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Matrix metalloproteinase-14 (MMP-14) (EC 3.4.24.80) (MMP-X1) (Membrane-type matrix metalloproteinase 1) (MT-MMP 1) (MTMMP1) (Membrane-type-1 matrix metalloproteinase) (MT1-MMP) (MT1MMP)

 MMP14_HUMAN             Reviewed;         582 AA.
P50281; A8K5L0; Q6GSF3; Q92678;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 3.
22-NOV-2017, entry version 188.
RecName: Full=Matrix metalloproteinase-14;
Short=MMP-14;
EC=3.4.24.80;
AltName: Full=MMP-X1;
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-8.
TISSUE=Placenta;
PubMed=8015608; DOI=10.1038/370061a0;
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], AND VARIANT SER-8.
TISSUE=Placenta;
PubMed=7721107; DOI=10.1016/0378-1119(94)00637-8;
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], AND VARIANT SER-8.
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-8.
TISSUE=Lung;
PubMed=7649159; DOI=10.1111/j.1432-1033.1995.tb20738.x;
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].
Luo G.-X., Reisfeld R.A., Strongin A.Y.;
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8706726; DOI=10.1111/j.1432-1033.1996.0239u.x;
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], AND VARIANT SER-8.
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
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; SER-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 GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-8.
TISSUE=Skin;
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).
[11]
PROTEIN SEQUENCE OF 112-116.
PubMed=8804434; DOI=10.1016/0014-5793(96)00861-7;
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).
[12]
FUNCTION IN THE FORMATION OF THE FIBROVASCULAR TISSUES.
PubMed=12714657; DOI=10.1167/iovs.02-0662;
Noda K., Ishida S., Inoue M., Obata K., Oguchi Y., Okada Y., Ikeda E.;
"Production and activation of matrix metalloproteinase-2 in
proliferative diabetic retinopathy.";
Invest. Ophthalmol. Vis. Sci. 44:2163-2170(2003).
[13]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
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).
[14]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=18223680; DOI=10.1038/sj.onc.1211035;
Bonnomet A., Polette M., Strumane K., Gilles C., Dalstein V.,
Kileztky C., Berx G., van Roy F., Birembaut P., Nawrocki-Raby B.;
"The E-cadherin-repressed hNanos1 gene induces tumor cell invasion by
upregulating MT1-MMP expression.";
Oncogene 27:3692-3699(2008).
[15]
FUNCTION.
PubMed=20837484; DOI=10.1074/jbc.M110.165159;
Golubkov V.S., Chekanov A.V., Cieplak P., Aleshin A.E., Chernov A.V.,
Zhu W., Radichev I.A., Zhang D., Dong P.D., Strongin A.Y.;
"The Wnt/planar cell polarity protein-tyrosine kinase-7 (PTK7) is a
highly efficient proteolytic target of membrane type-1 matrix
metalloproteinase: implications in cancer and embryogenesis.";
J. Biol. Chem. 285:35740-35749(2010).
[16]
INTERACTION WITH DLL1.
PubMed=21572390; DOI=10.1038/emboj.2011.136;
Jin G., Zhang F., Chan K.M., Xavier Wong H.L., Liu B., Cheah K.S.,
Liu X., Mauch C., Liu D., Zhou Z.;
"MT1-MMP cleaves Dll1 to negatively regulate Notch signalling to
maintain normal B-cell development.";
EMBO J. 30:2281-2293(2011).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BST2.
PubMed=22065321; DOI=10.1002/jcb.23433;
Gu G., Zhao D., Yin Z., Liu P.;
"BST-2 binding with cellular MT1-MMP blocks cell growth and migration
via decreasing MMP2 activity.";
J. Cell. Biochem. 113:1013-1021(2012).
[18]
FUNCTION.
PubMed=22330140; DOI=10.1038/onc.2012.1;
Cork S.M., Kaur B., Devi N.S., Cooper L., Saltz J.H., Sandberg E.M.,
Kaluz S., Van Meir E.G.;
"A proprotein convertase/MMP-14 proteolytic cascade releases a novel
40 kDa vasculostatin from tumor suppressor BAI1.";
Oncogene 31:5144-5152(2012).
[19]
PHOSPHORYLATION AT TYR-399.
PubMed=25171405; DOI=10.1016/j.cell.2014.06.048;
Bordoli M.R., Yum J., Breitkopf S.B., Thon J.N., Italiano J.E. Jr.,
Xiao J., Worby C., Wong S.K., Lin G., Edenius M., Keller T.L.,
Asara J.M., Dixon J.E., Yeo C.Y., Whitman M.;
"A secreted tyrosine kinase acts in the extracellular environment.";
Cell 158:1033-1044(2014).
[20]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 114-287 IN COMPLEX WITH
TIMP2.
PubMed=9724659; DOI=10.1093/emboj/17.17.5238;
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).
[21]
VARIANT WNCHRS ARG-17, AND CHARACTERIZATION OF VARIANT WNCHRS ARG-17.
PubMed=22922033; DOI=10.1016/j.ajhg.2012.07.022;
Evans B.R., Mosig R.A., Lobl M., Martignetti C.R., Camacho C.,
Grum-Tokars V., Glucksman M.J., Martignetti J.A.;
"Mutation of membrane type-1 metalloproteinase, MT1-MMP, causes the
multicentric osteolysis and arthritis disease Winchester syndrome.";
Am. J. Hum. Genet. 91:572-576(2012).
-!- 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 (By
similarity). May be involved in actin cytoskeleton reorganization
by cleaving PTK7 (PubMed:20837484). 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 (PubMed:12714657). Cleaves ADGRB1 to release
vasculostatin-40 which inhibits angiogenesis (PubMed:22330140).
{ECO:0000250|UniProtKB:P53690, ECO:0000269|PubMed:12714657,
ECO:0000269|PubMed:20837484, ECO:0000269|PubMed:22065321,
ECO:0000269|PubMed:22330140}.
-!- 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
(PubMed:21572390). {ECO:0000269|PubMed:21572390,
ECO:0000269|PubMed:22065321, ECO:0000269|PubMed:9724659}.
-!- INTERACTION:
Q9BV57:ADI1; NbExp=4; IntAct=EBI-992788, EBI-992807;
P56945:BCAR1; NbExp=3; IntAct=EBI-992788, EBI-702093;
Q8N6L0:CCDC155; NbExp=3; IntAct=EBI-992788, EBI-749265;
P22455:FGFR4; NbExp=6; IntAct=EBI-992788, EBI-6256193;
Q9R064:Gorasp2 (xeno); NbExp=14; IntAct=EBI-992788, EBI-4422912;
P53667:LIMK1; NbExp=4; IntAct=EBI-992788, EBI-444403;
P51884:LUM; NbExp=2; IntAct=EBI-992788, EBI-725780;
P16035:TIMP2; NbExp=2; IntAct=EBI-992788, EBI-1033507;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Melanosome. Cytoplasm.
Note=Identified by mass spectrometry in melanosome fractions from
stage I to stage IV. Forms a complex with BST2 and localizes to
the cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in stromal cells of colon, breast,
and head and neck. Expressed in lung tumors.
{ECO:0000269|PubMed:18223680}.
-!- INDUCTION: Up-regulated by NANOS1. {ECO:0000269|PubMed:18223680}.
-!- 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: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- PTM: Tyrosine phosphorylated by PKDCC/VLK.
{ECO:0000269|PubMed:25171405}.
-!- DISEASE: Winchester syndrome (WNCHRS) [MIM:277950]: A disease
characterized by severe osteolysis in the hands and feet,
generalized osteoporosis, bone thinning, and absence of
subcutaneous nodules. Various additional features include coarse
face, corneal opacities, gum hypertrophy, and EKG changes.
{ECO:0000269|PubMed:22922033}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp14/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MMP14ID41391ch14q11.html";
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EMBL; D26512; BAA05519.1; -; mRNA.
EMBL; X83535; CAA58519.1; -; mRNA.
EMBL; Z48481; CAA88372.1; -; mRNA.
EMBL; U41078; AAA83770.1; -; mRNA.
EMBL; X90925; CAA62432.1; -; mRNA.
EMBL; AK291325; BAF84014.1; -; mRNA.
EMBL; AY795074; AAV40837.1; -; Genomic_DNA.
EMBL; AL135998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC064803; AAH64803.1; -; mRNA.
CCDS; CCDS9577.1; -.
PIR; I38028; I38028.
RefSeq; NP_004986.1; NM_004995.3.
UniGene; Hs.2399; -.
PDB; 1BQQ; X-ray; 2.75 A; M=114-287.
PDB; 1BUV; X-ray; 2.75 A; M=114-287.
PDB; 2MQS; NMR; -; A=316-511.
PDB; 3C7X; X-ray; 1.70 A; A=316-511.
PDB; 3MA2; X-ray; 2.05 A; A/D=112-292.
PDB; 3X23; X-ray; 2.40 A; B=563-582.
PDB; 4P3C; X-ray; 1.94 A; M=215-227.
PDB; 4P3D; X-ray; 1.95 A; C/M=215-227.
PDB; 4QXU; X-ray; 2.30 A; K=218-228.
PDB; 5H0U; X-ray; 2.24 A; A=116-285.
PDBsum; 1BQQ; -.
PDBsum; 1BUV; -.
PDBsum; 2MQS; -.
PDBsum; 3C7X; -.
PDBsum; 3MA2; -.
PDBsum; 3X23; -.
PDBsum; 4P3C; -.
PDBsum; 4P3D; -.
PDBsum; 4QXU; -.
PDBsum; 5H0U; -.
ProteinModelPortal; P50281; -.
SMR; P50281; -.
BioGrid; 110466; 17.
CORUM; P50281; -.
DIP; DIP-35111N; -.
IntAct; P50281; 36.
MINT; MINT-246780; -.
STRING; 9606.ENSP00000308208; -.
BindingDB; P50281; -.
ChEMBL; CHEMBL3869; -.
DrugBank; DB00786; Marimastat.
GuidetoPHARMACOLOGY; 1638; -.
MEROPS; M10.014; -.
iPTMnet; P50281; -.
PhosphoSitePlus; P50281; -.
SwissPalm; P50281; -.
BioMuta; MMP14; -.
DMDM; 317373419; -.
EPD; P50281; -.
MaxQB; P50281; -.
PaxDb; P50281; -.
PeptideAtlas; P50281; -.
PRIDE; P50281; -.
Ensembl; ENST00000311852; ENSP00000308208; ENSG00000157227.
GeneID; 4323; -.
KEGG; hsa:4323; -.
UCSC; uc001whc.5; human.
CTD; 4323; -.
DisGeNET; 4323; -.
EuPathDB; HostDB:ENSG00000157227.12; -.
GeneCards; MMP14; -.
H-InvDB; HIX0202102; -.
HGNC; HGNC:7160; MMP14.
HPA; CAB009918; -.
HPA; HPA051432; -.
MalaCards; MMP14; -.
MIM; 277950; phenotype.
MIM; 600754; gene.
neXtProt; NX_P50281; -.
OpenTargets; ENSG00000157227; -.
Orphanet; 85196; Nodulosis-arthropathy-osteolysis syndrome.
Orphanet; 3460; Torg-Winchester syndrome.
PharmGKB; PA30872; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217928; -.
HOVERGEN; HBG052484; -.
InParanoid; P50281; -.
KO; K07763; -.
OMA; VMFPWYQ; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P50281; -.
TreeFam; TF352396; -.
BioCyc; MetaCyc:ENSG00000157227-MONOMER; -.
BRENDA; 3.4.24.80; 2681.
BRENDA; 3.4.24.B5; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
SIGNOR; P50281; -.
ChiTaRS; MMP14; human.
EvolutionaryTrace; P50281; -.
GeneWiki; MMP14; -.
GenomeRNAi; 4323; -.
PRO; PR:P50281; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000157227; -.
CleanEx; HS_MMP14; -.
ExpressionAtlas; P50281; baseline and differential.
Genevisible; P50281; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005615; C:extracellular space; IMP:CAFA.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0044354; C:macropinosome; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IMP:CAFA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0070006; F:metalloaminopeptidase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0043615; P:astrocyte cell migration; IEA:Ensembl.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
GO; GO:0048870; P:cell motility; TAS:ParkinsonsUK-UCL.
GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
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; IEP:UniProtKB.
GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0045579; P:positive regulation of B cell differentiation; ISS:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:1905523; P:positive regulation of macrophage migration; IEA:Ensembl.
GO; GO:0010831; P:positive regulation of myotube differentiation; ISS:UniProtKB.
GO; GO:0016485; P:protein processing; TAS:ParkinsonsUK-UCL.
GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:1990834; P:response to odorant; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0048771; P:tissue remodeling; IEA:Ensembl.
GO; GO:0031638; P:zymogen activation; IEA:Ensembl.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 2.
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.
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.
1: Evidence at protein level;
3D-structure; Calcium; Cleavage on pair of basic residues;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Disulfide bond; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Phosphoprotein; Polymorphism; Protease;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 111 Activation peptide.
{ECO:0000269|PubMed:8804434}.
/FTId=PRO_0000028798.
CHAIN 112 582 Matrix metalloproteinase-14.
/FTId=PRO_0000028799.
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.
METAL 243 243 Zinc; catalytic.
METAL 249 249 Zinc; catalytic.
MOD_RES 399 399 Phosphotyrosine; by PKDCC.
{ECO:0000303|PubMed:25171405}.
DISULFID 319 508 {ECO:0000250}.
VARIANT 4 4 A -> T (in dbSNP:rs17882219).
{ECO:0000269|Ref.8}.
/FTId=VAR_021029.
VARIANT 6 6 R -> K (in dbSNP:rs17884647).
{ECO:0000269|Ref.8}.
/FTId=VAR_021030.
