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Enzyme Name | UniProtKB | KEGG |
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| P32906 |
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Protein name | Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase | mannosyl-oligosaccharide 1,2-alpha-mannosidasemannosidase 1Amannosidase 1B1,2-alpha-mannosidaseexo-alpha-1,2-mannanasemannose-9 processing alpha-mannosidaseglycoprotein processing mannosidase Imannosidase IMan9-mannosidaseManI1,2-alpha-mannosyl-oligosaccharide alpha-D-mannohydrolase |
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Synonyms | EC 3.2.1.113ER alpha-1,2-mannosidaseMan(9)-alpha-mannosidase |
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RefSeq | NP_012665.3 (Protein) NM_001181789.3 (DNA/RNA sequence)
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Pfam | PF01532 (Glyco_hydro_47) [Graphical view]
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CAZy | GH47 (Glycoside Hydrolase Family)
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KEGG pathways | MAP code | Pathways |
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MAP00510 | N-Glycan biosynthesis | MAP00513 | High-mannose type N-glycan biosynthesis | MAP01030 | Glycan structures - biosynthesis 1 |
UniProtKB:Accession Number | P32906 |
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Entry name | MNS1_YEAST |
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Activity | Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2). |
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Subunit |
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Subcellular location | Endoplasmic reticulum membrane, Single-pass type II membrane protein. |
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Cofactor | Calcium. |
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Active-site residues | resource |
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literature [11], [15] | pdb | Catalytic residues | Cofactor-binding residues |
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| | | | | | | | | |
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1dl2A |  |  |  |  |  |  |  | GLU 132;ASP 275;GLU 435
| THR 525(Calcium binding)
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1g6iA |  |  |  |  |  |  |  | GLU 132;ASP 275;GLU 435
| THR 525(Calcium binding)
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[10] | p.585-586 |
| [15] | Fig.5, p.32 |
| [16] | Fig.9, p.132 |
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references | [1] |
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PubMed ID | 7945271 |
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Journal | Biochem J |
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Year | 1994 |
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Volume | 303 |
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Pages | 97-103 |
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Authors | Yoshida T, Maeda K, Kobayashi M, Ichishima E |
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Title | Chemical modification of Penicillium 1,2-alpha-D-mannosidase by water-soluble carbodi-imide: identification of a catalytically important aspartic acid residue. |
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[2] |
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PubMed ID | 7726853 |
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Journal | Biochem Biophys Res Commun |
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Year | 1995 |
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Volume | 209 |
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Pages | 322-6 |
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Authors | Lipari F, Gour-Salin BJ, Herscovics A |
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Title | The Saccharomyces cerevisiae processing alpha 1,2-mannosidase is an inverting glycosidase. |
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[3] |
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PubMed ID | 8724134 |
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Journal | Glycobiology |
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Year | 1996 |
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Volume | 6 |
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Pages | 265-70 |
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Authors | Scaman CH, Lipari F, Herscovics A |
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Title | A spectrophotometric assay for alpha-mannosidase activity. |
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[4] |
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PubMed ID | 8910350 |
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Journal | J Biol Chem |
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Year | 1996 |
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Volume | 271 |
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Pages | 27615-22 |
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Authors | Lipari F, Herscovics A |
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Title | Role of the cysteine residues in the alpha1,2-mannosidase involved in N-glycan biosynthesis in Saccharomyces cerevisiae. The conserved Cys340 and Cys385 residues form an essential disulfide bond. |
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[5] |
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PubMed ID | 9325167 |
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Journal | Biochem Biophys Res Commun |
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Year | 1997 |
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Volume | 238 |
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Pages | 779-83 |
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Authors | Fujita A, Yoshida T, Ichishima E |
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Title | Five crucial carboxyl residues of 1,2-alpha-mannosidase from Aspergillus saitoi (A. phoenicis), a food microorganism, are identified by site-directed mutagenesis. |
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[6] |
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PubMed ID | 9356293 |
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Journal | J Struct Biol |
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Year | 1997 |
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Volume | 120 |
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Pages | 69-72 |
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Authors | Dole K, Lipari F, Herscovics A, Howell PL |
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Title | Crystallization and preliminary X-ray analysis of the class 1 alpha 1,2-mannosidase from Saccharomyces cerevisiae. |
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[7] |
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PubMed ID | 9894008 |
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Journal | Biochemistry |
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Year | 1999 |
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Volume | 38 |
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Pages | 1111-8 |
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Authors | Lipari F, Herscovics A |
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Title | Calcium binding to the class I alpha-1,2-mannosidase from Saccharomyces cerevisiae occurs outside the EF hand motif. |
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[8] |
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PubMed ID | 10521544 |
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Journal | Glycobiology |
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Year | 1999 |
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Volume | 9 |
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Pages | 1073-8 |
