MMP3_CANLF
ID MMP3_CANLF Reviewed; 478 AA.
AC Q6Y4Q5;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Stromelysin-1;
DE Short=SL-1;
DE EC=3.4.24.17;
DE AltName: Full=Matrix metalloproteinase-3;
DE Short=MMP-3;
DE Flags: Precursor;
GN Name=MMP3;
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].
RA Sorensen K.C., Balkin R.G., Ktichell B.E., Siegel A.M., Schaeffer D.;
RT "Isolation, characterization and expression of stromelysin-1 (MMP3) in
RT canine tumors.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Can degrade fibronectin, laminin, gelatins of type I, III,
CC IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans.
CC Activates procollagenase (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage where P1', P2' and P3' are hydrophobic
CC residues.; EC=3.4.24.17;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
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.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; AY183143; AAO63580.1; -; mRNA.
DR RefSeq; NP_001002967.1; NM_001002967.1.
DR AlphaFoldDB; Q6Y4Q5; -.
DR SMR; Q6Y4Q5; -.
DR STRING; 9615.ENSCAFP00000022195; -.
DR MEROPS; M10.005; -.
DR PaxDb; Q6Y4Q5; -.
DR PRIDE; Q6Y4Q5; -.
DR Ensembl; ENSCAFT00030025210; ENSCAFP00030022012; ENSCAFG00030013617.
DR Ensembl; ENSCAFT00040038011; ENSCAFP00040033135; ENSCAFG00040020536.
DR Ensembl; ENSCAFT00845001397; ENSCAFP00845001083; ENSCAFG00845000842.
DR GeneID; 403445; -.
DR KEGG; cfa:403445; -.
DR CTD; 4314; -.
DR VEuPathDB; HostDB:ENSCAFG00845000842; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000159759; -.
DR HOGENOM; CLU_015489_6_0_1; -.
DR InParanoid; Q6Y4Q5; -.
DR OMA; NFVQQYL; -.
DR OrthoDB; 1075463at2759; -.
DR TreeFam; TF315428; -.
DR Reactome; R-CFA-1442490; Collagen degradation.
DR Reactome; R-CFA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CFA-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-CFA-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-CFA-9009391; Extra-nuclear estrogen signaling.
DR Proteomes; UP000002254; Chromosome 5.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0010727; P:negative regulation of hydrogen peroxide metabolic process; IEA:Ensembl.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00094; HX; 1.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR000585; Hemopexin-like_dom.
DR InterPro; IPR036375; Hemopexin-like_dom_sf.
DR InterPro; IPR018487; Hemopexin-like_repeat.
DR InterPro; IPR018486; Hemopexin_CS.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
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 Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00024; HEMOPEXIN; 1.
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..17
FT /evidence="ECO:0000255"
FT PROPEP 18..99
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028724"
FT CHAIN 100..478
FT /note="Stromelysin-1"
FT /id="PRO_0000028725"
FT REPEAT 288..337
FT /note="Hemopexin 1"
FT REPEAT 338..384
FT /note="Hemopexin 2"
FT REPEAT 386..434
FT /note="Hemopexin 3"
FT REPEAT 435..478
FT /note="Hemopexin 4"
FT REGION 260..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 90..97
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 260..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 92
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"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 291..478
FT /evidence="ECO:0000250"
SQ SEQUENCE 478 AA; 53633 MW; 5D1B9DA9D57BC041 CRC64;
MQNLPALLLF CGVVCSAYPV DRAAEDENNN MELTQQYLEN YYNLGKDVKP FVRRRNSGPV
VEKIREMQKF LGLEVTGKVD SDTLAMMRRP RCGVPDVGDF TTFPGMPKWR KTHLTYRIMN
YTPDLPRDAV DSAIEKALNV WKEVTPLTFS RTDEGEADIK ISFAVRDHGD FNPFDGPGNV
LGHAYPPGPG IYGDAHFDDD EQWTSDTSGT NLFLVAAHEL GHSLGLFHSA DPSALMYPVY
NVLADLARFH LSQDDVNGIQ SLYGGPPSDS SNDPVVPTES VPPGPGTPAA CDPTLSFDAI
STLRGEFLFF KDRHFWRKSL RTLEPGFYLI SSFWPSLPSG LDAAYEETSK DIVFIFKGNQ
FWAMRGTEVQ AGYPKGIHTL GFPPTVKKID AAVFDKEKKK TYFFVGDKYW RFDEKRQSME
PGFPKQIAED FPGVDSKVDA AFEAFGFYYF FNGSSQLEFD PNAKKVTHVL KSNSWLNC
