Stromelysin-1 precursor - Rattus norvegicus (Rat)

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P03957 (MMP3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 128. History...

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

Documents (2) |

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):
Matrix metalloproteinase-3
Short name=MMP-3
PTR1 protein
Transin-1

Gene names

Name:

Mmp3

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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-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
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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 proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to amino acid stimulus Inferred from expression pattern PubMed 17083784. Source: RGD response to estradiol stimulus Inferred from expression pattern PubMed 19889233. Source: RGD response to hypoxia Inferred from expression pattern PubMed 15099024. 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_component	cell 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_function	calcium 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

Probable

Propeptide

18 – 97

Activation peptide

PRO_0000028734

Chain

98 – 475

378

Stromelysin-1

PRO_0000028735

Regions

Domain

294 – 336

Hemopexin-like 1

Domain

338 – 381

Hemopexin-like 2

Domain

386 – 433

Hemopexin-like 3

Domain

435 – 475

Hemopexin-like 4

Motif

88 – 95

Cysteine switch By similarity

Sites

Active site

217

Metal binding

Zinc 2; in inhibited form By similarity

Metal binding

122

Calcium 1 By similarity

Metal binding

156

Calcium 2 By similarity

Metal binding

166

Zinc 1 By similarity

Metal binding

168

Zinc 1 By similarity

Metal binding

173

Calcium 3 By similarity

Metal binding

174

Calcium 3; via carbonyl oxygen By similarity

Metal binding

176

Calcium 3; via carbonyl oxygen By similarity

Metal binding

178

Calcium 3; via carbonyl oxygen By similarity

Metal binding

181

Zinc 1 By similarity

Metal binding

188

Calcium 2; via carbonyl oxygen By similarity

Metal binding

190

Calcium 2; via carbonyl oxygen By similarity

Metal binding

192

Calcium 2 By similarity

Metal binding

194

Zinc 1 By similarity

Metal binding

196

Calcium 3 By similarity

Metal binding

197

Calcium 1 By similarity

Metal binding

199

Calcium 1 By similarity

Metal binding

199

Calcium 3 By similarity

Metal binding

216

Zinc 2; catalytic By similarity

Metal binding

220

Zinc 2; catalytic By similarity

Metal binding

226

Zinc 2; catalytic By similarity

Metal binding

295

Calcium 4; via carbonyl oxygen By similarity

Metal binding

387

Calcium 4; via carbonyl oxygen By similarity

Metal binding

436

Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation

118

N-linked (GlcNAc...) Potential

Disulfide bond

288 ↔ 475

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P03957 [UniParc].

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

FASTA

475

53,428

        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.
IPI	IPI00324928.
PIR	KCRTIH. A00997.
UniGene	Rn.32086.
3D structure databases
ProteinModelPortal	P03957.
SMR	P03957. Positions 31-264.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000012310.
Protein family/group databases
MEROPS	M10.005.
Proteomic databases
PaxDb	P03957.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:621317. rat.
Organism-specific databases
RGD	621317. Mmp3.
Phylogenomic databases
eggNOG	NOG258253.
HOGENOM	HOG000217927.
HOVERGEN	HBG052484.
InParanoid	P03957.
OrthoDB	EOG4KKZ2X.
Gene expression databases
ArrayExpress	P03957.
Genevestigator	P03957.
GermOnline	ENSRNOG00000032626. Rattus norvegicus.
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	13948460.

Entry information

Entry name

MMP3_RAT

Accession

Primary (citable) accession number: P03957

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 1986
Last sequence update:	October 23, 1986
Last modified:	May 1, 2013
This is version 128 of the entry and version 1 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

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents