MMP26_HUMAN
ID MMP26_HUMAN Reviewed; 261 AA.
AC Q9NRE1; Q3MJ78; Q9GZS2; Q9NR87;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Matrix metalloproteinase-26;
DE Short=MMP-26;
DE EC=3.4.24.-;
DE AltName: Full=Endometase;
DE AltName: Full=Matrilysin-2;
DE Flags: Precursor;
GN Name=MMP26;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10824119; DOI=10.1046/j.1432-1327.2000.01363.x;
RA Begnoit de Coignac A., Elson G.C.A., Delneste Y., Magistrelli G.,
RA Jeannin P., Aubry J.-P., Berthier O., Schmitt D., Bonnefoy J.-Y.,
RA Gauchat J.-F.;
RT "Cloning of MMP-26 A novel matrilysin-like proteinase.";
RL Eur. J. Biochem. 267:3323-3329(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10987280;
RA Uria J.A., Lopez-Otin C.;
RT "Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and
RT showing the minimal domain organization required for secretion, latency,
RT and activity.";
RL Cancer Res. 60:4745-4751(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLU-43.
RX PubMed=10801841; DOI=10.1074/jbc.m002349200;
RA Park H.I., Ni J., Gerkema F.E., Liu D., Belozerov V.E., Sang Q.-X.A.;
RT "Identification and characterization of Homo sapiens endometase (matrix
RT metalloproteinase-26) from endometrial tumor.";
RL J. Biol. Chem. 275:20540-20544(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-43.
RC TISSUE=Kidney;
RX PubMed=11389678; DOI=10.1042/0264-6021:3560705;
RA Marchenko G.N., Ratnikov B.I., Rozanov D.V., Godzik A., Deryugina E.I.,
RA Strongin A.Y.;
RT "Characterization of matrix metalloproteinase-26, a novel metalloproteinase
RT widely expressed in cancer cells of epithelial origin.";
RL Biochem. J. 356:705-718(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: May hydrolyze collagen type IV, fibronectin, fibrinogen,
CC beta-casein, type I gelatin and alpha-1 proteinase inhibitor. Is also
CC able to activate progelatinase B.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Expressed specifically in uterus and placenta. Is
CC also widely expressed in malignant tumors from different sources as
CC well as in diverse tumor cell lines.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MMP26ID41403ch11p15.html";
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DR EMBL; AF230354; AAF80180.1; -; mRNA.
DR EMBL; AJ251531; CAC08821.1; -; mRNA.
DR EMBL; AF248646; AAF82359.1; -; mRNA.
DR EMBL; AF291664; AAG00603.1; -; mRNA.
DR EMBL; AF291665; AAG02470.1; -; Genomic_DNA.
DR EMBL; BC101541; AAI01542.1; -; mRNA.
DR EMBL; BC101543; AAI01544.1; -; mRNA.
DR CCDS; CCDS7752.1; -.
DR RefSeq; NP_068573.2; NM_021801.4.
DR AlphaFoldDB; Q9NRE1; -.
DR SMR; Q9NRE1; -.
DR BioGRID; 121151; 88.
DR IntAct; Q9NRE1; 14.
DR STRING; 9606.ENSP00000369753; -.
DR BindingDB; Q9NRE1; -.
DR ChEMBL; CHEMBL4707; -.
DR DrugBank; DB00786; Marimastat.
DR GuidetoPHARMACOLOGY; 1648; -.
DR MEROPS; M10.029; -.
DR GlyGen; Q9NRE1; 2 sites.
DR iPTMnet; Q9NRE1; -.
DR PhosphoSitePlus; Q9NRE1; -.
DR BioMuta; MMP26; -.
DR DMDM; 13629493; -.
DR MassIVE; Q9NRE1; -.
DR PaxDb; Q9NRE1; -.
DR PeptideAtlas; Q9NRE1; -.
DR PRIDE; Q9NRE1; -.
DR ProteomicsDB; 82343; -.
DR Antibodypedia; 10919; 196 antibodies from 30 providers.
DR DNASU; 56547; -.
