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Matrix metalloproteinase-14 (MMP-14) (EC 3.4.24.80) (Membrane-type matrix metalloproteinase 1) (MT-MMP 1) (MTMMP1) (Membrane-type-1 matrix metalloproteinase) (MT-MMP) (MT1-MMP) (MT1MMP)

 MMP14_RAT               Reviewed;         582 AA.
Q10739; Q6IN06;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
12-SEP-2018, entry version 161.
RecName: Full=Matrix metalloproteinase-14;
Short=MMP-14;
EC=3.4.24.80;
AltName: Full=Membrane-type matrix metalloproteinase 1;
Short=MT-MMP 1;
Short=MTMMP1;
AltName: Full=Membrane-type-1 matrix metalloproteinase;
Short=MT-MMP;
Short=MT1-MMP;
Short=MT1MMP;
Flags: Precursor;
Name=Mmp14; Synonyms=Mtmmp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7708715; DOI=10.1073/pnas.92.7.2730;
Okada A., Bellocq J.-P., Rouyer N., Chenard M.P., Rio M.C.,
Chambon P., Basset P.;
"Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in
stromal cells of human colon, breast, and head and neck carcinomas.";
Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Cossins J., Clements J., Catlin G., Wells G.;
"Expression and function of MT-MMP in glial cells.";
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Endopeptidase that degrades various components of the
extracellular matrix such as collagen. Activates progelatinase A.
Essential for pericellular collagenolysis and modeling of skeletal
and extraskeletal connective tissues during development. May be
involved in actin cytoskeleton reorganization by cleaving PTK7.
Acts as a positive regulator of cell growth and migration via
activation of MMP15 in association with pro-MMP2. Involved in the
formation of the fibrovascular tissues in association with pro-
MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits
angiogenesis. {ECO:0000250|UniProtKB:P50281,
ECO:0000250|UniProtKB:P53690}.
-!- CATALYTIC ACTIVITY: Endopeptidase activity. Activates
progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38.
Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide
of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and
354-Gln-|-Thr-355 in the aggrecan interglobular domain.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with BST2.
Interacts with DLL1; inhibits DLL1-induced Notch signaling.
{ECO:0000250|UniProtKB:P50281}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Melanosome {ECO:0000250}.
Cytoplasm {ECO:0000250}. Note=Forms a complex with BST2 and
localizes to the cytoplasm. {ECO:0000250}.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
{ECO:0000250|UniProtKB:P50281}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X83537; CAA58521.1; -; mRNA.
EMBL; X91785; CAA62897.1; -; mRNA.
EMBL; BC072509; AAH72509.1; -; mRNA.
PIR; I84471; I84471.
RefSeq; NP_112318.1; NM_031056.1.
UniGene; Rn.10371; -.
ProteinModelPortal; Q10739; -.
SMR; Q10739; -.
STRING; 10116.ENSRNOP00000049168; -.
MEROPS; M10.014; -.
iPTMnet; Q10739; -.
PhosphoSitePlus; Q10739; -.
PaxDb; Q10739; -.
PRIDE; Q10739; -.
Ensembl; ENSRNOT00000075610; ENSRNOP00000065434; ENSRNOG00000010947.
GeneID; 81707; -.
KEGG; rno:81707; -.
UCSC; RGD:620198; rat.
CTD; 4323; -.
RGD; 620198; Mmp14.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217928; -.
HOVERGEN; HBG052484; -.
InParanoid; Q10739; -.
KO; K07763; -.
OMA; YQNNEVD; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; Q10739; -.
TreeFam; TF352396; -.
Reactome; R-RNO-1442490; Collagen degradation.
Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
Reactome; R-RNO-1592389; Activation of Matrix Metalloproteinases.
PRO; PR:Q10739; -.
Proteomes; UP000002494; Chromosome 15.
Bgee; ENSRNOG00000010947; Expressed in 10 organ(s), highest expression level in liver.
Genevisible; Q10739; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
GO; GO:0044354; C:macropinosome; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IPI:RGD.
GO; GO:0070006; F:metalloaminopeptidase activity; IEA:Ensembl.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEP:RGD.
GO; GO:0043615; P:astrocyte cell migration; IEP:RGD.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; IEA:Ensembl.
GO; GO:0097094; P:craniofacial suture morphogenesis; IEA:Ensembl.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
GO; GO:0001935; P:endothelial cell proliferation; IEP:RGD.
GO; GO:0060322; P:head development; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:RGD.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
GO; GO:0001503; P:ossification; IEP:RGD.
GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
GO; GO:0045579; P:positive regulation of B cell differentiation; ISS:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:1905523; P:positive regulation of macrophage migration; IEA:Ensembl.
GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
GO; GO:0010954; P:positive regulation of protein processing; IMP:RGD.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0009725; P:response to hormone; IDA:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:1990834; P:response to odorant; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
GO; GO:0048771; P:tissue remodeling; IDA:RGD.
GO; GO:0031638; P:zymogen activation; IEA:Ensembl.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028693; MMP14.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021805; Pept_M10A_metallopeptidase_C.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
InterPro; IPR036366; PGBDSf.
PANTHER; PTHR10201:SF24; PTHR10201:SF24; 1.
Pfam; PF11857; DUF3377; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Calcium; Cleavage on pair of basic residues; Complete proteome;
Cytoplasm; Disulfide bond; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Phosphoprotein; Protease; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 111 Activation peptide.
/FTId=PRO_0000028806.
CHAIN 112 582 Matrix metalloproteinase-14.
/FTId=PRO_0000028807.
TOPO_DOM 112 541 Extracellular. {ECO:0000255}.
TRANSMEM 542 562 Helical. {ECO:0000255}.
TOPO_DOM 563 582 Cytoplasmic. {ECO:0000255}.
REPEAT 316 364 Hemopexin 1.
REPEAT 365 410 Hemopexin 2.
REPEAT 412 460 Hemopexin 3.
REPEAT 461 508 Hemopexin 4.
MOTIF 91 98 Cysteine switch. {ECO:0000250}.
ACT_SITE 240 240 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 93 93 Zinc; in inhibited form. {ECO:0000250}.
METAL 239 239 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 243 243 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 249 249 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
MOD_RES 399 399 Phosphotyrosine; by PKDCC.
{ECO:0000250|UniProtKB:P50281}.
DISULFID 319 508 {ECO:0000250}.
CONFLICT 68 68 M -> I (in Ref. 1; CAA58521).
{ECO:0000305}.
CONFLICT 255 255 A -> D (in Ref. 1; CAA58521).
{ECO:0000305}.
SEQUENCE 582 AA; 66080 MW; 48F1A8E3065E1AE8 CRC64;
MSPAPRPSRS LLLPLLTLGT TLASLGWAQS SNFSPEAWLQ QYGYLPPGDL RTHTQRSPQS
LSAAIAAMQR FYGLQVTGKA DSDTMKAMRR PRCGVPDKFG TEIKANVRRK RYAIQGLKWQ
HNEITFCIQN YTPKVGEYAT FEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIL
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVQNEDLNG NDIFLVAVHE
LGHALGLEHS NDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT
SRPSVPDKPR NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF
WMPNGKTYFF RGNKYYRFNE EFRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG
NKYWKFNNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA
AVVLPVLLLL LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV


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