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O18733

- MMP9_CANFA

UniProt

O18733 - MMP9_CANFA

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Protein
Matrix metalloproteinase-9
Gene
MMP9
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

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

Cofactori

Binds 2 zinc ions per subunit By similarity.
Binds 3 calcium ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi131 – 1311Calcium 1 By similarity
Metal bindingi165 – 1651Calcium 2; via carbonyl oxygen By similarity
Metal bindingi175 – 1751Zinc 1; structural By similarity
Metal bindingi177 – 1771Zinc 1; structural By similarity
Metal bindingi182 – 1821Calcium 3 By similarity
Metal bindingi183 – 1831Calcium 3; via carbonyl oxygen By similarity
Metal bindingi185 – 1851Calcium 3; via carbonyl oxygen By similarity
Metal bindingi187 – 1871Calcium 3; via carbonyl oxygen By similarity
Metal bindingi190 – 1901Zinc 1; structural By similarity
Metal bindingi197 – 1971Calcium 2; via carbonyl oxygen By similarity
Metal bindingi199 – 1991Calcium 2; via carbonyl oxygen By similarity
Metal bindingi201 – 2011Calcium 2 By similarity
Metal bindingi203 – 2031Zinc 1; structural By similarity
Metal bindingi205 – 2051Calcium 3 By similarity
Metal bindingi206 – 2061Calcium 1 By similarity
Metal bindingi208 – 2081Calcium 1 By similarity
Metal bindingi208 – 2081Calcium 3 By similarity
Metal bindingi401 – 4011Zinc 2; catalytic By similarity
Active sitei402 – 4021 By similarity
Metal bindingi405 – 4051Zinc 2; catalytic By similarity
Metal bindingi411 – 4111Zinc 2; catalytic By similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB-KW
  2. leukocyte migration Source: InterPro
  3. ossification Source: InterPro
  4. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-9 (EC:3.4.24.35)
Short name:
MMP-9
Alternative name(s):
92 kDa gelatinase
92 kDa type IV collagenase
Gelatinase B
Short name:
GELB
Gene namesi
Name:MMP9
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 By similarity
Add
BLAST
Propeptidei20 – 10687Activation peptide By similarity
PRO_0000028752Add
BLAST
Chaini107 – 704598Matrix metalloproteinase-9
PRO_0000028753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi127 – 1271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi230 ↔ 256 By similarity
Disulfide bondi244 ↔ 271 By similarity
Disulfide bondi288 ↔ 314 By similarity
Disulfide bondi302 ↔ 329 By similarity
Disulfide bondi347 ↔ 373 By similarity
Disulfide bondi361 ↔ 388 By similarity
Disulfide bondi513 ↔ 701 By similarity

Post-translational modificationi

N- and O-glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliO18733.
SMRiO18733. Positions 29-444, 510-704.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini225 – 27349Fibronectin type-II 1
Add
BLAST
Domaini283 – 33149Fibronectin type-II 2
Add
BLAST
Domaini342 – 39049Fibronectin type-II 3
Add
BLAST
Repeati515 – 56046Hemopexin 1
Add
BLAST
Repeati561 – 60545Hemopexin 2
Add
BLAST
Repeati607 – 65448Hemopexin 3
Add
BLAST
Repeati655 – 70147Hemopexin 4
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi445 – 50864Pro-rich
Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG328372.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.

Family and domain databases

Gene3Di2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProiIPR000562. 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]
PANTHERiPTHR10201:SF30. PTHR10201:SF30. 1 hit.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 3 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
PF04886. PT. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEiPS00546. 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]

Sequencei

Sequence statusi: Complete.

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

O18733-1 [UniParc]FASTAAdd to Basket

« Hide

MSPRQPLVLV FLVLGCCSAA PRPHKPTVVV FPGDLRTNLT DKQLAEEYLF    50
RYGYTQVAEL SNDKQSLSRG LRLLQRRLAL PETGELDKTT LEAMRAPRCG 100
VPDLGKFQTF EGDLKWHHND ITYWIQNYSE DLPRDVIDDA FARAFAVWSA 150
VTPLTFTRVY GPEADIIIQF GVREHGDGYP FDGKNGLLAH AFPPGPGIQG 200
DAHFDDEELW TLGKGVVVPT HFGNADGAPC HFPFTFEGRS YSACTTDGRS 250
DDTPWCSTTA DYDTDRRFGF CPSEKLYAQD GNGDGKPCVF PFTFEGRSYS 300
TCTTDGRSDG YRWCSTTADY DQDKLYGFCP TRVDSAVTGG NSAGEPCVFP 350
FIFLGKQYST CTREGRGDGH LWCATTSNFD RDKKWGFCPD QGYSLFLVAA 400
HEFGHALGLD HSSVPEALMY PMYSFTEGPP LHEDDVRGIQ HLYGPRPEPE 450
PQPPTAPPTA PPTVCATGPP TTRPSERPTA GPTGPPAAGP TGPPTAGPSE 500
APTVPVDPAE DICKVNIFDA IAEIRNYLHF FKEGKYWRFS KGKGRRVQGP 550
FLSPSTWPAL PRKLDSAFED GLTKKTFFFS GRQVWVYTGT SVVGPRRLDK 600
LGLGPEVTQV TGALPQGGGK VLLFSRQRFW SFDVKTQTVD PRSAGSVEQM 650
YPGVPLNTHD IFQYQEKAYF CQDRFYWRVN SRNEVNQVDE VGYVTFDILQ 700
CPED 704
Length:704
Mass (Da):78,123
Last modified:July 11, 2001 - v2
Checksum:i0DB394D2D6256B91
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311D → E in AAB81681. 1 Publication
Sequence conflicti276 – 2783LYA → FYT in AAB81681. 1 Publication
Sequence conflicti553 – 5553SPS → ITD in AAB81681. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB006421 mRNA. Translation: BAA22087.3.
U89842 mRNA. Translation: AAB81681.1.
UniGeneiCfa.3470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB006421 mRNA. Translation: BAA22087.3 .
U89842 mRNA. Translation: AAB81681.1 .
UniGenei Cfa.3470.

3D structure databases

ProteinModelPortali O18733.
SMRi O18733. Positions 29-444, 510-704.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M10.004.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG328372.
HOGENOMi HOG000217926.
HOVERGENi HBG052484.

Family and domain databases

Gene3Di 2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProi IPR000562. 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 ]
PANTHERi PTHR10201:SF30. PTHR10201:SF30. 1 hit.
Pfami 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 ]
PRINTSi PR00138. MATRIXIN.
SMARTi SM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEi PS00546. 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 ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiMMP9_CANFA
AccessioniPrimary (citable) accession number: O18733
Secondary accession number(s): O19130
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 11, 2001
Last modified: June 11, 2014
This is version 115 of the entry and version 2 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

External Data

Dasty 3

Similar proteinsi