ADX_PIG
ID ADX_PIG Reviewed; 186 AA.
AC P00258;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Adrenodoxin, mitochondrial;
DE AltName: Full=Adrenal ferredoxin;
DE AltName: Full=Ferredoxin-1;
DE Flags: Precursor;
GN Name=FDX1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=1536558; DOI=10.1016/0003-9861(92)90387-c;
RA Omdahl J.L., Wilson K., Swerdlow H., Driscoll W.J.;
RT "Molecular cloning and immunological characterization of porcine kidney
RT ferredoxin.";
RL Arch. Biochem. Biophys. 293:213-218(1992).
RN [2]
RP PROTEIN SEQUENCE OF 59-175.
RA Akhrem A.A., Lapko A.G., Lapko V.N., Morozova L.A., Repin V.A.,
RA Tishchenko I.V., Chashchin V.L.;
RT "Adrenodoxin.";
RL Bioorg. Khim. 4:462-475(1978).
RN [3]
RP PROTEIN SEQUENCE OF 59-76.
RX PubMed=2553401; DOI=10.1111/j.1432-1033.1989.tb15100.x;
RA Driscoll W.J., Omdahl J.L.;
RT "Characterization and N-terminal amino acid sequence of multiple
RT ferredoxins in kidney and adrenal mitochondria.";
RL Eur. J. Biochem. 185:181-187(1989).
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 Note=Binds 1 [2Fe-2S] cluster.;
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; M57674; AAA31030.1; -; mRNA.
DR PIR; S20332; AXPG.
DR RefSeq; NP_999230.1; NM_214065.1.
DR RefSeq; XP_013844957.1; XM_013989503.1.
DR AlphaFoldDB; P00258; -.
DR SMR; P00258; -.
DR PeptideAtlas; P00258; -.
DR PRIDE; P00258; -.
DR Ensembl; ENSSSCT00000065716; ENSSSCP00000033794; ENSSSCG00000035945.
DR Ensembl; ENSSSCT00025065808; ENSSSCP00025028084; ENSSSCG00025048372.
DR Ensembl; ENSSSCT00030088487; ENSSSCP00030040904; ENSSSCG00030063230.
DR Ensembl; ENSSSCT00035040880; ENSSSCP00035016356; ENSSSCG00035030873.
DR Ensembl; ENSSSCT00040052626; ENSSSCP00040021856; ENSSSCG00040039367.
DR Ensembl; ENSSSCT00045008298; ENSSSCP00045005644; ENSSSCG00045004989.
DR Ensembl; ENSSSCT00050024746; ENSSSCP00050010346; ENSSSCG00050018243.
DR Ensembl; ENSSSCT00055032153; ENSSSCP00055025603; ENSSSCG00055016302.
DR Ensembl; ENSSSCT00060081878; ENSSSCP00060035471; ENSSSCG00060060010.
DR Ensembl; ENSSSCT00065058339; ENSSSCP00065025290; ENSSSCG00065042670.
DR GeneID; 397133; -.
DR KEGG; ssc:397133; -.
DR CTD; 2230; -.
DR VGNC; VGNC:88078; FDX1.
DR GeneTree; ENSGT00940000156916; -.
DR InParanoid; P00258; -.
DR OMA; VFEDHIF; -.
DR OrthoDB; 1380051at2759; -.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000035945; Expressed in ovary and 47 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:1904322; P:cellular response to forskolin; IEA:Ensembl.
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:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IBA:GO_Central.
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; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Lipid metabolism; Metal-binding;
KW Mitochondrion; Phosphoprotein; Reference proteome; Steroid metabolism;
KW Steroidogenesis; Sterol metabolism; Transit peptide; Transport.
FT TRANSIT 1..58
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2553401, ECO:0000269|Ref.2"
FT CHAIN 59..186
FT /note="Adrenodoxin, mitochondrial"
FT /id="PRO_0000000990"
FT DOMAIN 65..169
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
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 113
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 150
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46656"
FT MOD_RES 64
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P46656"
FT MOD_RES 64
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P46656"
FT MOD_RES 156
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46656"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10109"
SQ SEQUENCE 186 AA; 19932 MW; BA6372223C403931 CRC64;
MAVRLLRVAS AALGDTAVRW QPLVGPRAGN RGPGGSIWLG LGGRAAAART LSLSARAWSS
SEDKITVHFI NRDGKTLTTQ GKVGDSLLDV VIENNLDIDG FGACEGTLAC STCHLIFEDH
IFEKLEAITD EENDMLDLAY GLTDRSRLGC QICLTKAMDN MTVRVPEAVA DARESIDLGK
NSSKLE
