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O18733 (MMP9_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-9

Short name=MMP-9
EC=3.4.24.35
Alternative name(s):
92 kDa gelatinase
92 kDa type IV collagenase
Gelatinase B
Short name=GELB
Gene names
Name:MMP9
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length704 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments By similarity.

Catalytic activity

Cleavage of gelatin types I and V and collagen types IV and V.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Binds 3 calcium ions per subunit By similarity.

Subunit structure

Exists as monomer or homodimer; disulfide-linked By similarity. Exists also as heterodimer with a 25 kDa protein By similarity. Interacts with ECM1 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix Probable.

Post-translational modification

N- and O-glycosylated By similarity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 3 fibronectin type-II domains.

Contains 4 hemopexin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Propeptide20 – 10687Activation peptide By similarity
PRO_0000028752
Chain107 – 704598Matrix metalloproteinase-9
PRO_0000028753

Regions

Domain225 – 27349Fibronectin type-II 1
Domain283 – 33149Fibronectin type-II 2
Domain342 – 39049Fibronectin type-II 3
Repeat515 – 56046Hemopexin 1
Repeat561 – 60545Hemopexin 2
Repeat607 – 65448Hemopexin 3
Repeat655 – 70147Hemopexin 4
Compositional bias445 – 50864Pro-rich

Sites

Active site4021 By similarity
Metal binding1311Calcium 1 By similarity
Metal binding1651Calcium 2; via carbonyl oxygen By similarity
Metal binding1751Zinc 1; structural By similarity
Metal binding1771Zinc 1; structural By similarity
Metal binding1821Calcium 3 By similarity
Metal binding1831Calcium 3; via carbonyl oxygen By similarity
Metal binding1851Calcium 3; via carbonyl oxygen By similarity
Metal binding1871Calcium 3; via carbonyl oxygen By similarity
Metal binding1901Zinc 1; structural By similarity
Metal binding1971Calcium 2; via carbonyl oxygen By similarity
Metal binding1991Calcium 2; via carbonyl oxygen By similarity
Metal binding2011Calcium 2 By similarity
Metal binding2031Zinc 1; structural By similarity
Metal binding2051Calcium 3 By similarity
Metal binding2061Calcium 1 By similarity
Metal binding2081Calcium 1 By similarity
Metal binding2081Calcium 3 By similarity
Metal binding4011Zinc 2; catalytic By similarity
Metal binding4051Zinc 2; catalytic By similarity
Metal binding4111Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Disulfide bond230 ↔ 256 By similarity
Disulfide bond244 ↔ 271 By similarity
Disulfide bond288 ↔ 314 By similarity
Disulfide bond302 ↔ 329 By similarity
Disulfide bond347 ↔ 373 By similarity
Disulfide bond361 ↔ 388 By similarity
Disulfide bond513 ↔ 701 By similarity

Experimental info

Sequence conflict1311D → E in AAB81681. Ref.1
Sequence conflict276 – 2783LYA → FYT in AAB81681. Ref.1
Sequence conflict553 – 5553SPS → ITD in AAB81681. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O18733 [UniParc].

Last modified July 11, 2001. Version 2.
Checksum: 0DB394D2D6256B91

FASTA70478,123
        10         20         30         40         50         60 
MSPRQPLVLV FLVLGCCSAA PRPHKPTVVV FPGDLRTNLT DKQLAEEYLF RYGYTQVAEL 

        70         80         90        100        110        120 
SNDKQSLSRG LRLLQRRLAL PETGELDKTT LEAMRAPRCG VPDLGKFQTF EGDLKWHHND 

       130        140        150        160        170        180 
ITYWIQNYSE DLPRDVIDDA FARAFAVWSA VTPLTFTRVY GPEADIIIQF GVREHGDGYP 

       190        200        210        220        230        240 
FDGKNGLLAH AFPPGPGIQG DAHFDDEELW TLGKGVVVPT HFGNADGAPC HFPFTFEGRS 

       250        260        270        280        290        300 
YSACTTDGRS DDTPWCSTTA DYDTDRRFGF CPSEKLYAQD GNGDGKPCVF PFTFEGRSYS 

       310        320        330        340        350        360 
TCTTDGRSDG YRWCSTTADY DQDKLYGFCP TRVDSAVTGG NSAGEPCVFP FIFLGKQYST 

       370        380        390        400        410        420 
CTREGRGDGH LWCATTSNFD RDKKWGFCPD QGYSLFLVAA HEFGHALGLD HSSVPEALMY 

       430        440        450        460        470        480 
PMYSFTEGPP LHEDDVRGIQ HLYGPRPEPE PQPPTAPPTA PPTVCATGPP TTRPSERPTA 

       490        500        510        520        530        540 
GPTGPPAAGP TGPPTAGPSE APTVPVDPAE DICKVNIFDA IAEIRNYLHF FKEGKYWRFS 

       550        560        570        580        590        600 
KGKGRRVQGP FLSPSTWPAL PRKLDSAFED GLTKKTFFFS GRQVWVYTGT SVVGPRRLDK 

       610        620        630        640        650        660 
LGLGPEVTQV TGALPQGGGK VLLFSRQRFW SFDVKTQTVD PRSAGSVEQM YPGVPLNTHD 

       670        680        690        700 
IFQYQEKAYF CQDRFYWRVN SRNEVNQVDE VGYVTFDILQ CPED 

« Hide

References

[1]"Dog mast cell alpha-chymase activates progelatinase B by cleaving the Phe88-Gln89 and Phe91-Glu92 bonds of the catalytic domain."
Fang K.C., Raymond W.W., Blount J.L., Caughey G.H.
J. Biol. Chem. 272:25628-25635(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"High expression of 92 kDa type IV collagenase (matrix metalloproteinase-9) in canine mammary adenocarcinoma."
Yokota H., Kumata T., Taketaba S., Kobayashi T., Moue H., Taniyama H., Hirayama K., Kagawa Y., Itoh N., Fujita O., Nakade T., Yuasa A.
Biochim. Biophys. Acta 1568:7-12(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Mongrel.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB006421 mRNA. Translation: BAA22087.3.
U89842 mRNA. Translation: AAB81681.1.
UniGeneCfa.3470.

3D structure databases

ProteinModelPortalO18733.
SMRO18733. Positions 29-444, 510-704.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM10.004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG328372.
HOGENOMHOG000217926.
HOVERGENHBG052484.

Family and domain databases

Gene3D2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProIPR000562. FN_type2_col-bd.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR013806. Kringle-like.
IPR024079. MetalloPept_cat_dom.
IPR028688. MMP9.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
IPR006970. PT.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF30. PTHR10201:SF30. 1 hit.
PfamPF00040. fn2. 3 hits.
PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
PF04886. PT. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMMP9_CANFA
AccessionPrimary (citable) accession number: O18733
Secondary accession number(s): O19130
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 11, 2001
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries