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   27-MAR-2024, entry version 190.
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}.
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; 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   GlyCosmos; O54732; 2 sites, No reported glycans.
DR   GlyGen; O54732; 2 sites.
DR   iPTMnet; O54732; -.
DR   PhosphoSitePlus; O54732; -.
DR   SwissPalm; O54732; -.
DR   MaxQB; O54732; -.
DR   PaxDb; 10090-ENSMUSP00000034243; -.
DR   PeptideAtlas; O54732; -.
DR   ProteomicsDB; 295685; -.
DR   Antibodypedia; 3619; 516 antibodies from 37 providers.
DR   DNASU; 17388; -.
DR   Ensembl; ENSMUST00000034243.7; ENSMUSP00000034243.6; ENSMUSG00000031790.9.
DR   GeneID; 17388; -.
DR   KEGG; mmu:17388; -.
DR   UCSC; uc009myh.1; mouse.
DR   AGR; MGI:109320; -.
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; YHSHEAV; -.
DR   OrthoDB; 2225278at2759; -.
DR   PhylomeDB; O54732; -.
DR   TreeFam; TF352396; -.
DR   BRENDA; 3.4.24.B5; 3474.
DR   Reactome; R-MMU-1442490; Collagen degradation.
DR   Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
DR   BioGRID-ORCS; 17388; 2 hits in 78 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 240 other cell types or tissues.
DR   GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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:SF25; MATRIX METALLOPROTEINASE-15; 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; O54732; MM.
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
//