Reviewed, UniProtKB/Swiss-Prot P03957 (MMP3_RAT)

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
    PTR1 protein

Gene names

Name:

Mmp3

Organism

Rattus norvegicus (Rat)

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	Direct protein sequencing
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro response to amino acid stimulus Inferred from expression pattern. Source: RGD response to cytokine stimulus Inferred from expression pattern. Source: RGD
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 – 97	80	Activation peptide		PRO_0000028734
	Chain	98 – 475	378	Stromelysin-1		PRO_0000028735
Regions
	Domain	294 – 336	43	Hemopexin-like 1
	Domain	338 – 381	44	Hemopexin-like 2
	Domain	386 – 433	48	Hemopexin-like 3
	Domain	435 – 475	41	Hemopexin-like 4
	Motif	88 – 95	8	Cysteine switch By similarity
Sites
	Active site	217	1
	Metal binding	90	1	Zinc 2; in inhibited form By similarity
	Metal binding	122	1	Calcium 1 By similarity
	Metal binding	156	1	Calcium 2 By similarity
	Metal binding	166	1	Zinc 1 By similarity
	Metal binding	168	1	Zinc 1 By similarity
	Metal binding	173	1	Calcium 3 By similarity
	Metal binding	174	1	Calcium 3; via carbonyl oxygen 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	181	1	Zinc 1 By similarity
	Metal binding	188	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	190	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	192	1	Calcium 2 By similarity
	Metal binding	194	1	Zinc 1 By similarity
	Metal binding	196	1	Calcium 3 By similarity
	Metal binding	197	1	Calcium 1 By similarity
	Metal binding	199	1	Calcium 1 By similarity
	Metal binding	199	1	Calcium 3 By similarity
	Metal binding	216	1	Zinc 2; catalytic By similarity
	Metal binding	220	1	Zinc 2; catalytic By similarity
	Metal binding	226	1	Zinc 2; catalytic By similarity
	Metal binding	295	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	387	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	436	1	Calcium 4; via carbonyl oxygen By similarity
Amino acid modifications
	Glycosylation	118	1	N-linked (GlcNAc...) Potential
	Disulfide bond	288 ↔ 475		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P03957-1 [UniParc]. Last modified October 23, 1986. Version 1. Checksum: D81239DC3E26782E	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

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: 3875482] [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: 2431284] [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: 1963430] [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: 2841336] [Abstract] Cited for: MUTAGENESIS, CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X02601 mRNA. Translation: CAA26448.1.
IPI	IPI00324928.
PIR	KCRTIH. A00997.
RefSeq	NP_598207.1.
UniGene	Rn.32086
3D structure databases
HSSP	HSSP built from PDB template 1HY7 based on UniProtKB P08254.
ModBase	Search...
Protein-protein interaction databases
STRING	P03957.
Protein family/group databases
MEROPS	M10.005.
Genome annotation databases
Ensembl	ENSRNOT00000012310; ENSRNOP00000012310; ENSRNOG00000032626; Rattus norvegicus. [Genome view]
GeneID	171045.
KEGG	rno:171045.
UCSC	NM_133523. rat.
Organism-specific databases
CTD	171045.
RGD	621317. Mmp3.
Phylogenomic databases
HOVERGEN	P03957.
Enzyme and pathway databases
BRENDA	3.4.24.17. 248.
Gene expression databases
ArrayExpress	P03957.
Genevestigator	P03957.
GermOnline	ENSRNOG00000032626. Rattus norvegicus.
Family and domain databases
InterPro	IPR000585. Hemopexin/matrixin. IPR018486. Hemopexin/matrixin_CS. IPR018487. Hemopexin/matrixin_repeat. IPR001818. Pept_M10A_M12B. IPR016293. Pept_M10A_matrix. IPR006025. Pept_M_Zn_BS. 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	621565.

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:	October 13, 2009
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)