MMP3_RABIT
ID MMP3_RABIT Reviewed; 478 AA.
AC P28863;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 155.
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 AltName: Full=Transin-1;
DE Flags: Precursor;
GN Name=MMP3;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2825726; DOI=10.1002/art.1780301108;
RA Fini M.E., Karmilowicz M.J., Ruby P.L., Beeman A.M., Borges K.A.,
RA Brinckerhoff C.E.;
RT "Cloning of a complementary DNA for rabbit proactivator. A
RT metalloproteinase that activates synovial cell collagenase, shares homology
RT with stromelysin and transin, and is coordinately regulated with
RT collagenase.";
RL Arthritis Rheum. 30:1254-1264(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-167.
RX PubMed=3030290; DOI=10.1042/bj2400913;
RA Whitham S.E., Murphy G., Angel P., Rahmsdorf H.J., Smith B., Lyons A.,
RA Harris T.J.R., Reynolds J.J., Herrlich P., Docherty A.J.P.;
RT "Comparison of human stromelysin and collagenase by cloning and sequence
RT analysis.";
RL Biochem. J. 240:913-916(1986).
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.
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:0000305}.
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; M25664; AAA31467.1; -; mRNA.
DR PIR; A37306; KCRBS1.
DR RefSeq; NP_001075749.1; NM_001082280.1.
DR AlphaFoldDB; P28863; -.
DR SMR; P28863; -.
DR STRING; 9986.ENSOCUP00000013084; -.
DR MEROPS; M10.005; -.
DR PRIDE; P28863; -.
DR Ensembl; ENSOCUT00000015227; ENSOCUP00000013084; ENSOCUG00000029337.
DR GeneID; 100009111; -.
DR KEGG; ocu:100009111; -.
DR CTD; 4314; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000159759; -.
DR InParanoid; P28863; -.
DR OrthoDB; 1075463at2759; -.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000029337; Expressed in uterus.
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; IEA:UniProtKB-EC.
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; ISS:UniProtKB.
DR GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
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 Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000305"
FT PROPEP 18..100
FT /note="Activation peptide"
FT /id="PRO_0000028732"
FT CHAIN 101..478
FT /note="Stromelysin-1"
FT /id="PRO_0000028733"
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 MOTIF 91..98
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 93
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 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 229
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 DISULFID 291..478
FT /evidence="ECO:0000250"
FT CONFLICT 83
FT /note="N -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="R -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 53942 MW; CA742E31A4549D40 CRC64;
MKTLPTLLLL CVALCSAYPL DGASRDADTT NMDLLQQYLE NYYNLEKDVK QFVKRKDSSP
VVKKIQEMQK FLGLEVTGKL DSNTLEVIRK PRCGVPDVGH FSTFPGTPKW TKTHLTYRIV
NYTPDLPRDA VDAAIEKALK VWEEVTPLTF SRKYEGEADI MISFGVREHG DFIPFDGPGN
VLAHAYAPGP GINGDAHFDD DEQWTKDTTG TNLFLVAAHE LGHSLGLFHS ANPEALMYPV
YNAFTDLARF RLSQDDVDGI QSLYGPAPAS PDNSGVPMEP VPPGSGTPVM CDPDLSFDAI
STLRGEILFF KDRYFWRKSL RILEPEFHLI SSFWPSLPSA VDAAYEVISR DTVFIFKGTQ
FWAIRGNEVQ AGYPRSIHTL GFPSTIRKID AAISDKERKK TYFFVEDKYW RFDEKRQSLE
PGFPRHIAED FPGINPKIDA VFEAFGFFYF FSGSSQSEFD PNAKKVTHVL KSNSWFQC
