MMP7_MOUSE
ID MMP7_MOUSE Reviewed; 264 AA.
AC Q10738;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Matrilysin;
DE EC=3.4.24.23;
DE AltName: Full=Matrin;
DE AltName: Full=Matrix metalloproteinase-7;
DE Short=MMP-7;
DE AltName: Full=Pump-1 protease;
DE AltName: Full=Uterine metalloproteinase;
DE Flags: Precursor;
GN Name=Mmp7;
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 [GENOMIC DNA / MRNA].
RC STRAIN=ICR; TISSUE=Uterus;
RX PubMed=7579699; DOI=10.1091/mbc.6.7.851;
RA Wilson C.L., Heppner K.J., Rudolph L.A., Matrisian L.M.;
RT "The metalloproteinase matrilysin is preferentially expressed by epithelial
RT cells in a tissue-restricted pattern in the mouse.";
RL Mol. Biol. Cell 6:851-869(1995).
CC -!- FUNCTION: Degrades casein, gelatins of types I, III, IV, and V, and
CC fibronectin. Activates procollagenase (By similarity). {ECO:0000250}.
CC -!- FUNCTION: May play a role in tissue reorganization.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of
CC insulin. No action on collagen types I, II, IV, V. Cleaves gelatin
CC chain alpha2(I) > alpha1(I).; EC=3.4.24.23;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium 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; L36238; AAA99984.1; -; Genomic_DNA.
DR EMBL; L36243; AAA99984.1; JOINED; Genomic_DNA.
DR EMBL; L36242; AAA99984.1; JOINED; Genomic_DNA.
DR EMBL; L36241; AAA99984.1; JOINED; Genomic_DNA.
DR EMBL; L36240; AAA99984.1; JOINED; Genomic_DNA.
DR EMBL; L36239; AAA99984.1; JOINED; Genomic_DNA.
DR EMBL; L36244; AAA99983.1; -; mRNA.
DR AlphaFoldDB; Q10738; -.
DR SMR; Q10738; -.
DR STRING; 10090.ENSMUSP00000018767; -.
DR MEROPS; M10.008; -.
DR PhosphoSitePlus; Q10738; -.
DR PaxDb; Q10738; -.
DR PeptideAtlas; Q10738; -.
DR PRIDE; Q10738; -.
DR ProteomicsDB; 295694; -.
DR MGI; MGI:103189; Mmp7.
DR eggNOG; KOG1565; Eukaryota.
DR InParanoid; Q10738; -.
DR BRENDA; 3.4.24.23; 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 Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR ChiTaRS; Mmp7; mouse.
DR PRO; PR:Q10738; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q10738; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002780; P:antibacterial peptide biosynthetic process; IMP:MGI.
DR GO; GO:0002779; P:antibacterial peptide secretion; IMP:MGI.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISO:MGI.
DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR028707; Matrilysin.
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 PANTHER; PTHR10201:SF143; PTHR10201:SF143; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen degradation; Extracellular matrix; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..94
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000028740"
FT CHAIN 95..264
FT /note="Matrilysin"
FT /id="PRO_0000028741"
FT MOTIF 85..92
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 87
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 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
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 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 201
FT /note="G -> D (in Ref. 1; AAA99983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 29755 MW; EDA31A5EBAC63342 CRC64;
MQLTLFCFVC LLPGHLALPL SQEAGDVSAH QWEQAQNYLR KFYPHDSKTK KVNSLVDNLK
EMQKFFGLPM TGKLSPYIME IMQKPRCGVP DVAEYSLMPN SPKWHSRIVT YRIVSYTSDL
PRIVVDQIVK KALRMWSMQI PLNFKRVSWG TADIIIGFAR RDHGDSFPFD GPGNTLGHAF
APGPGLGGDA HFDKDEYWTD GEDAGVNFLF AATHEFGHSL GLSHSSVPGT VMYPTYQRDY
SEDFSLTKDD IAGIQKLYGK RNTL
