ID Q5SSG2_MOUSE Unreviewed; 407 AA. AC Q5SSG2; DT 21-DEC-2004, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 2. DT 27-MAR-2024, entry version 135. DE SubName: Full=Matrix metallopeptidase 28 (epilysin) {ECO:0000313|Ensembl:ENSMUSP00000112566.2}; GN Name=Mmp28 {ECO:0000313|Ensembl:ENSMUSP00000112566.2, GN ECO:0000313|MGI:MGI:2153062}; 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 {ECO:0000313|Ensembl:ENSMUSP00000112566.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000112566.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112566.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000112566.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112566.2}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; CC Note=Can bind about 5 Ca(2+) ions per subunit. CC {ECO:0000256|PIRSR:PIRSR621190-2}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR621190-2}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR621190- CC 2}; CC -!- SIMILARITY: Belongs to the peptidase M10A family. CC {ECO:0000256|ARBA:ARBA00010370}. 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 AlphaFoldDB; Q5SSG2; -. DR SMR; Q5SSG2; -. DR MaxQB; Q5SSG2; -. DR ProteomicsDB; 353507; -. DR Antibodypedia; 73349; 331 antibodies from 32 providers. DR Ensembl; ENSMUST00000119346.2; ENSMUSP00000112566.2; ENSMUSG00000020682.18. DR UCSC; uc007kpd.1; mouse. DR AGR; MGI:2153062; -. DR MGI; MGI:2153062; Mmp28. DR VEuPathDB; HostDB:ENSMUSG00000020682; -. DR GeneTree; ENSGT00940000159596; -. DR HOGENOM; CLU_015489_1_0_1; -. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000020682; Expressed in ectoplacental cone and 72 other cell types or tissues. DR ExpressionAtlas; Q5SSG2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IMP:MGI. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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; IPR036375; Hemopexin-like_dom_sf. DR InterPro; IPR018487; Hemopexin-like_repeat. 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; IPR002477; Peptidoglycan-bd-like. DR InterPro; IPR036365; PGBD-like_sf. DR PANTHER; PTHR10201; MATRIX METALLOPROTEINASE; 1. DR PANTHER; PTHR10201:SF298; MATRIX METALLOPROTEINASE-28; 1. DR Pfam; PF00045; Hemopexin; 1. DR Pfam; PF00413; Peptidase_M10; 1. DR Pfam; PF01471; PG_binding_1; 1. DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1. DR PRINTS; PR00138; MATRIXIN. DR SMART; SM00120; HX; 1. DR SMART; SM00235; ZnMc; 1. DR SUPFAM; SSF50923; Hemopexin-like domain; 1. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR SUPFAM; SSF47090; PGBD-like; 1. DR PROSITE; PS51642; HEMOPEXIN_2; 1. PE 1: Evidence at protein level; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR621190-2}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR001191-2}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Proteomics identification {ECO:0007829|MaxQB:Q5SSG2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001191-2}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..407 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004262695" FT DOMAIN 126..285 FT /note="Peptidase metallopeptidase" FT /evidence="ECO:0000259|SMART:SM00235" FT REPEAT 325..369 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT ACT_SITE 241 FT /evidence="ECO:0000256|PIRSR:PIRSR001191-1" FT BINDING 91 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:0000256|PIRSR:PIRSR621190-2" FT BINDING 180 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 190 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 192 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 199 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 200 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 207 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 217 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 219 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 222 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 222 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 244 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 244 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2" FT BINDING 250 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 250 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2" FT BINDING 258 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 329 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 331 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 376 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" SQ SEQUENCE 407 AA; 45838 MW; 291BE954C1669FA0 CRC64; MVAGVSLLLR ALPLLLWGCQ DAQPTQHGLP ELRQEAEAFL EKYGYLSEQG SKAPASAQFR NAIREFQWIS QLPLSGVLDQ ATLRQMTRPR CGVADTDSHA TWTERISTLL AGHRAKMRRK KRFAKPGNKW YKQHLSYRLV NWPERLPEPA VRGAVRAAFQ LWSNVSALEF WEAPATGPAD IRLTFFQGDH NDGLANAFDG PGGALAHAFL PRRGEAHFDG DERWSLSRRR GRNLFVVLAH EIGHTLGLTH SPAPRALMAP YYKKLGRDAL LSWDDVLAVQ SLYGKPLGRS VATQLPGKVF TDFEAWDPHN SQSRRPETRG PKYCHSSFDA ITVDGQWRLY VFKGSYFWEV TVDGNVSEPR PLQKRWPGLP PGIEAAAVSL EDGDFYFFKG TGRRKDREQT PFPSGNY //