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Protein

Matrix metalloproteinase-9

Gene

MMP9

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: -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 Zn2+ ions per subunit.By similarity
  • Ca2+By similarityNote: Binds 3 Ca2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi131Calcium 1By similarity1
Metal bindingi165Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi175Zinc 1; structuralBy similarity1
Metal bindingi177Zinc 1; structuralBy similarity1
Metal bindingi182Calcium 3By similarity1
Metal bindingi183Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi185Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi187Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi190Zinc 1; structuralBy similarity1
Metal bindingi197Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi199Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi201Calcium 2By similarity1
Metal bindingi203Zinc 1; structuralBy similarity1
Metal bindingi205Calcium 3By similarity1
Metal bindingi206Calcium 1By similarity1
Metal bindingi208Calcium 1By similarity1
Metal bindingi208Calcium 3By similarity1
Metal bindingi401Zinc 2; catalyticBy similarity1
Active sitei402PROSITE-ProRule annotation1
Metal bindingi405Zinc 2; catalyticBy similarity1
Metal bindingi411Zinc 2; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation
LigandCalcium, 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 lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
PropeptideiPRO_000002875220 – 106Activation peptideBy similarityAdd BLAST87
ChainiPRO_0000028753107 – 704Matrix metalloproteinase-9Add BLAST598

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi127N-linked (GlcNAc...) asparagineSequence analysis1
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

Proteomic databases

PaxDbiO18733
PRIDEiO18733

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000035167

Structurei

3D structure databases

ProteinModelPortaliO18733
SMRiO18733
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini225 – 273Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini283 – 331Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini342 – 390Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST49
Repeati515 – 560Hemopexin 1Add BLAST46
Repeati561 – 605Hemopexin 2Add BLAST45
Repeati607 – 654Hemopexin 3Add BLAST48
Repeati655 – 701Hemopexin 4Add BLAST47

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi445 – 508Pro-richAdd BLAST64

Sequence similaritiesi

Belongs to the peptidase M10A family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
HOGENOMiHOG000217926
HOVERGENiHBG052484
InParanoidiO18733

Family and domain databases

CDDicd00062 FN2, 3 hits
cd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.10.10.10, 3 hits
2.110.10.10, 1 hit
3.40.390.10, 2 hits
InterProiView protein in InterPro
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR013806 Kringle-like
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028688 MMP9
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf
IPR006970 PT
PANTHERiPTHR10201:SF30 PTHR10201:SF30, 1 hit
PfamiView protein in Pfam
PF00040 fn2, 3 hits
PF00045 Hemopexin, 3 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PF04886 PT, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00059 FN2, 3 hits
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
SSF57440 SSF57440, 3 hits
PROSITEiView protein in PROSITE
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

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)DescriptionActionsGraphical viewLength
Sequence conflicti131D → E in AAB81681 (PubMed:9325284).Curated1
Sequence conflicti276 – 278LYA → FYT in AAB81681 (PubMed:9325284).Curated3
Sequence conflicti553 – 555SPS → ITD in AAB81681 (PubMed:9325284).Curated3

Sequence databases

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

Similar proteinsi

Entry informationi

Entry nameiMMP9_CANLF
AccessioniPrimary (citable) accession number: O18733
Secondary accession number(s): O19130
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 11, 2001
Last modified: May 23, 2018
This is version 135 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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