Reviewed, UniProtKB/Swiss-Prot P28863 (MMP3_RABIT)

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

Gene names

Name:

MMP3

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	478 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.
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
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell 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 – 100	83	Activation peptide		PRO_0000028732
	Chain	101 – 478	378	Stromelysin-1		PRO_0000028733
Regions
	Domain	297 – 339	43	Hemopexin-like 1
	Domain	341 – 384	44	Hemopexin-like 2
	Domain	389 – 436	48	Hemopexin-like 3
	Domain	438 – 478	41	Hemopexin-like 4
	Motif	91 – 98	8	Cysteine switch By similarity
Sites
	Active site	220	1	By similarity
	Metal binding	93	1	Zinc 2; in inhibited form By similarity
	Metal binding	125	1	Calcium 1 By similarity
	Metal binding	159	1	Calcium 2 By similarity
	Metal binding	169	1	Zinc 1 By similarity
	Metal binding	171	1	Zinc 1 By similarity
	Metal binding	176	1	Calcium 3 By similarity
	Metal binding	177	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	179	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	181	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	184	1	Zinc 1 By similarity
	Metal binding	191	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	193	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	195	1	Calcium 2 By similarity
	Metal binding	197	1	Zinc 1 By similarity
	Metal binding	199	1	Calcium 3 By similarity
	Metal binding	200	1	Calcium 1 By similarity
	Metal binding	202	1	Calcium 1 By similarity
	Metal binding	202	1	Calcium 3 By similarity
	Metal binding	219	1	Zinc 2; catalytic By similarity
	Metal binding	223	1	Zinc 2; catalytic By similarity
	Metal binding	229	1	Zinc 2; catalytic By similarity
	Metal binding	298	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	390	1	Calcium 4; via carbonyl oxygen By similarity
	Metal binding	439	1	Calcium 4; via carbonyl oxygen By similarity
Amino acid modifications
	Glycosylation	121	1	N-linked (GlcNAc...) Potential
	Disulfide bond	291 ↔ 478		By similarity
Experimental info
	Sequence conflict	83	1	N → D Ref.2
	Sequence conflict	128	1	R → K Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P28863-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: CA742E31A4549D40	FASTA	478	53,942
	10 20 30 40 50 60 MKTLPTLLLL CVALCSAYPL DGASRDADTT NMDLLQQYLE NYYNLEKDVK QFVKRKDSSP 70 80 90 100 110 120 VVKKIQEMQK FLGLEVTGKL DSNTLEVIRK PRCGVPDVGH FSTFPGTPKW TKTHLTYRIV 130 140 150 160 170 180 NYTPDLPRDA VDAAIEKALK VWEEVTPLTF SRKYEGEADI MISFGVREHG DFIPFDGPGN 190 200 210 220 230 240 VLAHAYAPGP GINGDAHFDD DEQWTKDTTG TNLFLVAAHE LGHSLGLFHS ANPEALMYPV 250 260 270 280 290 300 YNAFTDLARF RLSQDDVDGI QSLYGPAPAS PDNSGVPMEP VPPGSGTPVM CDPDLSFDAI 310 320 330 340 350 360 STLRGEILFF KDRYFWRKSL RILEPEFHLI SSFWPSLPSA VDAAYEVISR DTVFIFKGTQ 370 380 390 400 410 420 FWAIRGNEVQ AGYPRSIHTL GFPSTIRKID AAISDKERKK TYFFVEDKYW RFDEKRQSLE 430 440 450 460 470 PGFPRHIAED FPGINPKIDA VFEAFGFFYF FSGSSQSEFD PNAKKVTHVL KSNSWFQC

References

[1]

"Cloning of a complementary DNA for rabbit proactivator. A metalloproteinase that activates synovial cell collagenase, shares homology with stromelysin and transin, and is coordinately regulated with collagenase." Fini M.E., Karmilowicz M.J., Ruby P.L., Beeman A.M., Borges K.A., Brinckerhoff C.E. Arthritis Rheum. 30:1254-1264(1987) [PubMed: 2825726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

[2]

"Comparison of human stromelysin and collagenase by cloning and sequence analysis." Whitham S.E., Murphy G., Angel P., Rahmsdorf H.J., Smith B., Lyons A., Harris T.J.R., Reynolds J.J., Herrlich P., Docherty A.J.P. Biochem. J. 240:913-916(1986) [PubMed: 3030290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-167.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M25664 mRNA. Translation: AAA31467.1.
PIR	KCRBS1. A37306.
RefSeq	NP_001075749.1.
UniGene	Ocu.1964
3D structure databases
HSSP	HSSP built from PDB template 1G05 based on UniProtKB P08254.
ModBase	Search...
Protein family/group databases
MEROPS	M10.005.
Genome annotation databases
Ensembl	ENSOCUG00000015230. Oryctolagus cuniculus. [Contig view]
GeneID	100009111.
Phylogenomic databases
HOVERGEN	P28863.
OMA	P28863. DDEQWTK.
Enzyme and pathway databases
BRENDA	3.4.24.17. 255.
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...

Entry information

Entry name

MMP3_RABIT

Accession

Primary (citable) accession number: P28863

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)