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UniProtKB/Swiss-Prot entry P50281


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MMP14_HUMAN
Primary accession number P50281
Secondary accession numbers A8K5L0 Q6GSF3 Q92678
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on February 1, 2005 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 97)
Name and origin of the protein
Protein name Matrix metalloproteinase-14 [Precursor]
Synonyms MMP-14
EC 3.4.24.80
Membrane-type matrix metalloproteinase 1
MT-MMP 1
MTMMP1
Membrane-type-1 matrix metalloproteinase
MT1-MMP
MT1MMP
MMP-X1
Gene name
Name: MMP14
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
DOI=10.1038/370061a0; PubMed=8015608 [NCBI, ExPASy, EBI, Israel, Japan]
Sato H., Takino T., Okada Y., Cao J., Shinagawa A., Yamamoto E., Seiki M.;
"A matrix metalloproteinase expressed on the surface of invasive tumour cells.";
Nature 370:61-65(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
DOI=10.1016/0378-1119(94)00637-8; PubMed=7721107 [NCBI, ExPASy, EBI, Israel, Japan]
Takino T., Sato H., Yamamoto E., Seiki M.;
"Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain.";
Gene 155:293-298(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.92.7.2730; PubMed=7708715 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-8.
TISSUE=Lung;
DOI=10.1111/j.1432-1033.1995.tb20738.x; PubMed=7649159 [NCBI, ExPASy, EBI, Israel, Japan]
Will H., Hinzmann B.;
"cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment.";
Eur. J. Biochem. 231:602-608(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-8.
Luo G.-X., Reisfeld R.A., Strongin A.Y.;
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1111/j.1432-1033.1996.0239u.x; PubMed=8706726 [NCBI, ExPASy, EBI, Israel, Japan]
Lohi J.L., Westermarck J., Kaehaeri V.M., Keski-Oja J.;
"Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate.";
Eur. J. Biochem. 239:239-247(1996).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-4; LYS-6; PRO-8; VAL-233; ASN-273; TRP-302 AND ILE-355.
NIEHS SNPs program;
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PROTEIN SEQUENCE OF 112-116.
DOI=10.1016/0014-5793(96)00861-7; PubMed=8804434 [NCBI, ExPASy, EBI, Israel, Japan]
Sato H., Kinoshita T., Takino T., Nakayama K., Seiki M.;
"Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2.";
FEBS Lett. 393:101-104(1996).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1021/pr060363j; PubMed=17081065 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[12]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 114-287 IN COMPLEX WITH TIMP2.
DOI=10.1093/emboj/17.17.5238; PubMed=9724659 [NCBI, ExPASy, EBI, Israel, Japan]
Fernandez-Catalan C., Bode W., Huber R., Turk D., Calvete J.J., Lichte A., Tschesche H., Maskos K.;
"Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor.";
EMBO J. 17:5238-5248(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D26512; BAA05519.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X83535; CAA58519.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z48481; CAA88372.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U41078; AAA83770.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X90925; CAA62432.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291325; BAF84014.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY795074; AAV40837.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC064803; AAH64803.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00218398; -.
PIR I38028; I38028.
RefSeq NP_004986.1; -.
UniGene Hs.2399
3D structure databases
PDB
1BQQ; X-ray; 2.75 A; M=114-287.[ExPASy / RCSB / EBI]
1BUV; X-ray; 2.75 A; M=114-287.[ExPASy / RCSB / EBI]
3C7X; X-ray; 1.70 A; A=316-511.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BQQ; -.
1BUV; -.
3C7X; -.
ModBase P50281.
Protein-protein interaction databases
IntAct P50281; 2.
Protein family/group databases
MEROPS M10.014; -.
PTM databases
PhosphoSite P50281; -.
Enzyme and pathway databases
BRENDA 3.4.24.7; 247.
3.4.24.80; 247.
Organism-specific databases
GeneCards GC14P022375; -.
H-InvDB HIX0037743; -.
HGNC HGNC:7160; MMP14.
GenAtlas MMP14.
HPA CAB009918; -.
MIM 600754; gene. [NCBI / EBI]
PharmGKB PA30872; -.
Gene expression databases
ArrayExpress P50281; -.
Bgee P50281; -.
CleanEx HS_MMP14; -.
GermOnline ENSG00000157227; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005578; Cellular component: proteinaceous extracellular matrix (inferred from electronic annotation from InterPro).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004222; Molecular function: metalloendopeptidase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (traceable author statement from ProtInc).
