 

       310        320        330        340        350        360 
RGEVLFFKDR HFWRKSLRTP EPGFYLISSF WPSLPSNMDA AYEVTNRDTV FILKGNQIWA 

       370        380        390        400        410        420 
IRGHEELAGY PKSIHTLGLP ETVQKIDAAI SLKDQKKTYF FVEDKFWRFD EKKQSMDPEF 

       430        440        450        460        470 
PRKIAENFPG IGTKVDAVFE AFGFLYFFSG SSQLEFDPNA GKVTHILKSN SWFNC 

« Hide

References

[1]"Epidermal growth factor and oncogenes induce transcription of the same cellular mRNA in rat fibroblasts."
Matrisian L.M., Glaichenhaus N., Gesnel M.-C., Breathnach R.
EMBO J. 4:1435-1440(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Isolation of the oncogene and epidermal growth factor-induced transin gene: complex control in rat fibroblasts."
Matrisian L.M., Gleroy P., Ruhlmann C., Gesnel M.-C., Breathnach R.
Mol. Cell. Biol. 6:1679-1686(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Purification and properties of extracellular matrix-degrading metallo-proteinase overproduced by Rous sarcoma virus-transformed rat liver cell line, and its identification as transin."
Umenishi F., Yasumitsu H., Ashida Y., Yamauti J., Umeda M., Miyazaki K.
J. Biochem. 108:537-543(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-28; 110-119; 309-315 AND 316-325.
[4]"Structure-function relationships in the collagenase family member transin."
Sanchez-Lopez R., Nicholson R., Gesnel M.-C., Matrisian L.M., Breathnach R.
J. Biol. Chem. 263:11892-11899(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02601 mRNA. Translation: CAA26448.1.
PIRKCRTIH. A00997.
UniGeneRn.32086.

3D structure databases

ProteinModelPortalP03957.
SMRP03957. Positions 31-264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000012310.

Protein family/group databases

MEROPSM10.005.

Proteomic databases

PaxDbP03957.
PRIDEP03957.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:621317. rat.

Organism-specific databases

RGD621317. Mmp3.

Phylogenomic databases

eggNOGNOG258253.
HOGENOMHOG000217927.
HOVERGENHBG052484.
InParanoidP03957.
PhylomeDBP03957.

Gene expression databases

GenevestigatorP03957.

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

NextBio13948460.
PROP03957.

Entry information

Entry nameMMP3_RAT
AccessionPrimary (citable) accession number: P03957
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: June 11, 2014
This is version 138 of the entry and version 1 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