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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) (MT1-MMP) (MT1MMP)

 MMP14_PIG               Reviewed;         580 AA.
Q9XT90;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
28-FEB-2018, entry version 128.
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=MT1-MMP;
Short=MT1MMP;
Flags: Precursor;
Name=MMP14;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9881602; DOI=10.1016/S0945-053X(98)90098-1;
Caron C., Xue J., Bartlett J.D.;
"Expression and localization of membrane type 1 matrix
metalloproteinase in tooth tissues.";
Matrix Biol. 17:501-511(1998).
-!- 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}.
-!- TISSUE SPECIFICITY: Highly expressed in developing tooth tissues.
-!- 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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EMBL; AF067419; AAD38324.1; -; mRNA.
RefSeq; NP_999404.1; NM_214239.1.
UniGene; Ssc.734; -.
ProteinModelPortal; Q9XT90; -.
SMR; Q9XT90; -.
STRING; 9823.ENSSSCP00000002229; -.
MEROPS; M10.014; -.
PaxDb; Q9XT90; -.
PRIDE; Q9XT90; -.
GeneID; 397471; -.
KEGG; ssc:397471; -.
CTD; 4323; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOGENOM; HOG000217928; -.
HOVERGEN; HBG052484; -.
InParanoid; Q9XT90; -.
KO; K07763; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISS:AgBase.
GO; GO:0016477; P:cell migration; ISS:AgBase.
GO; GO:0030324; P:lung development; ISS:AgBase.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
GO; GO:0045579; P:positive regulation of B cell differentiation; ISS:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IEA:InterPro.
GO; GO:0030335; P:positive regulation of cell migration; IEA:InterPro.
GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
GO; GO:0031638; P:zymogen activation; ISS:AgBase.
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 28 {ECO:0000255}.
PROPEP 29 109 Activation peptide.
/FTId=PRO_0000028802.
CHAIN 110 580 Matrix metalloproteinase-14.
/FTId=PRO_0000028803.
TOPO_DOM 110 539 Extracellular. {ECO:0000255}.
TRANSMEM 540 560 Helical. {ECO:0000255}.
TOPO_DOM 561 580 Cytoplasmic. {ECO:0000255}.
REPEAT 314 362 Hemopexin 1.
REPEAT 363 408 Hemopexin 2.
REPEAT 410 458 Hemopexin 3.
REPEAT 459 506 Hemopexin 4.
MOTIF 89 96 Cysteine switch. {ECO:0000250}.
ACT_SITE 238 238 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 91 91 Zinc; in inhibited form. {ECO:0000250}.
METAL 237 237 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 241 241 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 247 247 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
MOD_RES 397 397 Phosphotyrosine; by PKDCC.
{ECO:0000250|UniProtKB:P50281}.
DISULFID 317 506 {ECO:0000250}.
SEQUENCE 580 AA; 65934 MW; B7B2C2C569A96CAC CRC64;
MSPAPRPVRS LLLPLLTLAS ALASLSSAQS FSPEAWLQQY GYLPPGDLRT HTQRSPQSLS
AAIAAMQRFY GLRVTGKADA DTMKAMRRPR CGVPDKFGAE IKANVRRKRY AIQGLKWQHN
EITFCIQNYT PKVGEYATFE AIRKAFRVWE SATPLRFREV PYAYIREGHE KQADIMIFFA
EGFHGDSTPF DGEGGFLAHA YFPGPNIGGD THFDSAEPWT VRNEDLNGND IFLVAVHELG
HALGLEHSND PSAIMAPFYQ WMDTENFVLP DDDRRGIQQL YGSESGFPTK MPPQPRTTSK
PSVPDKPKNP TYGPNICDGN FDTVAMLRGE MFVFKERWFW RVRKNQVMDG YPMPIGQFWR
GLPASINTAY ERKDGKFVFF KGDKHWVFDE ASLEPGYPKH IKELGRRLPT DKIDAALFWM
PNGKDYFFRG NKYYRFNEEL RAVDSEYPKN IKVWEGIPES PRGSFMGSDE VFTYFYKGNK
YWKFNNQKLK VEPGYPKSAL RDWMGCPSGG RPDEGTEEET EVIIIEVDEE GSGAVSAAAV
VLPVLLLLLV LAVGLAVFFF RRHGTPKRLL YCQRSLLDKV


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