GO:0006508; Biological process: proteolysis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000585; Hemopexin/matrixin.
IPR018486; Hemopexin/matrixin_CS.
IPR018487; Hemopexin/matrixin_repeat.
IPR001818; Pept_M10A_M12B.
IPR016293; Pept_M10A_matrix.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR002477; Peptidoglycan-bd-like.
Graphical view of domain structure.
Gene3D G3DSA:2.110.10.10; Hemopexin; 1.
Pfam PF00045; Hemopexin; 4.
PF00413; Peptidase_M10; 1.
PF01471; PG_binding_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS PR00138; MATRIXIN.
SMART SM00120; HX; 4.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.
PROSITE PS00546; CYSTEINE_SWITCH; 1.
PS00024; HEMOPEXIN; 1.
PS00142; ZINC_PROTEASE; 1.
Proteomic databases
PRIDE P50281; -.
Genome annotation databases
Ensembl ENSG00000157227; Homo sapiens. [Contig view]
GeneID 4323; -.
KEGG hsa:4323; -.
Phylogenomic databases
HOGENOM P50281; -.
HOVERGEN P50281; -.
Other
BindingDB P50281; -.
NextBio 17009; -.
SOURCE MMP14; Homo sapiens.
ProtoNet P50281.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; Disulfide bond; Hydrolase; Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease; Repeat; Signal; Transmembrane; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20     Potential. 
PROPEP   21   111  91     Activation peptide. PRO_0000028798
CHAIN   112   582  471     Matrix metalloproteinase-14. PRO_0000028799
TOPO_DOM   112   541  430     Extracellular (Potential). 
TRANSMEM   542   562  21     Potential. 
TOPO_DOM   563   582  20     Cytoplasmic (Potential). 
DOMAIN   323   366  44     Hemopexin-like 1. 
DOMAIN   368   412  45     Hemopexin-like 2. 
DOMAIN   415   461  47     Hemopexin-like 3. 
DOMAIN   463   508  46     Hemopexin-like 4. 
MOTIF   91    98  8     Cysteine switch (By similarity). 
ACT_SITE   240   240        By similarity. 
METAL   93    93        Zinc; in inhibited form (By similarity). 
METAL   239   239        Zinc; catalytic. 
METAL   243   243        Zinc; catalytic. 
METAL   249   249        Zinc; catalytic. 
DISULFID   319   508        By similarity. 
VARIANT   4     4  1     A -> T (in dbSNP:rs17882219 [NCBI]). VAR_021029 
VARIANT   6     6  1     R -> K (in dbSNP:rs17884647 [NCBI]). VAR_021030 
VARIANT   8     8  1     S -> P (in dbSNP:rs1042703 [NCBI]). VAR_021031 
VARIANT   233   233  1     I -> V (in dbSNP:rs17884841 [NCBI]). VAR_021032 
VARIANT   273   273  1     D -> N (in dbSNP:rs1042704 [NCBI]). VAR_021033 
VARIANT   302   302  1     R -> W (in dbSNP:rs17884719 [NCBI]). VAR_021034 
VARIANT   355   355  1     M -> I (in dbSNP:rs17880989 [NCBI]). VAR_021035 
VARIANT   431   431  1     R -> H (in dbSNP:rs3751489 [NCBI]). VAR_031267 
CONFLICT   338   338        E -> K (in Ref. 1; BAA05519). 
CONFLICT   500   500        S -> P (in Ref. 6; CAA62432). 
STRAND   122   125  4      
TURN   133   135  3      
HELIX   137   154  18      
STRAND   158   160  3      
STRAND   171   173  3      
STRAND   176   182  7      
STRAND   186   189  4      
STRAND   194   202  9      
TURN   208   211  4      
STRAND   213   216  4      
HELIX   233   243  11      
TURN   244   246  3      
STRAND   256   260  5      
HELIX   273   276  4      
HELIX   279   282  4      
TURN   283   285  3      
Sequence information
Length: 582 AA [This is the length of the unprocessed precursor] Molecular weight: 65884 Da [This is the MW of the unprocessed precursor] CRC64: 09EEDCE6A69BBC53 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSPAPRPSRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS 

        70         80         90        100        110        120 
LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ 

       130        140        150        160        170        180 
HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF 

       190        200        210        220        230        240 
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE 

       250        260        270        280        290        300 
LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGGESGFP TKMPPQPRTT 

       310        320        330        340        350        360 
SRPSVPDKPK NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF 

       370        380        390        400        410        420 
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF 

       430        440        450        460        470        480 
WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG 

       490        500        510        520        530        540 
NKYWKFNNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA 

       550        560        570        580 
AVVLPVLLLL LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV 

P50281 in FASTA format

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