Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00068
Entry Name
UniProt Accession
Theoretical PI
7.63
Molecular Weight
65893.93
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Matrix metalloproteinase-14
Protein Synonyms/Alias
MMP-14; 3.4.24.80; MMP-X1; Membrane-type matrix metalloproteinase 1; MT-MMP 1; MTMMP1; Membrane-type-1 matrix metalloproteinase; MT1-MMP; MT1MMP;
Gene Name
MMP14
Gene Synonyms/Alias
Created Date
01-OCT-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
574
Canonical
TPRRLLYCQRSLLDK
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Anilkumar N, Uekita T, Couchman JR, Nagase H, Seiki M, Itoh Y. Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. FASEB J. 2005Aug;19(10):1326-8. Epub 2005 Jun 9.[PMID:15946988]
Functional Description
Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro- MMP2.
Sequence Annotation
Topological domain: 112 541 Extracellular.
Transmembrane: 542 562 Helical.
Topological domain: 563 582 Cytoplasmic.
Motif: 91 98 Cysteine switch.
Active site: 240 240
Metal binding site: 93 93 Zinc; in inhibited form.
Metal binding site: 239 239 Zinc; catalytic.
Metal binding site: 243 243 Zinc; catalytic.
Metal binding site: 249 249 Zinc; catalytic.
Modified residue: 399 399 Phosphotyrosine; by PKDCC.
Protein Length
582 AA.
Protein Sequence
(Canonical)
MSPAPRPPRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS  60
LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ  120
HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF  180
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE  240
LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGGESGFP TKMPPQPRTT  300
SRPSVPDKPK NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF  360
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF  420
WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG  480
NKYWKFNNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA  540
AVVLPVLLLL LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV                     582
FASTA
(Canonical)
>LipidDB-9606-00068|P50281
MSPAPRPPRCLLLPLLTLGTALASLGSAQSSSFSPEAWLQQYGYLPPGDLRTHTQRSPQS
LSAAIAAMQKFYGLQVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQ
HNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIF
FAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHE
LGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTT
SRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQF
WRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALF
WMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKG
NKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAA
AVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV
Gene Ontology
GO:0031012; C:extracellular matrix; IEA:InterPro
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0005796; C:Golgi lumen; TAS:Reactome
GO:0005887; C:integral component of plasma membrane; TAS:ProtInc
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0005509; F:calcium ion binding; IEA:InterPro
GO:0004222; F:metalloendopeptidase activity; TAS:ProtInc
GO:0016504; F:peptidase activator activity; IEA:Ensembl
GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Ensembl
GO:0008270; F:zinc ion binding; TAS:ProtInc
GO:0001525; P:angiogenesis; IEA:Ensembl
GO:0043615; P:astrocyte cell migration; IEA:Ensembl
GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl
GO:0035988; P:chondrocyte proliferation; IEA:Ensembl
GO:0030574; P:collagen catabolic process; TAS:Reactome
GO:0097094; P:craniofacial suture morphogenesis; IEA:Ensembl
GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl
GO:0001958; P:endochondral ossification; IEA:Ensembl
GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB
GO:0001935; P:endothelial cell proliferation; IEA:Ensembl
GO:0022617; P:extracellular matrix disassembly; TAS:Reactome
GO:0030198; P:extracellular matrix organization; TAS:Reactome
GO:0030324; P:lung development; IEA:Ensembl
GO:0008584; P:male gonad development; IEA:Ensembl
GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl
GO:0001541; P:ovarian follicle development; IEA:Ensembl
GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB
GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB
GO:0006508; P:proteolysis; TAS:ProtInc
GO:0043627; P:response to estrogen; IEA:Ensembl
GO:0001666; P:response to hypoxia; IEA:Ensembl
GO:0009612; P:response to mechanical stimulus; IEA:Ensembl
GO:0006979; P:response to oxidative stress; IEA:Ensembl
GO:0048771; P:tissue remodeling; IEA:Ensembl
GO:0031638; P:zymogen activation; IEA:Ensembl
Interpro
InterPro; IPR000585; Hemopexin-like_dom
InterPro; IPR018487; Hemopexin-like_repeat
InterPro; IPR018486; Hemopexin_CS
InterPro; IPR024079; MetalloPept_cat_dom
InterPro; IPR028693; MMP14
InterPro; IPR001818; Pept_M10_metallopeptidase
InterPro; IPR021190; Pept_M10A
InterPro; IPR021805; Pept_M10A_metallopeptidase_C
InterPro; IPR016293; Pept_M10A_stromelysin-type
InterPro; IPR021158; Pept_M10A_Zn_BS
InterPro; IPR006026; Peptidase_Metallo
InterPro; IPR002477; Peptidoglycan-bd-like
Pfam
Pfam; PF11857; DUF3377;
Pfam; PF00045; Hemopexin;
Pfam; PF00413; Peptidase_M10;
Pfam; PF01471; PG_binding_1;
SMART
SMART; SM00120; HX;
SMART; SM00235; ZnMc;
PROSITE
PROSITE; PS00546; CYSTEINE_SWITCH;
PROSITE; PS00024; HEMOPEXIN;
PROSITE; PS51642; HEMOPEXIN_2;
PROSITE; PS00142; ZINC_PROTEASE;
PRINTS
PRINTS; PR00138; MATRIXIN;