MMP15_MOUSE
ID MMP15_MOUSE Reviewed; 657 AA.
AC O54732;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Matrix metalloproteinase-15;
DE Short=MMP-15;
DE EC=3.4.24.-;
DE AltName: Full=Membrane-type matrix metalloproteinase 2;
DE Short=MT-MMP 2;
DE Short=MTMMP2;
DE AltName: Full=Membrane-type-2 matrix metalloproteinase;
DE Short=MT2-MMP;
DE Short=MT2MMP;
DE Flags: Precursor;
GN Name=Mmp15;
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=Lung;
RX PubMed=9037199; DOI=10.1016/s0014-5793(96)01537-2;
RA Tanaka M., Sato H., Takino T., Iwata K., Inoue M., Seiki M.;
RT "Isolation of a mouse MT2-MMP gene from a lung cDNA library and
RT identification of its product.";
RL FEBS Lett. 402:219-222(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland, and Olfactory epithelium;
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. May activate progelatinase A.
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: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
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; D86332; BAA23667.1; -; mRNA.
DR EMBL; BC047278; AAH47278.1; -; mRNA.
DR EMBL; BC057952; AAH57952.1; -; mRNA.
DR CCDS; CCDS22561.1; -.
DR RefSeq; NP_032635.1; NM_008609.4.
DR AlphaFoldDB; O54732; -.
DR SMR; O54732; -.
DR STRING; 10090.ENSMUSP00000034243; -.
DR MEROPS; M10.015; -.
DR GlyGen; O54732; 2 sites.
DR iPTMnet; O54732; -.
DR PhosphoSitePlus; O54732; -.
DR SwissPalm; O54732; -.
DR MaxQB; O54732; -.
DR PaxDb; O54732; -.
DR PeptideAtlas; O54732; -.
DR PRIDE; O54732; -.
DR ProteomicsDB; 295685; -.
DR Antibodypedia; 3619; 493 antibodies from 37 providers.
DR DNASU; 17388; -.
DR Ensembl; ENSMUST00000034243; ENSMUSP00000034243; ENSMUSG00000031790.
DR GeneID; 17388; -.
DR KEGG; mmu:17388; -.
DR UCSC; uc009myh.1; mouse.
DR CTD; 4324; -.
DR MGI; MGI:109320; Mmp15.
DR VEuPathDB; HostDB:ENSMUSG00000031790; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000156939; -.
DR HOGENOM; CLU_015489_8_1_1; -.
DR InParanoid; O54732; -.
DR OMA; EMQKFYG; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; O54732; -.
DR TreeFam; TF352396; -.
DR BRENDA; 3.4.24.B5; 3474.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR BioGRID-ORCS; 17388; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mmp15; mouse.
DR PRO; PR:O54732; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O54732; protein.
DR Bgee; ENSMUSG00000031790; Expressed in external carotid artery and 238 other tissues.
DR Genevisible; O54732; MM.
DR GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS: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:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
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; IPR028729; MMP15.
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:SF25; PTHR10201:SF25; 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; Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Zinc; Zymogen.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT PROPEP 37..127
FT /evidence="ECO:0000250"
FT /id="PRO_0000028810"
FT CHAIN 128..657
FT /note="Matrix metalloproteinase-15"
FT /id="PRO_0000028811"
FT TOPO_DOM 128..614
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 363..411
FT /note="Hemopexin 1"
FT REPEAT 412..457
FT /note="Hemopexin 2"
FT REPEAT 459..507
FT /note="Hemopexin 3"
FT REPEAT 508..555
FT /note="Hemopexin 4"
FT REGION 295..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 105..112
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 326..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 107
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 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 366..555
FT /evidence="ECO:0000250"
SQ SEQUENCE 657 AA; 74666 MW; 26803400A6836EF2 CRC64;
MGSDRSALGR PGCTGSCLSS RASLLPLLLV LLDCLGHGTA SKDAEVYAAE NWLRLYGYLP
QPSRHMSTMR SAQILASALA EMQSFYGIPV TGVLDEETKT WMKRPRCGVP DQFGVHVKAN
LRRRRKRYTL TGKAWNNYHL TFSIQNYTEK LGWYNSMEAV RRAFQVWEQV TPLVFQEVSY
DDIRLRRRAE ADIMVLFASG FHGDSSPFDG VGGFLAHAYF PGPGLGGDTH FDADEPWTFS
STDLHGISLF LVAVHELGHA LGLEHSSNPS AIMAPFYQWM DTDNFQLPED DLRGIQQLYG
SPDGKPQPTR PLPTVRPRRP GRPDHQPPRP PQPPHPGGKP ERPPKPGPPP QPRATERPDQ
YGPNICDGNF DTVAVLRGEM FVFKGRWFWR VRHNRVLDNY PMPIGHFWRG LPGNISAAYE
RQDGHFVFFK GNRYWLFREA NLEPGYPQPL SSYGTDIPYD RIDTAIWWEP TGHTFFFQAD
RYWRFNEETQ HGDPGYPKPI SVWQGIPTSP KGAFLSNDAA YTYFYKGTKY WKFNNERLRM
EPGHPKSILR DFMGCQEHVE PRSRWPDVAR PPFNPNGGAE PEADGDSKEE NAGDKDEGSR
VVVQMEEVVR TVNVVMVLVP LLLLLCILGL AFALVQMQRK GAPRMLLYCK RSLQEWV