DR Ensembl; ENST00000380390.6; ENSP00000369753.1; ENSG00000167346.9.
DR Ensembl; ENST00000690848.1; ENSP00000510347.1; ENSG00000167346.9.
DR GeneID; 56547; -.
DR KEGG; hsa:56547; -.
DR MANE-Select; ENST00000380390.6; ENSP00000369753.1; NM_021801.5; NP_068573.2.
DR UCSC; uc001lzv.4; human.
DR CTD; 56547; -.
DR DisGeNET; 56547; -.
DR GeneCards; MMP26; -.
DR HGNC; HGNC:14249; MMP26.
DR HPA; ENSG00000167346; Tissue enriched (endometrium).
DR MIM; 605470; gene.
DR neXtProt; NX_Q9NRE1; -.
DR OpenTargets; ENSG00000167346; -.
DR PharmGKB; PA30883; -.
DR VEuPathDB; HostDB:ENSG00000167346; -.
DR eggNOG; KOG1565; Eukaryota.
DR GeneTree; ENSGT00940000163719; -.
DR HOGENOM; CLU_015489_4_1_1; -.
DR InParanoid; Q9NRE1; -.
DR OMA; WCLALPV; -.
DR OrthoDB; 1075463at2759; -.
DR PhylomeDB; Q9NRE1; -.
DR TreeFam; TF315428; -.
DR BRENDA; 3.4.24.B7; 2681.
DR PathwayCommons; Q9NRE1; -.
DR SignaLink; Q9NRE1; -.
DR BioGRID-ORCS; 56547; 11 hits in 1068 CRISPR screens.
DR GeneWiki; MMP26; -.
DR GenomeRNAi; 56547; -.
DR Pharos; Q9NRE1; Tchem.
DR PRO; PR:Q9NRE1; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NRE1; protein.
DR Bgee; ENSG00000167346; Expressed in buccal mucosa cell and 31 other tissues.
DR Genevisible; Q9NRE1; HS.
DR GO; GO:0031012; C:extracellular matrix; NAS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030574; P:collagen catabolic process; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:CACAO.
DR GO; GO:0006508; P:proteolysis; NAS:UniProtKB.
DR CDD; cd04278; ZnMc_MMP; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR033739; M10A_MMP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR028736; MMP26.
DR InterPro; IPR001818; Pept_M10_metallopeptidase.
DR InterPro; IPR021190; Pept_M10A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10201:SF76; PTHR10201:SF76; 1.
DR Pfam; PF00413; Peptidase_M10; 1.
DR PRINTS; PR00138; MATRIXIN.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Collagen degradation; Extracellular matrix; Glycoprotein;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..89
FT /evidence="ECO:0000250"
FT /id="PRO_0000028855"
FT CHAIN 90..261
FT /note="Matrix metalloproteinase-26"
FT /id="PRO_0000028856"
FT MOTIF 80..87
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT ACT_SITE 209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 43
FT /note="K -> E (in dbSNP:rs2499953)"
FT /evidence="ECO:0000269|PubMed:10801841,
FT ECO:0000269|PubMed:11389678"
FT /id="VAR_033489"
FT VARIANT 260
FT /note="I -> M (in dbSNP:rs16908114)"
FT /id="VAR_033490"
FT CONFLICT 71
FT /note="M -> I (in Ref. 1; AAF80180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 29708 MW; A66D0DBE3ED7DE76 CRC64;
MQLVILRVTI FLPWCFAVPV PPAADHKGWD FVEGYFHQFF LTKKESPLLT QETQTQLLQQ
FHRNGTDLLD MQMHALLHQP HCGVPDGSDT SISPGRCKWN KHTLTYRIIN YPHDMKPSAV
KDSIYNAVSI WSNVTPLIFQ QVQNGDADIK VSFWQWAHED GWPFDGPGGI LGHAFLPNSG
NPGVVHFDKN EHWSASDTGY NLFLVATHEI GHSLGLQHSG NQSSIMYPTY WYHDPRTFQL
SADDIQRIQH LYGEKCSSDI P
