MMP9_BOVIN
ID MMP9_BOVIN Reviewed; 712 AA.
AC P52176; A5PKB8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Matrix metalloproteinase-9 {ECO:0000303|PubMed:7770085};
DE Short=MMP-9 {ECO:0000303|PubMed:7770085};
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 {ECO:0000303|PubMed:7770085};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leukocyte;
RX PubMed=7770085; DOI=10.1016/0166-6851(94)00216-a;
RA Baylis H.A., Megson A., Hall R.;
RT "Infection with Theileria annulata induces expression of matrix
RT metalloproteinase 9 and transcription factor AP-1 in bovine leucocytes.";
RL Mol. Biochem. Parasitol. 69:211-222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; X78324; CAA55127.1; -; mRNA.
DR EMBL; BC142430; AAI42431.1; -; mRNA.
DR PIR; I46031; I46031.
DR RefSeq; NP_777169.1; NM_174744.2.
DR AlphaFoldDB; P52176; -.
DR SMR; P52176; -.
DR STRING; 9913.ENSBTAP00000027556; -.
DR BindingDB; P52176; -.
DR ChEMBL; CHEMBL5846; -.
DR MEROPS; M10.004; -.
DR PaxDb; P52176; -.
DR PeptideAtlas; P52176; -.
DR PRIDE; P52176; -.
DR Ensembl; ENSBTAT00000027556; ENSBTAP00000027556; ENSBTAG00000020676.
DR GeneID; 282871; -.
DR KEGG; bta:282871; -.
DR CTD; 4318; -.
DR VEuPathDB; HostDB:ENSBTAG00000020676; -.
DR VGNC; VGNC:31531; MMP9.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000157415; -.
DR InParanoid; P52176; -.
DR OMA; DVFQYRE; -.
DR OrthoDB; 1075463at2759; -.
DR PRO; PR:P52176; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000020676; Expressed in milk and 57 other tissues.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR GO; GO:0071492; P:cellular response to UV-A; IEA:Ensembl.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0050900; P:leukocyte migration; IEA:InterPro.
DR GO; GO:2001258; P:negative regulation of cation channel activity; IEA:Ensembl.
DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:2000697; P:negative regulation of epithelial cell differentiation involved in kidney development; IEA:Ensembl.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:1900122; P:positive regulation of receptor binding; IEA:Ensembl.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:1904645; P:response to amyloid-beta; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
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_0000028750"
FT CHAIN 107..712
FT /note="Matrix metalloproteinase-9"
FT /id="PRO_0000028751"
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 523..568
FT /note="Hemopexin 1"
FT REPEAT 569..613
FT /note="Hemopexin 2"
FT REPEAT 615..662
FT /note="Hemopexin 3"
FT REPEAT 663..709
FT /note="Hemopexin 4"
FT REGION 440..519
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 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..509
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 120
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 521..709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 712 AA; 79088 MW; E7FDA28372AEE0CE CRC64;
MSPLQPLVLA LLVLACCSAV PRRRQPTVVV FPGEPRTNLT NRQLAEEYLY RYGYTPGAEL
SEDGQSLQRA LLRFQRRLSL PETGELDSTT LNAMRAPRCG VPDVGRFQTF EGELKWHHHN
ITYWIQNYSE DLPRAVIDDA FARAFALWSA VTPLTFTRVY GPEADIVIQF GVREHGDGYP
FDGKNGLLAH AFPPGKGIQG DAHFDDEELW SLGKGVVIPT YFGNAKGAAC HFPFTFEGRS
YSACTTDGRS DDMLWCSTTA DYDADRQFGF CPSERLYTQD GNADGKPCVF PFTFQGRTYS
ACTSDGRSDG YRWCATTANY DQDKLYGFCP TRVDATVTGG NAAGELCVFP FTFLGKEYSA
CTREGRNDGH LWCATTSNFD KDKKWGFCPD QGYSLFLVAA HEFGHALGLD HTSVPEALMY
PMYRFTEEHP LHRDDVQGIQ HLYGPRPEPE PRPPTTTTTT TTEPQPTAPP TVCVTGPPTA
RPSEGPTTGP TGPPAAGPTG PPTAGPSAAP TESPDPAEDV CNVDIFDAIA EIRNRLHFFK
AGKYWRLSEG GGRRVQGPFL VKSKWPALPR KLDSAFEDPL TKKIFFFSGR QVWVYTGASL
LGPRRLDKLG LGPEVAQVTG ALPRPEGKVL LFSGQSFWRF DVKTQKVDPQ SVTPVDQMFP
GVPISTHDIF QYQEKAYFCQ DHFYWRVSSQ NEVNQVDYVG YVTFDLLKCP ED
