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Matrix metalloproteinase-25 (MMP-25) (EC 3.4.24.-) (Leukolysin) (Membrane-type matrix metalloproteinase 6) (MT-MMP 6) (MTMMP6) (Membrane-type-6 matrix metalloproteinase) (MT6-MMP) (MT6MMP)

 MMP25_HUMAN             Reviewed;         562 AA.
Q9NPA2; D3DUA8; Q9H3Q0;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
12-SEP-2018, entry version 173.
RecName: Full=Matrix metalloproteinase-25;
Short=MMP-25;
EC=3.4.24.-;
AltName: Full=Leukolysin;
AltName: Full=Membrane-type matrix metalloproteinase 6;
Short=MT-MMP 6;
Short=MTMMP6;
AltName: Full=Membrane-type-6 matrix metalloproteinase;
Short=MT6-MMP;
Short=MT6MMP;
Flags: Precursor;
Name=MMP25; Synonyms=MMP20, MMPL1, MT6MMP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal liver;
PubMed=10706098;
Velasco G., Cal S., Merlos-Suarez A., Ferrando A.A., Alvarez S.,
Nakano A., Arribas J., Lopez-Otin C.;
"Human MT6-matrix metalloproteinase: identification, progelatinase A
activation, and expression in brain tumors.";
Cancer Res. 60:877-882(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10628838; DOI=10.1038/sj.cr.7290028;
Pei D.Q.;
"Leukolysin/MMP25/MT6-MMP: a novel matrix metalloproteinase
specifically expressed in the leukocyte lineage.";
Cell Res. 9:291-303(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND GPI-ANCHOR.
PubMed=11034316; DOI=10.1016/S0014-5793(00)01919-0;
Kojima S., Itoh Y., Matsumoto S., Masuho Y., Seiki M.;
"Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the
second glycosyl-phosphatidyl inositol (GPI)-anchored MMP.";
FEBS Lett. 480:142-146(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
de Saint-Vis B.M., Clair-Moninot V.A., Lambert C.A., Vanbervliet B.,
Pin J.J., Chalus L., Ait-Yahia S., Caux C., Richelle-Nusgens B.V.,
Fossiez F., Lebecque S.;
"Molecular cloning of a novel human membrane-type matrix
metalloproteinase (MT-MMP) predominantly expressed in dendritic
cells.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: May activate progelatinase A.
-!- 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};
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor;
Extracellular side. Secreted, extracellular space, extracellular
matrix.
-!- TISSUE SPECIFICITY: Expressed predominantly in leukocytes, lung
and spleen. Expressed also in colon carcinoma, astrocytoma and
glioblastomas.
-!- 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}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ239053; CAB94713.1; -; mRNA.
EMBL; AF145442; AAF66697.2; -; mRNA.
EMBL; AF185270; AAG17007.1; -; mRNA.
EMBL; AB042328; BAB20584.1; -; mRNA.
EMBL; AJ272137; CAC03490.1; -; mRNA.
EMBL; CH471112; EAW85413.1; -; Genomic_DNA.
EMBL; CH471112; EAW85415.1; -; Genomic_DNA.
CCDS; CCDS10492.1; -.
RefSeq; NP_071913.1; NM_022468.4.
UniGene; Hs.654979; -.
ProteinModelPortal; Q9NPA2; -.
BioGrid; 122149; 1.
IntAct; Q9NPA2; 1.
STRING; 9606.ENSP00000337816; -.
BindingDB; Q9NPA2; -.
ChEMBL; CHEMBL1795103; -.
DrugBank; DB00786; Marimastat.
GuidetoPHARMACOLOGY; 1647; -.
MEROPS; M10.024; -.
iPTMnet; Q9NPA2; -.
PhosphoSitePlus; Q9NPA2; -.
BioMuta; MMP25; -.
DMDM; 12585274; -.
EPD; Q9NPA2; -.
PaxDb; Q9NPA2; -.
PeptideAtlas; Q9NPA2; -.
PRIDE; Q9NPA2; -.
ProteomicsDB; 81949; -.