VARIANT 8 8 P -> S (in dbSNP:rs1042703).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7649159,
ECO:0000269|PubMed:7708715,
ECO:0000269|PubMed:7721107,
ECO:0000269|PubMed:8015608,
ECO:0000269|Ref.8}.
/FTId=VAR_021031.
VARIANT 17 17 T -> R (in WNCHRS; results in increased
MMP14 proteosomal degradation and reduced
protein localization to cell membrane;
dbSNP:rs587777039).
{ECO:0000269|PubMed:22922033}.
/FTId=VAR_070567.
VARIANT 233 233 I -> V (in dbSNP:rs17884841).
{ECO:0000269|Ref.8}.
/FTId=VAR_021032.
VARIANT 273 273 D -> N (in dbSNP:rs1042704).
{ECO:0000269|Ref.8}.
/FTId=VAR_021033.
VARIANT 302 302 R -> W (in dbSNP:rs17884719).
{ECO:0000269|Ref.8}.
/FTId=VAR_021034.
VARIANT 355 355 M -> I (in dbSNP:rs17880989).
{ECO:0000269|Ref.8}.
/FTId=VAR_021035.
VARIANT 431 431 R -> H (in dbSNP:rs3751489).
/FTId=VAR_031267.
CONFLICT 338 338 E -> K (in Ref. 1; BAA05519).
{ECO:0000305}.
CONFLICT 500 500 S -> P (in Ref. 6; CAA62432).
{ECO:0000305}.
STRAND 120 128 {ECO:0000244|PDB:3MA2}.
TURN 133 135 {ECO:0000244|PDB:3MA2}.
HELIX 137 154 {ECO:0000244|PDB:3MA2}.
STRAND 158 161 {ECO:0000244|PDB:3MA2}.
HELIX 164 168 {ECO:0000244|PDB:3MA2}.
STRAND 171 173 {ECO:0000244|PDB:1BQQ}.
STRAND 176 182 {ECO:0000244|PDB:3MA2}.
STRAND 187 190 {ECO:0000244|PDB:3MA2}.
STRAND 194 202 {ECO:0000244|PDB:3MA2}.
TURN 208 211 {ECO:0000244|PDB:3MA2}.
STRAND 213 216 {ECO:0000244|PDB:3MA2}.
STRAND 230 232 {ECO:0000244|PDB:3MA2}.
HELIX 233 244 {ECO:0000244|PDB:3MA2}.
STRAND 258 260 {ECO:0000244|PDB:3MA2}.
HELIX 273 283 {ECO:0000244|PDB:3MA2}.
HELIX 318 320 {ECO:0000244|PDB:3C7X}.
STRAND 324 329 {ECO:0000244|PDB:3C7X}.
STRAND 332 337 {ECO:0000244|PDB:3C7X}.
STRAND 340 345 {ECO:0000244|PDB:3C7X}.
STRAND 354 356 {ECO:0000244|PDB:3C7X}.
HELIX 357 360 {ECO:0000244|PDB:3C7X}.
STRAND 370 373 {ECO:0000244|PDB:3C7X}.
STRAND 375 377 {ECO:0000244|PDB:2MQS}.
STRAND 379 383 {ECO:0000244|PDB:3C7X}.
STRAND 386 391 {ECO:0000244|PDB:3C7X}.
STRAND 400 402 {ECO:0000244|PDB:3C7X}.
HELIX 403 405 {ECO:0000244|PDB:3C7X}.
STRAND 416 420 {ECO:0000244|PDB:3C7X}.
TURN 422 424 {ECO:0000244|PDB:3C7X}.
STRAND 427 431 {ECO:0000244|PDB:3C7X}.
STRAND 434 439 {ECO:0000244|PDB:3C7X}.
TURN 440 443 {ECO:0000244|PDB:3C7X}.
STRAND 450 452 {ECO:0000244|PDB:3C7X}.
HELIX 453 455 {ECO:0000244|PDB:3C7X}.
STRAND 464 468 {ECO:0000244|PDB:3C7X}.
STRAND 472 479 {ECO:0000244|PDB:3C7X}.
STRAND 482 487 {ECO:0000244|PDB:3C7X}.
TURN 488 491 {ECO:0000244|PDB:3C7X}.
HELIX 501 504 {ECO:0000244|PDB:3C7X}.
STRAND 569 575 {ECO:0000244|PDB:3X23}.
SEQUENCE 582 AA; 65894 MW; 3722DE286A4BBCDE CRC64;
MSPAPRPPRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL RTHTQRSPQS
LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG AEIKANVRRK RYAIQGLKWQ
HNEITFCIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIF
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE
LGHALGLEHS SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGGESGFP TKMPPQPRTT
SRPSVPDKPK NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF
WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG
NKYWKFNNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA
AVVLPVLLLL LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV


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