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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).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn(2+) ions per subunit.By similarity
  • Ca2+By similarityNote: Binds 3 Ca(2+) ions per subunit.By similarity

Sites

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Propeptidei20 – 10687Activation peptideBy similarityPRO_0000028752Add
BLAST
Chaini107 – 704598Matrix metalloproteinase-9PRO_0000028753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi230 ↔ 256PROSITE-ProRule annotation
Disulfide bondi244 ↔ 271PROSITE-ProRule annotation
Disulfide bondi288 ↔ 314PROSITE-ProRule annotation
Disulfide bondi302 ↔ 329PROSITE-ProRule annotation
Disulfide bondi347 ↔ 373PROSITE-ProRule annotation
Disulfide bondi361 ↔ 388PROSITE-ProRule annotation
Disulfide bondi513 ↔ 701PROSITE-ProRule annotation

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. Exists also as heterodimer with a 25 kDa protein. Interacts with ECM1.By similarity

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated
Contains 3 fibronectin type-II domains.PROSITE-ProRule annotation
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG328372.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiO18733.

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

        10         20         30         40         50
MSPRQPLVLV FLVLGCCSAA PRPHKPTVVV FPGDLRTNLT DKQLAEEYLF
60 70 80 90 100
RYGYTQVAEL SNDKQSLSRG LRLLQRRLAL PETGELDKTT LEAMRAPRCG
110 120 130 140 150
VPDLGKFQTF EGDLKWHHND ITYWIQNYSE DLPRDVIDDA FARAFAVWSA
160 170 180 190 200
VTPLTFTRVY GPEADIIIQF GVREHGDGYP FDGKNGLLAH AFPPGPGIQG
210 220 230 240 250
DAHFDDEELW TLGKGVVVPT HFGNADGAPC HFPFTFEGRS YSACTTDGRS
260 270 280 290 300
DDTPWCSTTA DYDTDRRFGF CPSEKLYAQD GNGDGKPCVF PFTFEGRSYS
310 320 330 340 350
TCTTDGRSDG YRWCSTTADY DQDKLYGFCP TRVDSAVTGG NSAGEPCVFP
360 370 380 390 400
FIFLGKQYST CTREGRGDGH LWCATTSNFD RDKKWGFCPD QGYSLFLVAA
410 420 430 440 450
HEFGHALGLD HSSVPEALMY PMYSFTEGPP LHEDDVRGIQ HLYGPRPEPE
460 470 480 490 500
PQPPTAPPTA PPTVCATGPP TTRPSERPTA GPTGPPAAGP TGPPTAGPSE
510 520 530 540 550
APTVPVDPAE DICKVNIFDA IAEIRNYLHF FKEGKYWRFS KGKGRRVQGP
560 570 580 590 600
FLSPSTWPAL PRKLDSAFED GLTKKTFFFS GRQVWVYTGT SVVGPRRLDK
610 620 630 640 650
LGLGPEVTQV TGALPQGGGK VLLFSRQRFW SFDVKTQTVD PRSAGSVEQM
660 670 680 690 700
YPGVPLNTHD IFQYQEKAYF CQDRFYWRVN SRNEVNQVDE VGYVTFDILQ

CPED
Length:704
Mass (Da):78,123
Last modified:July 11, 2001 - v2
Checksum:i0DB394D2D6256B91
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311D → E in AAB81681. (PubMed:9325284)Curated
Sequence conflicti276 – 2783LYA → FYT in AAB81681. (PubMed:9325284)Curated
Sequence conflicti553 – 5553SPS → ITD in AAB81681. (PubMed:9325284)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006421 mRNA. Translation: BAA22087.3.
U89842 mRNA. Translation: AAB81681.1.
UniGeneiCfa.3470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
InParanoidi O18733.

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: November 26, 2014
This is version 118 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