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   24-JAN-2024, entry version 197.
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; 10090-ENSMUSP00000000924; -.
DR   ProteomicsDB; 295684; -.
DR   Antibodypedia; 3609; 600 antibodies from 36 providers.
DR   DNASU; 17385; -.
DR   Ensembl; ENSMUST00000000924.13; ENSMUSP00000000924.7; ENSMUSG00000000901.18.
DR   Ensembl; ENSMUST00000120281.8; ENSMUSP00000112940.2; ENSMUSG00000000901.18.
DR   GeneID; 17385; -.
DR   KEGG; mmu:17385; -.
DR   UCSC; uc007fto.1; mouse.
DR   AGR; MGI:97008; -.
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; YWRFNPH; -.
DR   OrthoDB; 2225278at2759; -.
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; 1 hit in 79 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 189 other cell types or tissues.
DR   ExpressionAtlas; Q02853; baseline and differential.
DR   GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.110.10.10; Hemopexin-like domain; 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   PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1.
DR   PANTHER; PTHR10201:SF20; STROMELYSIN-3; 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; Hemopexin-like domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00024; HEMOPEXIN; 1.
DR   PROSITE; PS51642; HEMOPEXIN_2; 4.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
DR   Genevisible; Q02853; MM.
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
//