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Protein

Stromelysin-1

Gene

MMP3

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase (By similarity).By similarity

Catalytic activityi

Preferential cleavage where P1', P2' and P3' are hydrophobic residues.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Zinc 2; in inhibited formBy similarity
Metal bindingi124 – 1241Calcium 1By similarity
Metal bindingi158 – 1581Calcium 2By similarity
Metal bindingi168 – 1681Zinc 1By similarity
Metal bindingi170 – 1701Zinc 1By similarity
Metal bindingi175 – 1751Calcium 3By similarity
Metal bindingi176 – 1761Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi178 – 1781Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi183 – 1831Zinc 1By similarity
Metal bindingi190 – 1901Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi194 – 1941Calcium 2By similarity
Metal bindingi196 – 1961Zinc 1By similarity
Metal bindingi198 – 1981Calcium 3By similarity
Metal bindingi199 – 1991Calcium 1By similarity
Metal bindingi201 – 2011Calcium 1By similarity
Metal bindingi201 – 2011Calcium 3By similarity
Metal bindingi218 – 2181Zinc 2; catalyticBy similarity
Active sitei219 – 2191PROSITE-ProRule annotation
Metal bindingi222 – 2221Zinc 2; catalyticBy similarity
Metal bindingi228 – 2281Zinc 2; catalyticBy similarity
Metal bindingi298 – 2981Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi390 – 3901Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi439 – 4391Calcium 4; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-CFA-1442490. Collagen degradation.
R-CFA-1474228. Degradation of the extracellular matrix.
R-CFA-1592389. Activation of Matrix Metalloproteinases.
R-CFA-2179392. EGFR Transactivation by Gastrin.

Protein family/group databases

MEROPSiM10.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Stromelysin-1 (EC:3.4.24.17)
Short name:
SL-1
Alternative name(s):
Matrix metalloproteinase-3
Short name:
MMP-3
Gene namesi
Name:MMP3
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Propeptidei18 – 9982Activation peptideBy similarityPRO_0000028724Add
BLAST
Chaini100 – 478379Stromelysin-1PRO_0000028725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi291 ↔ 478By similarity
Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiQ6Y4Q5.

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000022195.

Structurei

3D structure databases

ProteinModelPortaliQ6Y4Q5.
SMRiQ6Y4Q5. Positions 33-267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati288 – 33750Hemopexin 1Add
BLAST
Repeati338 – 38447Hemopexin 2Add
BLAST
Repeati386 – 43449Hemopexin 3Add
BLAST
Repeati435 – 47844Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine switchBy similarity

Domaini

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 similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ6Y4Q5.
KOiK01394.
OMAiVAVCSAY.
OrthoDBiEOG091G03DP.
TreeFamiTF315428.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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]
PANTHERiPTHR10201:SF164. PTHR10201:SF164. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6Y4Q5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNLPALLLF CGVVCSAYPV DRAAEDENNN MELTQQYLEN YYNLGKDVKP
60 70 80 90 100
FVRRRNSGPV VEKIREMQKF LGLEVTGKVD SDTLAMMRRP RCGVPDVGDF
110 120 130 140 150
TTFPGMPKWR KTHLTYRIMN YTPDLPRDAV DSAIEKALNV WKEVTPLTFS
160 170 180 190 200
RTDEGEADIK ISFAVRDHGD FNPFDGPGNV LGHAYPPGPG IYGDAHFDDD
210 220 230 240 250
EQWTSDTSGT NLFLVAAHEL GHSLGLFHSA DPSALMYPVY NVLADLARFH
260 270 280 290 300
LSQDDVNGIQ SLYGGPPSDS SNDPVVPTES VPPGPGTPAA CDPTLSFDAI
310 320 330 340 350
STLRGEFLFF KDRHFWRKSL RTLEPGFYLI SSFWPSLPSG LDAAYEETSK
360 370 380 390 400
DIVFIFKGNQ FWAMRGTEVQ AGYPKGIHTL GFPPTVKKID AAVFDKEKKK
410 420 430 440 450
TYFFVGDKYW RFDEKRQSME PGFPKQIAED FPGVDSKVDA AFEAFGFYYF
460 470
FNGSSQLEFD PNAKKVTHVL KSNSWLNC
Length:478
Mass (Da):53,633
Last modified:July 5, 2004 - v1
Checksum:i5D1B9DA9D57BC041
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY183143 mRNA. Translation: AAO63580.1.
RefSeqiNP_001002967.1. NM_001002967.1.
UniGeneiCfa.3447.

Genome annotation databases

EnsembliENSCAFT00000023908; ENSCAFP00000022195; ENSCAFG00000015063.
GeneIDi403445.
KEGGicfa:403445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY183143 mRNA. Translation: AAO63580.1.
RefSeqiNP_001002967.1. NM_001002967.1.
UniGeneiCfa.3447.

3D structure databases

ProteinModelPortaliQ6Y4Q5.
SMRiQ6Y4Q5. Positions 33-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000022195.

Protein family/group databases

MEROPSiM10.005.

Proteomic databases

PaxDbiQ6Y4Q5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000023908; ENSCAFP00000022195; ENSCAFG00000015063.
GeneIDi403445.
KEGGicfa:403445.

Organism-specific databases

CTDi4314.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ6Y4Q5.
KOiK01394.
OMAiVAVCSAY.
OrthoDBiEOG091G03DP.
TreeFamiTF315428.

Enzyme and pathway databases

ReactomeiR-CFA-1442490. Collagen degradation.
R-CFA-1474228. Degradation of the extracellular matrix.
R-CFA-1592389. Activation of Matrix Metalloproteinases.
R-CFA-2179392. EGFR Transactivation by Gastrin.

Family and domain databases

CDDicd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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]
PANTHERiPTHR10201:SF164. PTHR10201:SF164. 1 hit.
PfamiPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP3_CANLF
AccessioniPrimary (citable) accession number: Q6Y4Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.