Reviewed, UniProtKB/Swiss-Prot Q28397 (MMP3_HORSE)

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

Gene names

Name:

MMP3

Organism

Equus caballus (Horse)

Taxonomic identifier

9796 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Protein attributes

Sequence length	477 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 matrixProbable.
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	Glycoprotein Zymogen
Technical term	3D-structure
Gene Ontology (GO)
Biological process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	proteinaceous extracellular matrix Inferred from electronic annotation. Source: InterPro
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: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Propeptide

18 – 99

82

Activation peptide

PRO_0000028726

Chain

100 – 477

378

Stromelysin-1

PRO_0000028727

Regions

Domain

296 – 338

43

Hemopexin-like 1

Domain

340 – 383

44

Hemopexin-like 2

Domain

388 – 435

48

Hemopexin-like 3

Domain

437 – 477

41

Hemopexin-like 4

Motif

90 – 97

8

Cysteine switch By similarity

Sites

Active site

219

1

By similarity

Metal binding

92

1

Zinc 2; in inhibited form By similarity

Metal binding

124

1

Calcium 1 By similarity

Metal binding

158

1

Calcium 2 By similarity

Metal binding

168

1

Zinc 1 By similarity

Metal binding

170

1

Zinc 1 By similarity

Metal binding

175

1

Calcium 3 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

180

1

Calcium 3; via carbonyl oxygen By similarity

Metal binding

183

1

Zinc 1 By similarity

Metal binding

190

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

192

1

Calcium 2; via carbonyl oxygen By similarity

Metal binding

194

1

Calcium 2 By similarity

Metal binding

196

1

Zinc 1 By similarity

Metal binding

198

1

Calcium 3 By similarity

Metal binding

199

1

Calcium 1 By similarity

Metal binding

201

1

Calcium 1 By similarity

Metal binding

201

1

Calcium 3 By similarity

Metal binding

218

1

Zinc 2; catalytic By similarity

Metal binding

222

1

Zinc 2; catalytic By similarity

Metal binding

228

1

Zinc 2; catalytic By similarity

Metal binding

297

1

Calcium 4; via carbonyl oxygen By similarity

Metal binding

389

1

Calcium 4; via carbonyl oxygen By similarity

Metal binding

438

1

Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation

120

1

N-linked (GlcNAc...) Potential

Disulfide bond

290 ↔ 477

By similarity

Experimental info

Sequence conflict

346

1

V → E Ref.2

Secondary structure

1

.

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477

Helix Strand Turn

Details...

Beta strand

110 – 118

9

Helix

127 – 144

18

Beta strand

148 – 151

4

Beta strand

153 – 155

3

Beta strand

158 – 164

7

Beta strand

169 – 172

4

Beta strand

176 – 179

4

Beta strand

182 – 184

3

Beta strand

187 – 189

3

Turn

190 – 193

4

Beta strand

195 – 198

4

Beta strand

203 – 211

9

Helix

212 – 224

13

Beta strand

237 – 239

3

Beta strand

246 – 248

3

Helix

253 – 263

11

Sequences

	Sequence		Length	Mass (Da)
	Q28397-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 361CE1427E09A272	FASTA	477	54,190
	10 20 30 40 50 60 MKNLPILLLL CVAACSAYPL DRSARDEDSN MDLLQDYLEK YYDLGKEMRQ YVRRKDSGPI 70 80 90 100 110 120 VKKIQEMQKF LGLKVTGKLD SDTVEVMHKS RCGVPDVGHF TTFPGMPKWS KTHLTYRIVN 130 140 150 160 170 180 YTQDLPRDAV DSDVEKALKI WEEVTPLTFS RIYEGEADIM ITFAVREHGD FFPFDGPGKV 190 200 210 220 230 240 LAHAYPPGPG MNGDAHFDDD EHWTKDASGI NFLLVAAHEL GHSLGLYHST NTEALMYPLY 250 260 270 280 290 300 NTLKGPARVR LSQDDVTGIQ SLYGPPPASP DSPVEPSEPE PPAPGTLAMC DPALSFDAIS 310 320 330 340 350 360 TLRGEILFFK DRYFWRKTFR TLVPEFHPIS SFWPSLPSGI DAAYEVTSRD SVFIFKGNKF 370 380 390 400 410 420 WAIRGNEEQA GYPRGIHTLG FPPTVRKIDA AIFDKEKQKT YFFVEDKYWR FDEKRQSMEP 430 440 450 460 470 GYPKQIAEDF PGIDSKLDAA FESFGFFYFF SGSSQFEFDP NAKKVTHVLK SNSWFNC

References

[1]	"Molecular characteristics of equine stromelysin and the tissue inhibitor of metalloproteinase 1." Richardson D.W., Dodge G.R. Am. J. Vet. Res. 59:1557-1562(1998) [PubMed: 9858406] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cartilage.
[2]	"Molecular cloning and cartilage gene expression of equine stromelysin 1 (matrix metalloproteinase 3)." Balkman C.E., Nixon A.J. Am. J. Vet. Res. 59:30-36(1998) [PubMed: 9442239] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cartilage.
[3]	"Theoretical model of horse stromelysin." Mallena S.C., Sharma J.A.R.P. Submitted (MAR-2002) to the PDB data bank Cited for: 3D-STRUCTURE MODELING.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U62529 mRNA. Translation: AAB05774.1.

RefSeq

NP_001075964.1.

UniGene

Eca.8032

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L9I	model	-	A	100-267	[»]

ModBase

Search...

Protein family/group databases

MEROPS

M10.005.

Genome annotation databases

GeneID

100034195.

Phylogenomic databases

HOVERGEN

Q28397.

Family and domain databases

InterPro

IPR000585. Hemopexin.
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. False negative.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MMP3_HORSE

Accession

Primary (citable) accession number: Q28397

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	November 25, 2008
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)