DNASU; 64386; -.
Ensembl; ENST00000336577; ENSP00000337816; ENSG00000008516.
GeneID; 64386; -.
KEGG; hsa:64386; -.
UCSC; uc002cth.4; human.
CTD; 64386; -.
DisGeNET; 64386; -.
EuPathDB; HostDB:ENSG00000008516.16; -.
GeneCards; MMP25; -.
HGNC; HGNC:14246; MMP25.
HPA; CAB025177; -.
MIM; 608482; gene.
neXtProt; NX_Q9NPA2; -.
OpenTargets; ENSG00000008516; -.
PharmGKB; PA30882; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217928; -.
HOVERGEN; HBG052484; -.
InParanoid; Q9NPA2; -.
KO; K08003; -.
OMA; VDWLTRY; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; Q9NPA2; -.
TreeFam; TF315428; -.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; MMP25; human.
GeneWiki; MMP25; -.
GenomeRNAi; 64386; -.
PRO; PR:Q9NPA2; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000008516; Expressed in 208 organ(s), highest expression level in blood.
CleanEx; HS_MMP20; -.
CleanEx; HS_MMP25; -.
ExpressionAtlas; Q9NPA2; baseline and differential.
Genevisible; Q9NPA2; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060022; P:hard palate development; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 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; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028733; MMP25.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
PANTHER; PTHR10201:SF142; PTHR10201:SF142; 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; SSF50923; SSF50923; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Calcium; Cell membrane; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
Metalloprotease; Protease; Reference proteome; Repeat; Secreted;
Signal; Zinc; Zymogen.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 107 {ECO:0000250}.
/FTId=PRO_0000028852.
CHAIN 108 539 Matrix metalloproteinase-25.
/FTId=PRO_0000028853.
PROPEP 540 562 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000028854.
REPEAT 314 363 Hemopexin 1.
REPEAT 367 412 Hemopexin 2.
REPEAT 413 461 Hemopexin 3.
REPEAT 462 508 Hemopexin 4.
MOTIF 88 95 Cysteine switch. {ECO:0000250}.
COMPBIAS 103 107 Poly-Arg.
COMPBIAS 549 555 Poly-Leu.
ACT_SITE 234 234 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 90 90 Zinc; in inhibited form. {ECO:0000250}.
METAL 233 233 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 237 237 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 243 243 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
LIPID 539 539 GPI-anchor amidated alanine.
{ECO:0000255}.
DISULFID 317 508 {ECO:0000250}.
CONFLICT 47 47 P -> R (in Ref. 3; BAB20584).
{ECO:0000305}.
SEQUENCE 562 AA; 62554 MW; A6A50AE05D969C64 CRC64;
MRLRLRLLAL LLLLLAPPAR APKPSAQDVS LGVDWLTRYG YLPPPHPAQA QLQSPEKLRD
AIKVMQRFAG LPETGRMDPG TVATMRKPRC SLPDVLGVAG LVRRRRRYAL SGSVWKKRTL
TWRVRSFPQS SQLSQETVRV LMSYALMAWG MESGLTFHEV DSPQGQEPDI LIDFARAFHQ
DSYPFDGLGG TLAHAFFPGE HPISGDTHFD DEETWTFGSK DGEGTDLFAV AVHEFGHALG
LGHSSAPNSI MRPFYQGPVG DPDKYRLSQD DRDGLQQLYG KAPQTPYDKP TRKPLAPPPQ
PPASPTHSPS FPIPDRCEGN FDAIANIRGE TFFFKGPWFW RLQPSGQLVS PRPARLHRFW
EGLPAQVRVV QAAYARHRDG RILLFSGPQF WVFQDRQLEG GARPLTELGL PPGEEVDAVF
SWPQNGKTYL VRGRQYWRYD EAAARPDPGY PRDLSLWEGA PPSPDDVTVS NAGDTYFFKG
AHYWRFPKNS IKTEPDAPQP MGPNWLDCPA PSSGPRAPRP PKATPVSETC DCQCELNQAA
GRWPAPIPLL LLPLLVGGVA SR


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