ID MMP16_MOUSE Reviewed; 607 AA. AC Q9WTR0; Q6PEQ6; Q9ERT6; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 24-JAN-2024, entry version 189. DE RecName: Full=Matrix metalloproteinase-16; DE Short=MMP-16; DE EC=3.4.24.-; DE AltName: Full=Membrane-type matrix metalloproteinase 3; DE Short=MT-MMP 3; DE Short=MTMMP3; DE AltName: Full=Membrane-type-3 matrix metalloproteinase; DE Short=MT3-MMP; DE Short=MT3MMP; DE Flags: Precursor; GN Name=Mmp16; 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 [MRNA]. RA Seiki M., Kinoh H.; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Budde P., Gatsios P., Nienaber N.T., Li H., Staege M.S., Graeve L., RA Heinrich P.C., Frey J.; RT "Differential localization and Triton X-100 solubility of membrane-type RT matrix metalloproteinases 1-3."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Endopeptidase that degrades various components of the CC extracellular matrix, such as collagen type III and fibronectin. CC Activates progelatinase A. Involved in the matrix remodeling of blood CC vessels. It has no effect on type I, II, IV and V collagen. However, CC upon interaction with CSPG4, it may be involved in degradation and CC invasion of type I collagen by melanoma cells (By similarity). CC {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 zinc ions per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC -!- SUBUNIT: Interacts with CSPG4 through CSPG4 chondroitin sulfate CC glycosaminoglycan. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. CC Note=Localized at the cell surface of melanoma cells. {ECO:0000250}. 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 -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. 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; AB021228; BAA78420.1; -; mRNA. DR EMBL; AF282844; AAG17704.1; -; mRNA. DR EMBL; AL683877; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL805957; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466538; EDL05585.1; -; Genomic_DNA. DR EMBL; CH466538; EDL05587.1; -; Genomic_DNA. DR EMBL; BC057926; AAH57926.1; -; mRNA. DR CCDS; CCDS17989.1; -. DR RefSeq; NP_062698.2; NM_019724.4. DR RefSeq; XP_017175506.1; XM_017320017.1. DR AlphaFoldDB; Q9WTR0; -. DR SMR; Q9WTR0; -. DR STRING; 10090.ENSMUSP00000029881; -. DR MEROPS; M10.016; -. DR GlyCosmos; Q9WTR0; 1 site, No reported glycans. DR GlyGen; Q9WTR0; 1 site. DR PhosphoSitePlus; Q9WTR0; -. DR PaxDb; 10090-ENSMUSP00000029881; -. DR ProteomicsDB; 295686; -. DR Antibodypedia; 12678; 455 antibodies from 38 providers. DR DNASU; 17389; -. DR Ensembl; ENSMUST00000029881.10; ENSMUSP00000029881.4; ENSMUSG00000028226.16. DR GeneID; 17389; -. DR KEGG; mmu:17389; -. DR UCSC; uc008sbw.2; mouse. DR AGR; MGI:1276107; -. DR CTD; 4325; -. DR MGI; MGI:1276107; Mmp16. DR VEuPathDB; HostDB:ENSMUSG00000028226; -. DR eggNOG; KOG1565; Eukaryota. DR GeneTree; ENSGT00940000157532; -. DR InParanoid; Q9WTR0; -. DR OMA; KHDRPKP; -. DR OrthoDB; 2225278at2759; -. DR PhylomeDB; Q9WTR0; -. DR TreeFam; TF352396; -. DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases. DR BioGRID-ORCS; 17389; 1 hit in 80 CRISPR screens. DR ChiTaRS; Mmp16; mouse. DR PRO; PR:Q9WTR0; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q9WTR0; Protein. DR Bgee; ENSMUSG00000028226; Expressed in vault of skull and 185 other cell types or tissues. DR ExpressionAtlas; Q9WTR0; baseline and differential. DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0070006; F:metalloaminopeptidase activity; ISO:MGI. DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; ISO:MGI. DR GO; GO:0060348; P:bone development; IGI:MGI. DR GO; GO:0035988; P:chondrocyte proliferation; IGI:MGI. DR GO; GO:0030574; P:collagen catabolic process; IDA:MGI. DR GO; GO:0097094; P:craniofacial suture morphogenesis; IGI:MGI. DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IGI:MGI. DR GO; GO:0001958; P:endochondral ossification; IGI:MGI. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0001503; P:ossification; IGI:MGI. DR GO; GO:0016485; P:protein processing; ISO:MGI. DR GO; GO:0006508; P:proteolysis; ISO:MGI. DR GO; GO:0001501; P:skeletal system development; IBA:GO_Central. 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; IPR021805; Pept_M10A_metallopeptidase_C. 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:SF26; MATRIX METALLOPROTEINASE-16; 1. DR Pfam; PF11857; DUF3377; 1. DR Pfam; PF00045; Hemopexin; 4. 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; 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. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR Genevisible; Q9WTR0; MM. PE 2: Evidence at transcript level; KW Calcium; Cell membrane; Cleavage on pair of basic residues; KW Collagen degradation; Disulfide bond; Glycoprotein; Hydrolase; Membrane; KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen. FT SIGNAL 1..31 FT /evidence="ECO:0000255" FT PROPEP 32..119 FT /evidence="ECO:0000250" FT /id="PRO_0000028814" FT CHAIN 120..607 FT /note="Matrix metalloproteinase-16" FT /id="PRO_0000028815" FT TOPO_DOM 120..564 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 565..585 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 586..607 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 340..388 FT /note="Hemopexin 1" FT REPEAT 389..434 FT /note="Hemopexin 2" FT REPEAT 436..484 FT /note="Hemopexin 3" FT REPEAT 485..532 FT /note="Hemopexin 4" FT REGION 281..340 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 99..106 FT /note="Cysteine switch" FT /evidence="ECO:0000250" FT COMPBIAS 292..312 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 313..327 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 247 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095" FT BINDING 101 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 183 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 193 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 195 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 200 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 201 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 203 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 208 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 215 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 219 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 221 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 223 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 226 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 246 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 250 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P51512" FT BINDING 256 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P51512" FT CARBOHYD 83 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 343..532 FT /evidence="ECO:0000250" FT CONFLICT 17 FT /note="R -> H (in Ref. 1; BAA78420)" FT /evidence="ECO:0000305" FT CONFLICT 19 FT /note="G -> V (in Ref. 2; AAG17704)" FT /evidence="ECO:0000305" FT CONFLICT 196 FT /note="S -> R (in Ref. 2; AAG17704)" FT /evidence="ECO:0000305" SQ SEQUENCE 607 AA; 69571 MW; C4CB54F75B26A296 CRC64; MILLAFSSGR RLDFVHRSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY GYLPPTDPRM SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR CGVPDQTRGS SKFNIRRKRY ALTGQKWQHK HITYSIKNVT PKVGDPETRR AIRRAFDVWQ NVTPLTFEEV PYSELENGKR DVDITIIFAS GFHGDSSPFD GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL FLVAVHELGH ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT RPLPTVPPHR SVPPADPRRH DRPKPPRPPT GRPSYPGAKP NICDGNFNTL AILRREMFVF KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD GNFVFFKGNK YWVFKDTTLQ PGYPHDLITL GNGIPPHGID SAIWWEDVGK TYFFKGDRYW RYSEEMKTMD PGYPKPITIW KGIPESPQGA FVHKENGFTY FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRDK EGLSPPDDVD IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK RSMQEWV //