MMP17_MOUSE
ID MMP17_MOUSE Reviewed; 578 AA.
AC Q9R0S3; Q80UM9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Matrix metalloproteinase-17;
DE Short=MMP-17;
DE EC=3.4.24.-;
DE AltName: Full=Membrane-type matrix metalloproteinase 4;
DE Short=MT-MMP 4;
DE Short=MTMMP4;
DE AltName: Full=Membrane-type-4 matrix metalloproteinase;
DE Short=MT4-MMP;
DE Short=MT4MMP;
DE Flags: Precursor;
GN Name=Mmp17; Synonyms=Mt4mmp;
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].
RC TISSUE=Embryonic brain;
RX PubMed=10471807; DOI=10.1016/s0014-5793(99)01065-0;
RA Kajita M., Kinoh H., Ito N., Takamura A., Itoh Y., Okada A., Sato H.,
RA Seiki M.;
RT "Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a
RT novel major transcript: isolation of complementary DNA clones for human and
RT mouse mt4-mmp transcripts.";
RL FEBS Lett. 457:353-356(1999).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Seiki M.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10799478; DOI=10.1074/jbc.275.19.14046;
RA English W.R., Puente X.S., Freije J.M.P., Knaeuper V., Amour A.,
RA Merryweather A., Lopez-Otin C., Murphy G.;
RT "Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis
RT factor-alpha convertase activity but does not activate pro-MMP2.";
RL J. Biol. Chem. 275:14046-14055(2000).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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).
RN [6]
RP GPI-ANCHOR, AND MUTAGENESIS OF GLU-248.
RX PubMed=10567400; DOI=10.1074/jbc.274.48.34260;
RA Itoh Y., Kajita M., Kinoh H., Mori H., Okada A., Seiki M.;
RT "Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a
RT glycosylphosphatidylinositol-anchored proteinase.";
RL J. Biol. Chem. 274:34260-34266(1999).
CC -!- FUNCTION: Endopeptidase that degrades various components of the
CC extracellular matrix, such as fibrin. May be involved in the activation
CC of membrane-bound precursors of growth factors or inflammatory
CC mediators, such as tumor necrosis factor-alpha. May also be involved in
CC tumoral process. Not obvious if able to proteolytically activate
CC progelatinase A. Does not hydrolyze collagen types I, II, III, IV and
CC V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.
CC {ECO:0000269|PubMed:10799478}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor;
CC Extracellular side. Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Expressed by monocytes and macrophages.
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; AB021224; BAA82708.2; -; mRNA.
DR EMBL; AJ010731; CAB92315.1; -; mRNA.
DR EMBL; CH466529; EDL19513.1; -; Genomic_DNA.
DR EMBL; BC051917; AAH51917.1; -; mRNA.
DR CCDS; CCDS19695.1; -.
DR RefSeq; NP_035976.3; NM_011846.5.
DR AlphaFoldDB; Q9R0S3; -.
DR SMR; Q9R0S3; -.
DR STRING; 10090.ENSMUSP00000031390; -.
DR MEROPS; M10.017; -.
DR GlyGen; Q9R0S3; 2 sites.
DR iPTMnet; Q9R0S3; -.
DR PhosphoSitePlus; Q9R0S3; -.
DR REPRODUCTION-2DPAGE; Q9R0S3; -.
DR CPTAC; non-CPTAC-3927; -.
DR PaxDb; Q9R0S3; -.
DR PeptideAtlas; Q9R0S3; -.
DR PRIDE; Q9R0S3; -.
DR ProteomicsDB; 291475; -.
DR Antibodypedia; 31995; 315 antibodies from 31 providers.
DR DNASU; 23948; -.
DR Ensembl; ENSMUST00000031390; ENSMUSP00000031390; ENSMUSG00000029436.
DR GeneID; 23948; -.
DR KEGG; mmu:23948; -.
DR UCSC; uc008zsy.1; mouse.
DR CTD; 4326; -.
DR MGI; MGI:1346076; Mmp17.
DR VEuPathDB; HostDB:ENSMUSG00000029436; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000158699; -.
DR HOGENOM; CLU_015489_8_2_1; -.
DR InParanoid; Q9R0S3; -.
DR OMA; WLVCGDP; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q9R0S3; -.
DR TreeFam; TF315428; -.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 23948; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Mmp17; mouse.
DR PRO; PR:Q9R0S3; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9R0S3; protein.
DR Bgee; ENSMUSG00000029436; Expressed in primary motor cortex and 205 other tissues.
DR Genevisible; Q9R0S3; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0042756; P:drinking behavior; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR028726; MMP17.
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:SF21; PTHR10201:SF21; 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; PS51642; HEMOPEXIN_2; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
KW Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT PROPEP 40..124
FT /evidence="ECO:0000250"
FT /id="PRO_0000028821"
FT CHAIN 125..558
FT /note="Matrix metalloproteinase-17"
FT /id="PRO_0000028822"
FT PROPEP 559..578
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000028823"
FT REPEAT 333..382
FT /note="Hemopexin 1"
FT REPEAT 386..432
FT /note="Hemopexin 2"
FT REPEAT 436..479
FT /note="Hemopexin 3"
FT REPEAT 480..527
FT /note="Hemopexin 4"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 107..114
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 307..326
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT LIPID 558
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 336..527
FT /evidence="ECO:0000250"
FT MUTAGEN 248
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10567400"
FT CONFLICT 45
FT /note="A -> G (in Ref. 3; CAB92315)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="L -> V (in Ref. 1; BAA82708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 64333 MW; 168C933B63A1EB7B CRC64;
MGRRPRGPGS PRGPGPPRPG PGLPPLLLVL ALAAHGGCAA PAPRAEDLSL GVEWLSRFGY
LPPADPASGQ LQTQEELSKA ITAMQQFGGL ETTGILDEAT LALMKTPRCS LPDLPPGAQS
RRKRQTPPPT KWSKRNLSWR VRTFPRDSPL GRDTVRALMY YALKVWSDIT PLNFHEVAGN
AADIQIDFSK ADHNDGYPFD GPGGTVAHAF FPGDHHTAGD THFDDDEPWT FRSSDAHGMD
LFAVAVHEFG HAIGLSHVAA PSSIMQPYYQ GPVGDPLRYG LPYEDRVRVW QLYGVRESVS
PTAQLDTPEP EEPPLLPEPP NNRSSTPPQK DVPHRCTAHF DAVAQIRGEA FFFKGKYFWR
LTRDRHLVSL QPAQMHRFWR GLPLHLDSVD AVYERTSDHK IVFFKGDRYW VFKDNNVEEG
YPRPVSDFSL PPGGIDAVFS WAHNDRTYFF KDQLYWRYDD HTRRMDPGYP AQGPLWRGVP
SMLDDAMRWS DGASYFFRGQ EYWKVLDGEL EAAPGYPQST ARDWLVCGEP LADAEDVGPG
PQGRSGAQDG LAVCSCTSDA HRLALPSLLL LTPLLWGL
