MMP11_MOUSE
ID MMP11_MOUSE Reviewed; 492 AA.
AC Q02853;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Stromelysin-3;
DE Short=SL-3;
DE Short=ST3;
DE EC=3.4.24.-;
DE AltName: Full=Matrix metalloproteinase-11;
DE Short=MMP-11;
DE Flags: Precursor;
GN Name=Mmp11;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1429845; DOI=10.1083/jcb.119.4.997;
RA Lefebvre O., Wolf C., Limacher J.-M., Hutin P., Wendling C., Lemeur M.,
RA Basset P., Rio M.C.;
RT "The breast cancer-associated stromelysin-3 gene is expressed during mouse
RT mammary gland apoptosis.";
RL J. Cell Biol. 119:997-1002(1992).
RN [2]
RP SEQUENCE REVISION.
RA Lefebvre O.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 102-265.
RX PubMed=11254383; DOI=10.1006/jmbi.2001.4493;
RA Gall A.-L., Ruff M., Kannan R., Cuniasse P., Yiotakis A., Dive V.,
RA Rio M.-C., Basset P., Moras D.;
RT "Crystal structure of the stromelysin-3 (MMP-11) catalytic domain complexed
RT with a phosphinic inhibitor mimicking the transition-state.";
RL J. Mol. Biol. 307:577-586(2001).
CC -!- FUNCTION: May play an important role in the progression of epithelial
CC malignancies.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the mammary gland during
CC apoptosis.
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 -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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DR EMBL; Z12604; CAA78248.1; -; mRNA.
DR CCDS; CCDS23937.1; -.
DR PIR; A44399; A44399.
DR RefSeq; NP_001293113.1; NM_001306184.1.
DR RefSeq; NP_032632.1; NM_008606.3.
DR PDB; 1HV5; X-ray; 2.60 A; A/B/C/D/E/F=102-265.
DR PDBsum; 1HV5; -.
DR AlphaFoldDB; Q02853; -.
DR SMR; Q02853; -.
DR BioGRID; 201444; 2.
DR STRING; 10090.ENSMUSP00000000924; -.
DR BindingDB; Q02853; -.
DR ChEMBL; CHEMBL3412; -.
DR MEROPS; M10.007; -.
DR PhosphoSitePlus; Q02853; -.
DR PaxDb; Q02853; -.
DR PRIDE; Q02853; -.
DR ProteomicsDB; 295684; -.
DR Antibodypedia; 3609; 553 antibodies from 36 providers.
DR DNASU; 17385; -.
DR Ensembl; ENSMUST00000000924; ENSMUSP00000000924; ENSMUSG00000000901.
DR Ensembl; ENSMUST00000120281; ENSMUSP00000112940; ENSMUSG00000000901.
DR GeneID; 17385; -.
DR KEGG; mmu:17385; -.
DR UCSC; uc007fto.1; mouse.
DR CTD; 4320; -.
DR MGI; MGI:97008; Mmp11.
DR VEuPathDB; HostDB:ENSMUSG00000000901; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000156340; -.
DR HOGENOM; CLU_015489_8_3_1; -.
DR InParanoid; Q02853; -.
DR OMA; IYIFSGG; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q02853; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.B3; 3474.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 17385; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Mmp11; mouse.
DR EvolutionaryTrace; Q02853; -.
DR PRO; PR:Q02853; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q02853; protein.
DR Bgee; ENSMUSG00000000901; Expressed in floor plate spinal cord region and 186 other tissues.
DR ExpressionAtlas; Q02853; baseline and differential.
DR Genevisible; Q02853; MM.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0030574; P:collagen catabolic process; IDA:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
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; IPR006026; Peptidase_Metallo.
DR InterPro; IPR028705; Stromelysin-3.
DR PANTHER; PTHR10201:SF20; PTHR10201:SF20; 1.
DR Pfam; PF00045; Hemopexin; 4.
DR Pfam; PF00413; Peptidase_M10; 1.
DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00120; HX; 4.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cleavage on pair of basic residues;
KW Collagen degradation; Disulfide bond; Extracellular matrix; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT PROPEP 36..101
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028772"
FT CHAIN 102..492
FT /note="Stromelysin-3"
FT /id="PRO_0000028773"
FT REPEAT 295..343
FT /note="Hemopexin 1"
FT REPEAT 344..386
FT /note="Hemopexin 2"
FT REPEAT 388..436
FT /note="Hemopexin 3"
FT REPEAT 437..484
FT /note="Hemopexin 4"
FT MOTIF 82..89
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 220
FT BINDING 84
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 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 180
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT DISULFID 298..484
FT /evidence="ECO:0000250"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1HV5"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:1HV5"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:1HV5"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:1HV5"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:1HV5"
SQ SEQUENCE 492 AA; 55441 MW; B54E260E4AB3D7C3 CRC64;
MARAACLLRA ISRVLLLPLP LLLLLLLLLP SPLMARARPP ESHRHHPVKK GPRLLHAALP
NTLTSVPASH WVPSPAGSSR PLRCGVPDLP DVLNARNRQK RFVLSGGRWE KTDLTYRILR
FPWQLVREQV RQTVAEALQV WSEVTPLTFT EVHEGRADIM IDFARYWHGD NLPFDGPGGI
LAHAFFPKTH REGDVHFDYD ETWTIGDNQG TDLLQVAAHE FGHVLGLQHT TAAKALMSPF
YTFRYPLSLS PDDRRGIQHL YGRPQMAPTS PAPTLSSQAG TDTNEIALLE PETPPDVCET
SFDAVSTIRG ELFFFKAGFV WRLRSGRLQP GYPALASRHW QGLPSPVDAA FEDAQGQIWF
FQGAQYWVYD GEKPVLGPAP LSKLGLQGSP VHAALVWGPE KNKIYFFRGG DYWRFHPRTQ
RVDNPVPRRS TDWRGVPSEI DAAFQDAEGY AYFLRGHLYW KFDPVKVKVL EGFPRPVGPD
FFDCAEPANT FR
