ID D3YV89_MOUSE Unreviewed; 551 AA. AC D3YV89; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAR-2024, entry version 107. DE SubName: Full=Matrix metallopeptidase 27 {ECO:0000313|Ensembl:ENSMUSP00000117469.2}; GN Name=Mmp27 {ECO:0000313|Ensembl:ENSMUSP00000117469.2, GN ECO:0000313|MGI:MGI:3039232}; 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:ENSMUSP00000117469.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000117469.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000117469.2, 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:ENSMUSP00000117469.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000117469.2}; 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; D3YV89; -. DR SMR; D3YV89; -. DR MEROPS; M10.027; -. DR iPTMnet; D3YV89; -. DR PhosphoSitePlus; D3YV89; -. DR PaxDb; 10090-ENSMUSP00000091423; -. DR ProteomicsDB; 361235; -. DR Antibodypedia; 31767; 169 antibodies from 28 providers. DR DNASU; 234911; -. DR Ensembl; ENSMUST00000151853.8; ENSMUSP00000117469.2; ENSMUSG00000070323.12. DR UCSC; uc009ocs.1; mouse. DR AGR; MGI:3039232; -. DR MGI; MGI:3039232; Mmp27. DR VEuPathDB; HostDB:ENSMUSG00000070323; -. DR eggNOG; KOG1565; Eukaryota. DR GeneTree; ENSGT00940000161159; -. DR HOGENOM; CLU_015489_6_0_1; -. DR InParanoid; D3YV89; -. DR OMA; IPHACDP; -. DR PhylomeDB; D3YV89; -. DR TreeFam; TF315428; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; D3YV89; Protein. DR Bgee; ENSMUSG00000070323; Expressed in granulocyte and 12 other cell types or tissues. DR ExpressionAtlas; D3YV89; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO: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; IBA:GO_Central. 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: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; 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; MATRIX METALLOPROTEINASE; 1. DR PANTHER; PTHR10201:SF115; MATRIX METALLOPROTEINASE-27; 1. DR Pfam; PF00045; Hemopexin; 3. DR Pfam; PF00413; Peptidase_M10; 1. DR Pfam; PF01471; PG_binding_1; 1. DR PIRSF; PIRSF001191; Peptidase_M10A_matrix; 2. 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 SUPFAM; SSF47090; PGBD-like; 1. DR PROSITE; PS00546; CYSTEINE_SWITCH; 1. DR PROSITE; PS00024; HEMOPEXIN; 1. DR PROSITE; PS51642; HEMOPEXIN_2; 4. PE 3: Inferred from homology; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR621190-2}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR621190-3}; 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 Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001191-2}; KW Zymogen {ECO:0000256|ARBA:ARBA00023145}. FT DOMAIN 116..303 FT /note="Peptidase metallopeptidase" FT /evidence="ECO:0000259|SMART:SM00235" FT REPEAT 317..366 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT REPEAT 367..412 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT REPEAT 414..462 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT REPEAT 463..506 FT /note="Hemopexin" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01011" FT MOTIF 103..110 FT /note="Cysteine switch" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-5" FT ACT_SITE 258 FT /evidence="ECO:0000256|PIRSR:PIRSR001191-1" FT BINDING 105 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 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 169 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 213 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 214 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 221 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 230 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 232 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 236 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 239 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="3" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 239 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 257 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2" FT BINDING 257 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 261 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 261 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2" FT BINDING 267 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR001191-2" FT BINDING 267 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 275 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 327 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 329 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 373 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 420 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 467 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="4" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT BINDING 469 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="5" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-2" FT MOD_RES 401 FT /note="Phosphotyrosine; by PKDCC" FT /evidence="ECO:0000256|PIRSR:PIRSR621190-4" FT DISULFID 320..506 FT /evidence="ECO:0000256|PIRSR:PIRSR621190-3" SQ SEQUENCE 551 AA; 62544 MW; DCB1EB235899FD0A CRC64; MPYKQKQALT EETGMKCLLS LMVNFITLSA AFPPDRKDKN EENNQLAQAY LNQFYSLEIE GSHFVQSKNR SLFDGKLREM QAFFGLTVTG KLDSDTLAIM KVPRCGVPDV GQYGYTLPGW RKYSLTYRIM NYTPDMTPAD VDEAIQKALQ VWSKVTPLTF TRISKGVADI MIAFRTGGKA CSEGSDFFED HRELTYLPIN CLSVHGWCPR HFDGPLGVLG HAFPPGLGLG GDTHFDEDET WIAKDGEGFN LFLVAAHEFG HSLGLSHSND QTALMFPNYI SLDPSKYPLS QDDIDGIQSI YGSPPKVTTK PSGNSEPHAC DPTLTFDAIT TFRREVMFFK GRHLWRVYSD IAGAEFEFID SFWPSLPADL QAAYESPRDE LLVFKDENFW VIRGYSVLPG YPKSIHTLGF PRRVKKIDAA VCDHDTRKTF FFVGIWCWRY DEMAQAMDRG FPQRIIKCFP GIRLRVDAVF QHNGFLYFFH GSRQFEYDMK AKNITQVIKT NSWFLCNEPL NASFNVSVKG KANSIGTVIL HHKRLSLLTF SIVHVLTKTY N //