MMP16_MOUSE
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 03-AUG-2022, entry version 181.
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}.
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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 GlyGen; Q9WTR0; 1 site.
DR PhosphoSitePlus; Q9WTR0; -.
DR PaxDb; Q9WTR0; -.
DR PRIDE; Q9WTR0; -.
DR ProteomicsDB; 295686; -.
DR Antibodypedia; 12678; 417 antibodies from 38 providers.
DR DNASU; 17389; -.
DR Ensembl; ENSMUST00000029881; ENSMUSP00000029881; ENSMUSG00000028226.
DR GeneID; 17389; -.
DR KEGG; mmu:17389; -.
DR UCSC; uc008sbw.2; mouse.
DR CTD; 4325; -.
DR MGI; MGI:1276107; Mmp16.
DR VEuPathDB; HostDB:ENSMUSG00000028226; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000157532; -.
DR InParanoid; Q9WTR0; -.
DR OMA; DFMGCEG; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q9WTR0; -.
DR TreeFam; TF352396; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 17389; 1 hit in 75 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 184 other tissues.
DR ExpressionAtlas; Q9WTR0; baseline and differential.
DR Genevisible; Q9WTR0; MM.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005887; C:integral component of 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; 2.110.10.10; -; 1.
DR Gene3D; 3.40.390.10; -; 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; IPR028697; MMP16.
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:SF26; PTHR10201:SF26; 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; SSF47090; SSF47090; 1.
DR SUPFAM; SSF50923; SSF50923; 1.
DR PROSITE; PS00546; CYSTEINE_SWITCH; 1.
DR PROSITE; PS00024; HEMOPEXIN; 1.
DR PROSITE; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
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
