NFS1

NFS1
Identifiers
Aliases	NFS1, IscS, NIFS, HUSSY-08, NFS1 cysteine desulfurase, cysteine desulfurase, COXPD52
External IDs	OMIM: 603485; MGI: 1316706; GeneCards: NFS1
Enzyme activity
Gene location (Human)
Chr.	Chromosome 20 (human)
End	35,699,355 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	155,986,106 bp
RNA expression pattern
	Top expressed in
	right adrenal cortex; ; left adrenal gland; ; left adrenal cortex; ; right lobe of liver; ; apex of heart; ; right testis; ; left testis; ; mucosa of transverse colon; ; right frontal lobe; ; anterior cingulate cortex;
	Top expressed in
	right kidney; ; sternocleidomastoid muscle; ; digastric muscle; ; temporal muscle; ; triceps brachii muscle; ; muscle of thigh; ; saccule; ; human kidney; ; otic placode; ; proximal tubule;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; protein homodimerization activity; iron-sulfur cluster binding; metal ion binding; protein binding; catalytic activity; pyridoxal phosphate binding; cysteine desulfurase activity;
Cellular component	cytosol; nucleoplasm; nucleus; cytoplasm; mitochondrion; mitochondrial matrix;
Biological process	molybdopterin cofactor biosynthetic process; [2Fe-2S cluster assembly]; Mo-molybdopterin cofactor biosynthetic process; sulfur amino acid metabolic process; small molecule metabolic process; iron incorporation into metallo-sulfur cluster; protein-containing complex assembly; iron-sulfur cluster assembly;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	9054
	18041
	ENSG00000244005
	ENSMUSG00000027618
	Q9Y697
	Q9Z1J3
	NM_001198989; NM_021100; NM_181679
	NM_010911
	NP_001185918; NP_066923
	NP_035041
	Wikidata
View/Edit Human	View/Edit Mouse

Cysteine desulfurase, mitochondrial is an enzyme that in humans is encoded by the NFS1 gene.^[5]^[6]^[7]

Iron-sulfur clusters are required for the function of many cellular enzymes. The protein encoded by this gene supplies inorganic sulfur to these clusters by removing the sulfur from cysteine, creating alanine and a protein-bound hydropersulfide in the process. The terminal sulfur atom of the hydropersulfide is transferred to the iron-sulfur cluster scaffold protein ISCU, mediated by the accessory protein frataxin.^[8]

This gene uses alternate in-frame translation initiation sites to generate mitochondrial forms and cytoplasmic/nuclear forms. Selection of the alternative initiation sites is determined by the cytosolic pH. The encoded protein belongs to the class-V family of pyridoxal phosphate-dependent aminotransferases.^[7]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000244005 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027618 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Land T, Rouault TA (Jan 1999). "Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization". Mol Cell. 2 (6): 807–15. doi:10.1016/S1097-2765(00)80295-6. PMID 9885568.
↑ Biederbick A, Stehling O, Rosser R, Niggemeyer B, Nakai Y, Elsasser HP, Lill R (Jul 2006). "Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation". Mol Cell Biol. 26 (15): 5675–87. doi:10.1128/MCB.00112-06. PMC 1592756. PMID 16847322.
1 2 "Entrez Gene: NFS1 NFS1 nitrogen fixation 1 homolog (S. cerevisiae)".
↑ Maio, Nunziata; Jain, Anshika; Rouault, Tracey A. (2020-01-06). "Mammalian iron-sulfur cluster biogenesis: Recent insights into the roles of frataxin, acyl carrier protein and ATPase-mediated transfer to recipient proteins". Current Opinion in Chemical Biology. 55: 34–44. doi:10.1016/j.cbpa.2019.11.014. ISSN 1879-0402. PMC 7237328. PMID 31918395.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Tong WH, Rouault T (2000). "Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells". EMBO J. 19 (21): 5692–700. doi:10.1093/emboj/19.21.5692. PMC 305809. PMID 11060020.
Stanchi F, Bertocco E, Toppo S, et al. (2001). "Characterization of 16 novel human genes showing high similarity to yeast sequences". Yeast. 18 (1): 69–80. doi:10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H. PMID 11124703. S2CID 21397515.
Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
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.
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.
Li K, Tong WH, Hughes RM, Rouault TA (2006). "Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly". J. Biol. Chem. 281 (18): 12344–51. doi:10.1074/jbc.M600582200. PMID 16527810.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000244005 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027618 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9885568-5] Land T, Rouault TA (Jan 1999). "Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization". Mol Cell. 2 (6): 807–15. doi:10.1016/S1097-2765(00)80295-6. PMID 9885568.

[pmid16847322-6] Biederbick A, Stehling O, Rosser R, Niggemeyer B, Nakai Y, Elsasser HP, Lill R (Jul 2006). "Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation". Mol Cell Biol. 26 (15): 5675–87. doi:10.1128/MCB.00112-06. PMC 1592756. PMID 16847322.

[entrez-7] 1 2 "Entrez Gene: NFS1 NFS1 nitrogen fixation 1 homolog (S. cerevisiae)".

[8] Maio, Nunziata; Jain, Anshika; Rouault, Tracey A. (2020-01-06). "Mammalian iron-sulfur cluster biogenesis: Recent insights into the roles of frataxin, acyl carrier protein and ATPase-mediated transfer to recipient proteins". Current Opinion in Chemical Biology. 55: 34–44. doi:10.1016/j.cbpa.2019.11.014. ISSN 1879-0402. PMC 7237328. PMID 31918395.

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References

Further reading