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Authors | Tremblay LO, Herscovics A |
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Title | Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. |
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[9] |
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PubMed ID | 10830477 |
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Journal | Biosci Biotechnol Biochem |
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Year | 2000 |
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Volume | 64 |
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Pages | 675-88 |
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Authors | Ichishima E |
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Title | Unique catalytic and molecular properties of hydrolases from Aspergillus used in Japanese bioindustries. |
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[10] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 34-549. |
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Medline ID | 20141183 |
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PubMed ID | 10675327 |
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Journal | EMBO J |
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Year | 2000 |
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Volume | 19 |
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Pages | 581-8 |
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Authors | Vallee F, Lipari F, Yip P, Sleno B, Herscovics A, Howell PL |
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Title | Crystal structure of a class I alpha1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control. |
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Related PDB | 1dl2 |
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Related UniProtKB | P32906 |
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[11] |
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PubMed ID | 10753911 |
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Journal | J Biol Chem |
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Year | 2000 |
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Volume | 275 |
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Pages | 11071-4 |
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Authors | Romero PA, Vallee F, Howell PL, Herscovics A |
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Title | Mutation of Arg(273) to Leu alters the specificity of the yeast N-glycan processing class I alpha1,2-mannosidase. |
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[12] |
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PubMed ID | 11673242 |
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Journal | Bioinformatics |
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Year | 2001 |
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Volume | 17 |
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Pages | 965-76 |
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Authors | Jordan IK, Bishop GR, Gonzalez DS |
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Title | Sequence and structural aspects of functional diversification in class I alpha-mannosidase evolution. |
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[13] |
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PubMed ID | 11792827 |
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Journal | J Cell Sci |
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Year | 2001 |
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Volume | 114 |
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Pages | 4629-35 |
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Authors | Massaad MJ, Herscovics A |
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Title | Interaction of the endoplasmic reticulum alpha 1,2-mannosidase Mns1p with Rer1p using the split-ubiquitin system. |
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[14] |
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PubMed ID | 11545593 |
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Journal | J Mol Biol |
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Year | 2001 |
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Volume | 312 |
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Pages | 157-65 |
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Authors | Van Petegem F, Contreras H, Contreras R, Van Beeumen J |
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Title | Trichoderma reesei alpha-1,2-mannosidase: structural basis for the cleavage of four consecutive mannose residues. |
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[15] |
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Comments | X-ray crystallography (ISBN:085404826x) |
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Journal | Carbohydrate Bioengineering |
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Year | 2002 |
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Volume |
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Pages | 28-33 |
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Authors | Herscovics A, Lipari F, Sleno B, Romera PA, Vallee F, Yip P, Howell PA |
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Title | Structure and Function of Class I A1,2-Mannosidases Involved in Glycoprotein Biosynthesis. |
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Related PDB | 1g6i |
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[16] |
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PubMed ID | 12211022 |
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Journal | Proteins |
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Year | 2002 |
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Volume | 49 |
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Pages | 125-34 |
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Authors | Mulakala C, Reilly PJ |
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Title | Understanding protein structure-function relationships in Family 47 alpha-1,2-mannosidases through computational docking of ligands. |
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[17] |
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PubMed ID | 12702721 |
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Journal | J Biol Chem |
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Year | 2003 |
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Volume | 278 |
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Pages | 25289-94 |
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Authors | Tatara Y, Lee BR, Yoshida T, Takahashi K, Ichishima E |
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Title | Identification of catalytic residues of Ca2+-independent 1,2-alpha-D-mannosidase from Aspergillus saitoi by site-directed mutagenesis. |
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comments | This enzyme belongs to the glycosyl hydrolase family-47, with an inverting mechanism (see [2]). Class I alpha-1,2-alpha-mannosidase (glycosylhydrolase family 47) includes 2 subgroups, Endoplasmic Reticulum subgroup and Golgi subgroup. This entry is for ER subgroup from yeast. Another ER subgroup enzyme from human is included in D00470. According to the literature [10], [15] & [16], the catalytic mechanism must be similar to that of the human counterpart (D00470 in EzCatDB). (1) Glu435 acts as a general base, to activate a water molecule. The water is also bound to the Ca2+. (2) The activated water makes a nucleophilic attack on the C1 atom of Man10. (3) Glu330 acts as a general acid, to protonate leaving O2 atom of Man7, through a water.
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created | updated |
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2004-08-28 | 2014-07-09 |
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