SUMF1

SUMF1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1Y1E, 1Y1F, 1Y1G, 1Y1H, 1Y1I, 1Y1J, 1Z70, 2AFT, 2AFY, 2AII, 2AIJ, 2AIK, 2HI8, 2HIB
Identifiers
Aliases	SUMF1, AAPA3037, FGE, UNQ3037, sulfatase modifying factor 1
External IDs	OMIM: 607939 MGI: 1889844 HomoloGene: 16268 GeneCards: SUMF1
Gene location (Human) Chr. Chromosome 3 (human) Band 3p26.1 Start 3,700,814 bp End 4,467,273 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6|6 E1 Start 108,083,989 bp End 108,162,543 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in renal medulla synovial membrane synovial joint tibia human penis nipple stromal cell of endometrium pylorus bronchial epithelial cell urethra Top expressed in ascending aorta aortic valve conjunctival fornix iris supraoptic nucleus cumulus cell stria vascularis median eminence external carotid artery internal carotid artery More reference expression data BioGPS n/a
Gene ontology Molecular function protein homodimerization activity metal ion binding oxidoreductase activity Formylglycine-generating oxidase activity cupric ion binding Cellular component endoplasmic reticulum lumen endoplasmic reticulum Biological process post-translational protein modification glycosphingolipid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 285362 58911 Ensembl ENSG00000144455 ENSMUSG00000030101 UniProt Q8NBK3 Q8R0F3 RefSeq (mRNA) NM_001164674 NM_001164675 NM_182760 NM_145937 RefSeq (protein) NP_001158146 NP_001158147 NP_877437 NP_666049 Location (UCSC) Chr 3: 3.7 – 4.47 Mb Chr 6: 108.08 – 108.16 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Sulfatase-modifying factor 1 is an enzyme that in humans is encoded by the SUMF1 gene.

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 human form of the aerobic Formylglycine-generating enzyme (FGE), in the endoplasmic reticulum (ER). The genetic defect of FGly formation caused by mutations in the SUMF1 gene results in inactive FGE, and subsequently multiple sulfatase deficiency (MSD; MIM 272200), a lysosomal storage disorder (Roeser et al., 2006).[supplied by OMIM]

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): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• 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): 2265–2270. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. 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): 576–581. doi:10.1002/humu.20040. PMID 15146462. S2CID 44637380.
• 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): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Preusser-Kunze A, Mariappan M, Schmidt B, et al. (2005). "Molecular characterization of the human Calpha-formylglycine-generating enzyme". J. Biol. Chem. 280 (15): 14900–14910. 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" (PDF). Cell. 121 (4): 541–552. doi:10.1016/j.cell.2005.03.001. PMID 15907468. S2CID 2956795.
• 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): 655–660. doi:10.1038/sj.embor.7400454. PMC 1369113. PMID 15962010.
• 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): 117–126. 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): 81–86. Bibcode:2006PNAS..103...81R. doi:10.1073/pnas.0507592102. PMC 1324989. PMID 16368756.
• Fraldi A, Biffi A, Lombardi A, et al. (2007). "SUMF1 enhances sulfatase activities in vivo in five sulfatase deficiencies". Biochem. J. 403 (2): 305–312. doi:10.1042/BJ20061783. PMC 1874239. PMID 17206939.
• 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): 2443–2453. doi:10.1038/sj.emboj.7601695. PMC 1868907. PMID 17446859.
• 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. S2CID 8500605.