SUMF1
| Sulfatase modifying factor 1 |
PDB rendering based on 1y1e. |
| Available structures |
| PDB |
1Y1E, 1Y1F, 1Y1G, 1Y1H, 1Y1I, 1Y1J, 1Z70, 2AFT, 2AFY, 2AII, 2AIJ, 2AIK, 2HI8, 2HIB |
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| Identifiers |
| Symbols |
SUMF1; AAPA3037; FGE; MGC131853; MGC150436 |
| External IDs |
OMIM: 607939 MGI: 1889844 HomoloGene: 16268 GeneCards: SUMF1 Gene |
| EC number |
1.13.-.- |
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| Orthologs |
| Species |
Human |
Mouse |
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| Entrez |
285362 |
58911 |
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| Ensembl |
ENSG00000144455 |
ENSMUSG00000030101 |
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| UniProt |
Q8NBK3 |
Q3TTT6 |
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| RefSeq (mRNA) |
NM_001164674.1 |
NM_145937.3 |
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| RefSeq (protein) |
NP_001158146.1 |
NP_666049.2 |
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| Location (UCSC) |
Chr 3:
3.74 – 4.51 Mb |
Chr 6:
108.06 – 108.14 Mb |
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| PubMed search |
[1] |
[2] |
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Sulfatase-modifying factor 1 is an enzyme that in humans is encoded by the SUMF1 gene.[1][2][3]
Sulfatases catalyze the hydrolysis of sulfate esters such as glycosaminoglycans, sulfolipids, and steroid sulfates. C-alpha-formylglycine (FGly), the catalytic residue in the active site of eukaryotic sulfatases, is posttranslationally generated from a cysteine by SUMF1, the FGly-generating enzyme (FGE), in the endoplasmic reticulum (ER). The genetic defect of FGly formation caused by mutations in the SUMF1 gene results in multiple sulfatase deficiency (MSD; MIM 272200), a lysosomal storage disorder (Roeser et al., 2006).[supplied by OMIM][3]
References
- ^ Dierks T, Schmidt B, Borissenko LV, Peng J, Preusser A, Mariappan M, von Figura K (May 2003). "Multiple sulfatase deficiency is caused by mutations in the gene encoding the human C(alpha)-formylglycine generating enzyme". Cell 113 (4): 435–44. doi:10.1016/S0092-8674(03)00347-7. PMID 12757705.
- ^ Cosma MP, Pepe S, Annunziata I, Newbold RF, Grompe M, Parenti G, Ballabio A (May 2003). "The multiple sulfatase deficiency gene encodes an essential and limiting factor for the activity of sulfatases". Cell 113 (4): 445–56. doi:10.1016/S0092-8674(03)00348-9. PMID 12757706.
- ^ a b "Entrez Gene: SUMF1 sulfatase modifying factor 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=285362.
Further reading
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Clark HF, Gurney AL, Abaya E, et al. (2003). "The Secreted Protein Discovery Initiative (SPDI), a Large-Scale Effort to Identify Novel Human Secreted and Transmembrane Proteins: A Bioinformatics Assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=403697.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Cosma MP, Pepe S, Parenti G, et al. (2004). "Molecular and functional analysis of SUMF1 mutations in multiple sulfatase deficiency". Hum. Mutat. 23 (6): 576–81. doi:10.1002/humu.20040. PMID 15146462.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Preusser-Kunze A, Mariappan M, Schmidt B, et al. (2005). "Molecular characterization of the human Calpha-formylglycine-generating enzyme". J. Biol. Chem. 280 (15): 14900–10. doi:10.1074/jbc.M413383200. PMID 15657036.
- Dierks T, Dickmanns A, Preusser-Kunze A, et al. (2005). "Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme". Cell 121 (4): 541–52. doi:10.1016/j.cell.2005.03.001. PMID 15907468.
- Zito E, Fraldi A, Pepe S, et al. (2005). "Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2". EMBO Rep. 6 (7): 655–60. doi:10.1038/sj.embor.7400454. PMC 1369113. PMID 15962010. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1369113.
- Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
- Roeser D, Preusser-Kunze A, Schmidt B, et al. (2006). "A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme". Proc. Natl. Acad. Sci. U.S.A. 103 (1): 81–6. doi:10.1073/pnas.0507592102. PMC 1324989. PMID 16368756. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1324989.
- Fraldi A, Biffi A, Lombardi A, et al. (2007). "SUMF1 enhances sulfatase activities in vivo in five sulfatase deficiencies". Biochem. J. 403 (2): 305–12. doi:10.1042/BJ20061783. PMC 1874239. PMID 17206939. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1874239.
- Zito E, Buono M, Pepe S, et al. (2007). "Sulfatase modifying factor 1 trafficking through the cells: from endoplasmic reticulum to the endoplasmic reticulum". EMBO J. 26 (10): 2443–53. doi:10.1038/sj.emboj.7601695. PMC 1868907. PMID 17446859. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1868907.
- Annunziata I, Bouchè V, Lombardi A, et al. (2007). "Multiple sulfatase deficiency is due to hypomorphic mutations of the SUMF1 gene". Hum. Mutat. 28 (9): 928. doi:10.1002/humu.9504. PMID 17657823.
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PDB gallery
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1y1e: human formylglycine generating enzyme
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1y1f: human formylglycine generating enzyme with cysteine sulfenic acid
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1y1g: human formylglycine generating enzyme, double sulfonic acid form
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1y1h: human formylglycine generating enzyme, oxidised Cys refined as hydroperoxide
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1y1i: hyuman formylglycine generating enzyme, reduced form
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1y1j: human formylglycine generating enzyme, sulfonic acid/desulfurated form
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1z70: 1.15A resolution structure of the formylglycine generating enzyme FGE
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2aft: Formylglycine generating enzyme C336S mutant
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2afy: Formylglycine generating enzyme C341S mutant
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2aii: wild-type Formylglycine generating enzyme reacted with iodoacetamide
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2aij: Formylglycine generating enzyme C336S mutant covalently bound to substrate peptide CTPSR
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2aik: Formylglycine generating enzyme C336S mutant covalently bound to substrate peptide LCTPSRA
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2hi8: human formylglycine generating enzyme, C336S mutant, bromide co-crystallization
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2hib: human formylglycine generating enzyme, C336S mutant, iodide co-crystallization
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| Sphingolipid |
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| NCL |
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| Ceramide synthesis |
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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