Matrix metalloproteinase-9 precursor - Canis familiaris (Dog)

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O18733 (MMP9_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length	704 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	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	Secreted › extracellular space › extracellular 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-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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	extracellular space Inferred from sequence or structural similarity. Source: UniProtKB proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metalloendopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB 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 – 19

By similarity

Propeptide

20 – 106

Activation peptide By similarity

PRO_0000028752

Chain

107 – 704

598

Matrix metalloproteinase-9

PRO_0000028753

Regions

Domain

225 – 273

Fibronectin type-II 1

Domain

283 – 331

Fibronectin type-II 2

Domain

342 – 390

Fibronectin type-II 3

Domain

518 – 562

Hemopexin-like 1

Domain

564 – 605

Hemopexin-like 2

Domain

610 – 656

Hemopexin-like 3

Domain

658 – 701

Hemopexin-like 4

Compositional bias

445 – 508

Pro-rich

Sites

Active site

402

By similarity

Metal binding

131

Calcium 1 By similarity

Metal binding

165

Calcium 2; via carbonyl oxygen By similarity

Metal binding

175

Zinc 1; structural By similarity

Metal binding

177

Zinc 1; structural By similarity

Metal binding

182

Calcium 3 By similarity

Metal binding

183

Calcium 3; via carbonyl oxygen By similarity

Metal binding

185

Calcium 3; via carbonyl oxygen By similarity

Metal binding

187

Calcium 3; via carbonyl oxygen By similarity

Metal binding

190

Zinc 1; structural By similarity

Metal binding

197

Calcium 2; via carbonyl oxygen By similarity

Metal binding

199

Calcium 2; via carbonyl oxygen By similarity

Metal binding

201

Calcium 2 By similarity

Metal binding

203

Zinc 1; structural By similarity

Metal binding

205

Calcium 3 By similarity

Metal binding

206

Calcium 1 By similarity

Metal binding

208

Calcium 1 By similarity

Metal binding

208

Calcium 3 By similarity

Metal binding

401

Zinc 2; catalytic By similarity

Metal binding

405

Zinc 2; catalytic By similarity

Metal binding

411

Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

127

N-linked (GlcNAc...) Potential

Disulfide bond

230 ↔ 256

By similarity

Disulfide bond

244 ↔ 271

By similarity

Disulfide bond

288 ↔ 314

By similarity

Disulfide bond

302 ↔ 329

By similarity

Disulfide bond

347 ↔ 373

By similarity

Disulfide bond

361 ↔ 388

By similarity

Disulfide bond

513 ↔ 701

By similarity

Experimental info

Sequence conflict

131

D → E in AAB81681. Ref.1

Sequence conflict

276 – 278

LYA → FYT in AAB81681. Ref.1

Sequence conflict

553 – 555

SPS → ITD in AAB81681. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O18733 [UniParc].

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

704

78,123

        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

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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.
UniGene	Cfa.3470.
3D structure databases
ProteinModelPortal	O18733.
SMR	O18733. Positions 29-444, 510-704.
ModBase	Search...
Protein family/group databases
MEROPS	M10.004.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG328372.
HOGENOM	HOG000217926.
HOVERGEN	HBG052484.
OrthoDB	EOG4H9XJZ.
Family and domain databases
Gene3D	2.10.10.10. 3 hits. 2.110.10.10. 1 hit. 3.40.390.10. 2 hits.
InterPro	IPR000562. FN_type2_col-bd. IPR000585. Hemopexin-like_dom. IPR018487. Hemopexin-like_repeat. IPR013806. Kringle-like. IPR024079. MetalloPept_cat_dom. IPR001818. Pept_M10_metallopeptidase. IPR021190. Pept_M10A. IPR021158. Pept_M10A_Zn_BS. IPR006026. Peptidase_Metallo. IPR002477. Peptidoglycan-bd-like. IPR006970. PT. [Graphical view]
Pfam	PF00040. fn2. 3 hits. PF00045. Hemopexin. 3 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. PF04886. PT. 1 hit. [Graphical view]
PRINTS	PR00138. MATRIXIN.
SMART	SM00059. FN2. 3 hits. SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
SUPFAM	SSF50923. Hemopexin. 1 hit. SSF57440. Kringle-like. 3 hits. SSF47090. PGBD_like. 1 hit.
PROSITE	PS00546. CYSTEINE_SWITCH. 1 hit. PS00023. FN2_1. 3 hits. PS51092. FN2_2. 3 hits. PS00024. HEMOPEXIN. False negative. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MMP9_CANFA

Accession

Primary (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:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents