SUMF1

Available structures

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

MGI: 1889844 HomoloGene: 16268 GeneCards: SUMF1

Genetically Related Diseases

multiple sclerosis^[1]

Gene ontology
Molecular function	• protein homodimerization activity • metal ion binding • oxidoreductase activity
Cellular component	• endoplasmic reticulum lumen • endoplasmic reticulum
Biological process	• post-translational protein modification • oxidation-reduction process • 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_001158146.1 NP_001158147.1 NP_877437.2


NP_666049.2

Location (UCSC)

Chr 3: 3.7 – 4.47 Mb

Chr 6: 108.11 – 108.19 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Sulfatase-modifying factor 1 is an enzyme that in humans is encoded by the SUMF1 gene.^[4]^[5]^[6]

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]^[6]

References

↑ "Diseases that are genetically associated with SUMF1 view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "Entrez Gene: SUMF1 sulfatase modifying factor 1".

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.
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.
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.
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.
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.
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.
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.
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.

PDB gallery

1y1e: human formylglycine generating enzyme

1y1f: human formylglycine generating enzyme with cysteine sulfenic acid

1y1g: human formylglycine generating enzyme, double sulfonic acid form

1y1h: human formylglycine generating enzyme, oxidised Cys refined as hydroperoxide

1y1i: hyuman formylglycine generating enzyme, reduced form

1y1j: human formylglycine generating enzyme, sulfonic acid/desulfurated form

1z70: 1.15A resolution structure of the formylglycine generating enzyme FGE

2aft: Formylglycine generating enzyme C336S mutant

2afy: Formylglycine generating enzyme C341S mutant

2aii: wild-type Formylglycine generating enzyme reacted with iodoacetamide

2aij: Formylglycine generating enzyme C336S mutant covalently bound to substrate peptide CTPSR

2aik: Formylglycine generating enzyme C336S mutant covalently bound to substrate peptide LCTPSRA

2hi8: human formylglycine generating enzyme, C336S mutant, bromide co-crystallization

2hib: human formylglycine generating enzyme, C336S mutant, iodide co-crystallization

Metabolism, lipid metabolism, glycolipid enzymes

Sphingolipid

To glycosphingolipid	Glycosyltransferase Sulfotransferase

To ceramide	From ganglioside Beta-galactosidase Hexosaminidase A Neuraminidase Glucocerebrosidase From globoside Hexosaminidase B Alpha-galactosidase Beta-galactosidase Glucocerebrosidase From sphingomyelin Sphingomyelin phosphodiesterase Sphingomyelin phosphodiesterase 1 From sulfatide Arylsulfatase A Galactosylceramidase

To sphingosine	Ceramidase ACER1 ACER2 ACER3 ASAH1 ASAH2 ASAH2B ASAH2C

Other	Sphingosine kinase

NCL

Ceramide synthesis

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SUMF1

References

Further reading