ADX_MOUSE
ID ADX_MOUSE Reviewed; 188 AA.
AC P46656;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Adrenodoxin, mitochondrial;
DE AltName: Full=Adrenal ferredoxin;
DE AltName: Full=Ferredoxin-1;
DE Flags: Precursor;
GN Name=Fdx1;
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].
RC TISSUE=Adrenal gland;
RX PubMed=7893748; DOI=10.1016/0167-4781(95)00003-y;
RA Stromstedt M., Waterman M.R.;
RT "A full-length cDNA encoding mouse adrenodoxin.";
RL Biochim. Biophys. Acta 1261:126-128(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=7640310; DOI=10.1016/0167-4781(95)00102-m;
RA Itoh S., Iemura O., Yamada E., Yoshimura T., Tsujikawa K., Kohama Y.,
RA Mimura T.;
RT "Mouse cytochrome P-450 linked ferredoxin: its cDNA cloning and
RT inducibility by dibutyryladenosine 3',5'-cyclic monophosphate and
RT forskolin.";
RL Biochim. Biophys. Acta 1263:173-175(1995).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, 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).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-162, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Essential for the synthesis of various steroid hormones,
CC participates in the reduction of mitochondrial cytochrome P450 for
CC steroidogenesis. Transfers electrons from adrenodoxin reductase to
CC CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain
CC cleavage. Does not form a ternary complex with adrenodoxin reductase
CC and CYP11A1 but shuttles between the two enzymes to transfer electrons.
CC {ECO:0000250|UniProtKB:P00257}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P10109};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:P10109};
CC -!- SUBUNIT: Interacts with CYP11A1. {ECO:0000250|UniProtKB:P10109}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P10109}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; L29123; AAA74303.1; -; mRNA.
DR EMBL; D43689; BAA07786.1; -; mRNA.
DR EMBL; D43690; BAA07787.1; -; mRNA.
DR CCDS; CCDS23178.1; -.
DR PIR; S53524; S53524.
DR RefSeq; NP_001288657.1; NM_001301728.1.
DR RefSeq; NP_032022.1; NM_007996.2.
DR AlphaFoldDB; P46656; -.
DR SMR; P46656; -.
DR BioGRID; 199626; 3.
DR STRING; 10090.ENSMUSP00000034552; -.
DR iPTMnet; P46656; -.
DR PhosphoSitePlus; P46656; -.
DR EPD; P46656; -.
DR jPOST; P46656; -.
DR PaxDb; P46656; -.
DR PeptideAtlas; P46656; -.
DR PRIDE; P46656; -.
DR ProteomicsDB; 296072; -.
DR Antibodypedia; 32013; 117 antibodies from 23 providers.
DR DNASU; 14148; -.
DR Ensembl; ENSMUST00000034552; ENSMUSP00000034552; ENSMUSG00000032051.
DR GeneID; 14148; -.
DR KEGG; mmu:14148; -.
DR UCSC; uc009plo.2; mouse.
DR CTD; 2230; -.
DR MGI; MGI:103224; Fdx1.
DR VEuPathDB; HostDB:ENSMUSG00000032051; -.
DR eggNOG; KOG3309; Eukaryota.
DR GeneTree; ENSGT00940000156916; -.
DR HOGENOM; CLU_082632_2_1_1; -.
DR InParanoid; P46656; -.
DR OMA; VFEDHIF; -.
DR OrthoDB; 1380051at2759; -.
DR PhylomeDB; P46656; -.
DR TreeFam; TF319845; -.
DR Reactome; R-MMU-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR Reactome; R-MMU-196108; Pregnenolone biosynthesis.
DR Reactome; R-MMU-211976; Endogenous sterols.
DR Reactome; R-MMU-2395516; Electron transport from NADPH to Ferredoxin.
DR BioGRID-ORCS; 14148; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Fdx1; mouse.
DR PRO; PR:P46656; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P46656; protein.
DR Bgee; ENSMUSG00000032051; Expressed in adrenal gland and 257 other tissues.
DR ExpressionAtlas; P46656; baseline and differential.
DR Genevisible; P46656; MM.
DR GO; GO:0030061; C:mitochondrial crista; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0008386; F:cholesterol monooxygenase (side-chain-cleaving) activity; ISO:MGI.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; ISO:MGI.
DR GO; GO:0015039; F:NADPH-adrenodoxin reductase activity; ISO:MGI.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:MGI.
DR GO; GO:1904322; P:cellular response to forskolin; IDA:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0042446; P:hormone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0070995; P:NADPH oxidation; ISO:MGI.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:MGI.
DR GO; GO:0050790; P:regulation of catalytic activity; ISO:MGI.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Acetylation; Cholesterol metabolism; Electron transport; Iron;
KW Iron-sulfur; Lipid metabolism; Metal-binding; Mitochondrion;
KW Phosphoprotein; Reference proteome; Steroid metabolism; Steroidogenesis;
KW Sterol metabolism; Transit peptide; Transport.
FT TRANSIT 1..64
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 65..188
FT /note="Adrenodoxin, mitochondrial"
FT /id="PRO_0000000989"
FT DOMAIN 69..175
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 116
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 156
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 162
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10109"
SQ SEQUENCE 188 AA; 20123 MW; 1118DE79BC8BDF48 CRC64;
MAAAPGARLL RAACASVPFR GLDRCRLLVC GTGAGTAISP WTPSPRLHAE AGPGRPLSVS
ARARSSSEDK ITVHFKNRDG ETLTTKGKIG DSLLDVVIEN NLDIDGFGAC EGTLACSTCH
LIFEDHIYEK LDAITDEEND MLDLAFGLTD RSRLGCQVCL TKAMDNMTVR VPEAVADVRQ
SVDMSKNS
