MMP9_CANLF
ID MMP9_CANLF Reviewed; 704 AA.
AC O18733; O19130;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Matrix metalloproteinase-9;
DE Short=MMP-9;
DE EC=3.4.24.35 {ECO:0000250|UniProtKB:P14780};
DE AltName: Full=92 kDa gelatinase;
DE AltName: Full=92 kDa type IV collagenase;
DE AltName: Full=Gelatinase B;
DE Short=GELB;
DE Flags: Precursor;
GN Name=MMP9;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9325284; DOI=10.1074/jbc.272.41.25628;
RA Fang K.C., Raymond W.W., Blount J.L., Caughey G.H.;
RT "Dog mast cell alpha-chymase activates progelatinase B by cleaving the
RT Phe88-Gln89 and Phe91-Glu92 bonds of the catalytic domain.";
RL J. Biol. Chem. 272:25628-25635(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Mongrel;
RX PubMed=11731079; DOI=10.1016/s0304-4165(01)00192-1;
RA Yokota H., Kumata T., Taketaba S., Kobayashi T., Moue H., Taniyama H.,
RA Hirayama K., Kagawa Y., Itoh N., Fujita O., Nakade T., Yuasa A.;
RT "High expression of 92 kDa type IV collagenase (matrix metalloproteinase-9)
RT in canine mammary adenocarcinoma.";
RL Biochim. Biophys. Acta 1568:7-12(2001).
CC -!- FUNCTION: Matrix metalloproteinase that plays an essential role in
CC local proteolysis of the extracellular matrix and in leukocyte
CC migration (By similarity). Could play a role in bone osteoclastic
CC resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By
CC similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By
CC similarity). Cleaves type IV and type V collagen into large C-terminal
CC three quarter fragments and shorter N-terminal one quarter fragments.
CC Degrades fibronectin but not laminin or Pz-peptide (By similarity).
CC {ECO:0000250|UniProtKB:P14780, ECO:0000250|UniProtKB:P41245}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of gelatin types I and V and collagen types IV and
CC V.; EC=3.4.24.35; Evidence={ECO:0000250|UniProtKB:P14780};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P14780};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P14780};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780};
CC -!- SUBUNIT: Exists as monomer or homodimer; disulfide-linked. Exists also
CC as heterodimer with LCN2. Macrophages and transformed cell lines
CC produce only the monomeric form. Interacts with ECM1.
CC {ECO:0000250|UniProtKB:P14780}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P14780}.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme. {ECO:0000250|UniProtKB:P14780}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P14780}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; AB006421; BAA22087.3; -; mRNA.
DR EMBL; U89842; AAB81681.1; -; mRNA.
DR AlphaFoldDB; O18733; -.
DR SMR; O18733; -.
DR STRING; 9612.ENSCAFP00000035167; -.
DR MEROPS; M10.004; -.
DR PaxDb; O18733; -.
DR PRIDE; O18733; -.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; O18733; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032502; P:developmental process; IEA:UniProt.
DR GO; GO:0050900; P:leukocyte migration; IEA:InterPro.
DR GO; GO:0001503; P:ossification; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd00062; FN2; 3.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.10.10.10; -; 2.
DR Gene3D; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 2.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR028688; MMP9.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR021158; Pept_M10A_Zn_BS.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR006970; PT.
DR PANTHER; PTHR10201:SF30; PTHR10201:SF30; 1.
DR Pfam; PF00040; fn2; 3.
DR Pfam; PF00045; Hemopexin; 3.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF04886; PT; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00059; FN2; 3.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR SUPFAM; SSF57440; SSF57440; 3.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00023; FN2_1; 3.
DR PROSITE; PS51092; FN2_2; 3.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen degradation; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT PROPEP 20..106
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT /id="PRO_0000028752"
FT CHAIN 107..704
FT /note="Matrix metalloproteinase-9"
FT /id="PRO_0000028753"
FT DOMAIN 225..273
FT /note="Fibronectin type-II 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 283..331
FT /note="Fibronectin type-II 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 342..390
FT /note="Fibronectin type-II 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT REPEAT 515..560
FT /note="Hemopexin 1"
FT REPEAT 561..605
FT /note="Hemopexin 2"
FT REPEAT 607..654
FT /note="Hemopexin 3"
FT REPEAT 655..701
FT /note="Hemopexin 4"
FT REGION 434..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..104
FT /note="Cysteine switch"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT COMPBIAS 446..468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P14780"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 230..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 244..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 288..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 302..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 347..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 361..388
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DISULFID 513..701
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT CONFLICT 131
FT /note="D -> E (in Ref. 1; AAB81681)"
FT /evidence="ECO:0000305"
FT CONFLICT 276..278
FT /note="LYA -> FYT (in Ref. 1; AAB81681)"
FT /evidence="ECO:0000305"
FT CONFLICT 553..555
FT /note="SPS -> ITD (in Ref. 1; AAB81681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 78123 MW; 0DB394D2D6256B91 CRC64;
MSPRQPLVLV FLVLGCCSAA PRPHKPTVVV FPGDLRTNLT DKQLAEEYLF RYGYTQVAEL
SNDKQSLSRG LRLLQRRLAL PETGELDKTT LEAMRAPRCG VPDLGKFQTF EGDLKWHHND
ITYWIQNYSE DLPRDVIDDA FARAFAVWSA VTPLTFTRVY GPEADIIIQF GVREHGDGYP
FDGKNGLLAH AFPPGPGIQG DAHFDDEELW TLGKGVVVPT HFGNADGAPC HFPFTFEGRS
YSACTTDGRS DDTPWCSTTA DYDTDRRFGF CPSEKLYAQD GNGDGKPCVF PFTFEGRSYS
TCTTDGRSDG YRWCSTTADY DQDKLYGFCP TRVDSAVTGG NSAGEPCVFP FIFLGKQYST
CTREGRGDGH LWCATTSNFD RDKKWGFCPD QGYSLFLVAA HEFGHALGLD HSSVPEALMY
PMYSFTEGPP LHEDDVRGIQ HLYGPRPEPE PQPPTAPPTA PPTVCATGPP TTRPSERPTA
GPTGPPAAGP TGPPTAGPSE APTVPVDPAE DICKVNIFDA IAEIRNYLHF FKEGKYWRFS
KGKGRRVQGP FLSPSTWPAL PRKLDSAFED GLTKKTFFFS GRQVWVYTGT SVVGPRRLDK
LGLGPEVTQV TGALPQGGGK VLLFSRQRFW SFDVKTQTVD PRSAGSVEQM YPGVPLNTHD
IFQYQEKAYF CQDRFYWRVN SRNEVNQVDE VGYVTFDILQ CPED
