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 08-NOV-2023, entry version 160.
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).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=22510880; DOI=10.1038/emboj.2012.91;
RA Wilson C.H., Crombie C., van der Weyden L., Poulogiannis G., Rust A.G.,
RA Pardo M., Gracia T., Yu L., Choudhary J., Poulin G.B., McIntyre R.E.,
RA Winton D.J., March H.N., Arends M.J., Fraser A.G., Adams D.J.;
RT "Nuclear receptor binding protein 1 regulates intestinal progenitor cell
RT homeostasis and tumour formation.";
RL EMBO J. 31:2486-2497(2012).
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 -!- TISSUE SPECIFICITY: Expressed in the intestinal epithelium (at protein
CC level). {ECO:0000269|PubMed:22510880}.
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 CCDS; CCDS40531.1; -.
DR AlphaFoldDB; Q10738; -.
DR SMR; Q10738; -.
DR STRING; 10090.ENSMUSP00000018767; -.
DR MEROPS; M10.008; -.
DR PhosphoSitePlus; Q10738; -.
DR PaxDb; 10090-ENSMUSP00000018767; -.
DR PeptideAtlas; Q10738; -.
DR ProteomicsDB; 295694; -.
DR AGR; MGI:103189; -.
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; Collagenase (Catalytic Domain); 1.
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 PANTHER; PTHR10201:SF143; MATRILYSIN; 1.
DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 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; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein 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
//
