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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //