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Q6Y4Q5 (MMP3_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity.

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 By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 9982Activation peptide By similarity
PRO_0000028724
Chain100 – 478379Stromelysin-1
PRO_0000028725

Regions

Domain297 – 33943Hemopexin-like 1
Domain341 – 38444Hemopexin-like 2
Domain389 – 43648Hemopexin-like 3
Domain438 – 47841Hemopexin-like 4
Motif90 – 978Cysteine switch By similarity

Sites

Active site2191 By similarity
Metal binding921Zinc 2; in inhibited form By similarity
Metal binding1241Calcium 1 By similarity
Metal binding1581Calcium 2 By similarity
Metal binding1681Zinc 1 By similarity
Metal binding1701Zinc 1 By similarity
Metal binding1751Calcium 3 By similarity
Metal binding1761Calcium 3; via carbonyl oxygen By similarity
Metal binding1781Calcium 3; via carbonyl oxygen By similarity
Metal binding1801Calcium 3; via carbonyl oxygen By similarity
Metal binding1831Zinc 1 By similarity
Metal binding1901Calcium 2; via carbonyl oxygen By similarity
Metal binding1941Calcium 2 By similarity
Metal binding1961Zinc 1 By similarity
Metal binding1981Calcium 3 By similarity
Metal binding1991Calcium 1 By similarity
Metal binding2011Calcium 1 By similarity
Metal binding2011Calcium 3 By similarity
Metal binding2181Zinc 2; catalytic By similarity
Metal binding2221Zinc 2; catalytic By similarity
Metal binding2281Zinc 2; catalytic By similarity
Metal binding2981Calcium 4; via carbonyl oxygen By similarity
Metal binding3901Calcium 4; via carbonyl oxygen By similarity
Metal binding4391Calcium 4; via carbonyl oxygen By similarity

Amino acid modifications

Glycosylation4521N-linked (GlcNAc...) Potential
Disulfide bond291 ↔ 478 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6Y4Q5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5D1B9DA9D57BC041

FASTA47853,633
        10         20         30         40         50         60 
MQNLPALLLF CGVVCSAYPV DRAAEDENNN MELTQQYLEN YYNLGKDVKP FVRRRNSGPV 

        70         80         90        100        110        120 
VEKIREMQKF LGLEVTGKVD SDTLAMMRRP RCGVPDVGDF TTFPGMPKWR KTHLTYRIMN 

       130        140        150        160        170        180 
YTPDLPRDAV DSAIEKALNV WKEVTPLTFS RTDEGEADIK ISFAVRDHGD FNPFDGPGNV 

       190        200        210        220        230        240 
LGHAYPPGPG IYGDAHFDDD EQWTSDTSGT NLFLVAAHEL GHSLGLFHSA DPSALMYPVY 

       250        260        270        280        290        300 
NVLADLARFH LSQDDVNGIQ SLYGGPPSDS SNDPVVPTES VPPGPGTPAA CDPTLSFDAI 

       310        320        330        340        350        360 
STLRGEFLFF KDRHFWRKSL RTLEPGFYLI SSFWPSLPSG LDAAYEETSK DIVFIFKGNQ 

       370        380        390        400        410        420 
FWAMRGTEVQ AGYPKGIHTL GFPPTVKKID AAVFDKEKKK TYFFVGDKYW RFDEKRQSME 

       430        440        450        460        470 
PGFPKQIAED FPGVDSKVDA AFEAFGFYYF FNGSSQLEFD PNAKKVTHVL KSNSWLNC

« Hide

References

[1]"Isolation, characterization and expression of stromelysin-1 (MMP3) in canine tumors."
Sorensen K.C., Balkin R.G., Ktichell B.E., Siegel A.M., Schaeffer D.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY183143 mRNA. Translation: AAO63580.1.
RefSeqNP_001002967.1. NM_001002967.1.
UniGeneCfa.3447.

3D structure databases

ProteinModelPortalQ6Y4Q5.
SMRQ6Y4Q5. Positions 33-267.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6Y4Q5.

Protein family/group databases

MEROPSM10.005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403445.
KEGGcfa:403445.

Organism-specific databases

CTD4314.

Phylogenomic databases

eggNOGmaNOG09579.
GeneTreeENSGT00580000081219.
HOVERGENHBG052484.
InParanoidQ6Y4Q5.
OrthoDBEOG4KKZ2X.
PhylomeDBQ6Y4Q5.

Family and domain databases

InterProIPR000585. Hemopexin/matrixin.
IPR018486. Hemopexin/matrixin_CS.
IPR018487. Hemopexin/matrixin_repeat.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR016293. Pept_M10A_matrix_strom.
IPR021190. Pept_M10A_matrixin.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
Gene3DG3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
G3DSA:2.110.10.10. Hemopexin. 1 hit.
KOK01394.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF50923. Hemopexin. 1 hit.
SSF47090. PGBD_like. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMMP3_CANFA
AccessionPrimary (citable) accession number: Q6Y4Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: July 5, 2004
Last modified: November 16, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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