NFS1_MOUSE
ID NFS1_MOUSE Reviewed; 459 AA.
AC Q9Z1J3; Q8C6I5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Cysteine desulfurase, mitochondrial {ECO:0000305};
DE Short=m-Nfs1 {ECO:0000303|PubMed:9738949};
DE EC=2.8.1.7 {ECO:0000250|UniProtKB:P0A6B9};
DE Flags: Precursor;
GN Name=Nfs1 {ECO:0000303|PubMed:9738949, ECO:0000312|MGI:MGI:1316706};
GN Synonyms=Nifs;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Olfactory epithelium;
RX PubMed=9738949; DOI=10.1016/s0014-5793(98)00897-7;
RA Nakai Y., Yoshihara Y., Hayashi H., Kagamiyama H.;
RT "cDNA cloning and characterization of mouse nifS-like protein, m-Nfs1:
RT mitochondrial localization of eukaryotic NifS-like proteins.";
RL FEBS Lett. 433:143-148(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, Pancreas, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to
CC produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-
CC S) clusters. May be involved in the biosynthesis of molybdenum
CC cofactor. {ECO:0000250|UniProtKB:Q9Y697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000250|UniProtKB:Q9Y697};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P0A6B9};
CC -!- SUBUNIT: Binds ISCU/NIFUN. Forms a complex with LYRM4. Interacts with
CC HSPA9. {ECO:0000250|UniProtKB:Q9Y697}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9738949}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9Y697}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y697}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9738949}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR EMBL; AJ222660; CAA10916.1; -; mRNA.
DR EMBL; AK075575; BAC35831.1; -; mRNA.
DR EMBL; AK132838; BAE21386.1; -; mRNA.
DR EMBL; AK148527; BAE28601.1; -; mRNA.
DR EMBL; AK159828; BAE35407.1; -; mRNA.
DR EMBL; AL833786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX649640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL06179.1; -; Genomic_DNA.
DR CCDS; CCDS16962.1; -.
DR RefSeq; NP_035041.2; NM_010911.2.
DR AlphaFoldDB; Q9Z1J3; -.
DR SMR; Q9Z1J3; -.
DR BioGRID; 201759; 4.
DR ComplexPortal; CPX-5823; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR CORUM; Q9Z1J3; -.
DR IntAct; Q9Z1J3; 1.
DR STRING; 10090.ENSMUSP00000029147; -.
DR iPTMnet; Q9Z1J3; -.
DR PhosphoSitePlus; Q9Z1J3; -.
DR REPRODUCTION-2DPAGE; Q9Z1J3; -.
DR EPD; Q9Z1J3; -.
DR jPOST; Q9Z1J3; -.
DR MaxQB; Q9Z1J3; -.
DR PaxDb; Q9Z1J3; -.
DR PeptideAtlas; Q9Z1J3; -.
DR PRIDE; Q9Z1J3; -.
DR ProteomicsDB; 252819; -.
DR Antibodypedia; 35035; 233 antibodies from 26 providers.
DR DNASU; 18041; -.
DR Ensembl; ENSMUST00000029147; ENSMUSP00000029147; ENSMUSG00000027618.
DR GeneID; 18041; -.
DR KEGG; mmu:18041; -.
DR UCSC; uc008nmj.2; mouse.
DR CTD; 9054; -.
DR MGI; MGI:1316706; Nfs1.
DR VEuPathDB; HostDB:ENSMUSG00000027618; -.
DR eggNOG; KOG1549; Eukaryota.
DR GeneTree; ENSGT00940000155740; -.
DR HOGENOM; CLU_003433_0_2_1; -.
DR InParanoid; Q9Z1J3; -.
DR OMA; KGLYWAR; -.
DR OrthoDB; 664730at2759; -.
DR PhylomeDB; Q9Z1J3; -.
DR TreeFam; TF105658; -.
DR BRENDA; 2.8.1.7; 3474.
DR Reactome; R-MMU-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR Reactome; R-MMU-947581; Molybdenum cofactor biosynthesis.
DR BioGRID-ORCS; 18041; 26 hits in 77 CRISPR screens.
DR ChiTaRS; Nfs1; mouse.
DR PRO; PR:Q9Z1J3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z1J3; protein.
DR Bgee; ENSMUSG00000027618; Expressed in right kidney and 266 other tissues.
DR ExpressionAtlas; Q9Z1J3; baseline and differential.
DR Genevisible; Q9Z1J3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0031071; F:cysteine desulfurase activity; ISO:MGI.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IDA:HGNC-UCL.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR010240; Cys_deSase_IscS.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR02006; IscS; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW Molybdenum cofactor biosynthesis; Nucleus; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..459
FT /note="Cysteine desulfurase, mitochondrial"
FT /id="PRO_0000001294"
FT ACT_SITE 383
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT BINDING 129..130
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 209
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 257..259
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 297
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 383
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared with ISCU"
FT /note="via persulfide group"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT MOD_RES 260
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT CONFLICT 221
FT /note="G -> R (in Ref. 1; CAA10916)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="N -> K (in Ref. 1; CAA10916)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="L -> F (in Ref. 1; CAA10916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 50570 MW; 986D636C5506C7B0 CRC64;
MVGSVAGNML LRAAWRRASL AATSLALGRS SVPTRGLRLR VVDHGPHSPV HSEAEAVLRP
LYMDVQATTP LDPRVLDAML PYLVNYYGNP HSRTHAYGWE SEAAMERARQ QVASLIGADP
REIIFTSGAT ESNNIAIKGV ARFYRSRKKH LVTTQTEHKC VLDSCRSLEA EGFRVTYLPV
QKSGIIDLKE LEAAIQPDTS LVSVMTVNNE IGVKQPIAEI GQICSSRKVY FHTDAAQAVG
KIPLDVNDMK IDLMSISGHK LYGPKGVGAI YIRRRPRVRV EALQSGGGQE RGMRSGTVPT
PLVVGLGAAC ELAQQEMEYD HKRISKLAER LVQNIMKNLP DVVMNGDPKQ HYPGCINLSF
AYVEGESLLM ALKDVALSSG SACTSASLEP SYVLRAIGTD EDLAHSSIRF GIGRFTTEEE
VDYTAEKCIH HVKRLREMSP LWEMVQDGID LKSIKWTQH
