ID   FDX2_MOUSE              Reviewed;         174 AA.
AC   Q9CPW2; Q6P8M0; Q9CV00;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=Ferredoxin-2, mitochondrial {ECO:0000305};
DE   AltName: Full=Adrenodoxin-like protein;
DE   AltName: Full=Ferredoxin-1-like protein;
DE   Flags: Precursor;
GN   Name=Fdx2 {ECO:0000312|MGI:MGI:1915415}; Synonyms=Fdx1l;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Small intestine;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, 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).
CC   -!- FUNCTION: Electron donor, of the core iron-sulfur cluster (ISC)
CC       assembly complex, that acts to reduce the persulfide into sulfide
CC       during [2Fe-2S] clusters assembly on the scaffolding protein ISCU (By
CC       similarity). The core iron-sulfur cluster (ISC) assembly complex is
CC       involved in the de novo synthesis of a [2Fe-2S] cluster, the first step
CC       of the mitochondrial iron-sulfur protein biogenesis. This process is
CC       initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that
CC       produces persulfide which is delivered on the scaffold protein ISCU in
CC       a FXN-dependent manner. Then this complex is stabilized by FDX2 which
CC       provides reducing equivalents to accomplish the [2Fe-2S] cluster
CC       assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to
CC       chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity).
CC       Essential for coenzyme Q biosynthesis: together with FDXR, transfers
CC       the electrons required for the hydroxylation reaction performed by COQ6
CC       (By similarity). {ECO:0000250|UniProtKB:Q6P4F2,
CC       ECO:0000250|UniProtKB:Q9H1K1}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:Q9H1K1};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:Q9H1K1};
CC   -!- SUBUNIT: Component of the mitochondrial core iron-sulfur cluster (ISC)
CC       complex composed of NFS1, LYRM4, NDUFAB1, ISCU, FXN, and FDX2; this
CC       complex is a heterohexamer containing two copies of each monomer. Form
CC       a heterodimer complex with NFS1. Interacts (in both their reduced and
CC       oxidized states) with the cysteine desulfurase (NFS1:LYRM4) complex;
CC       this interaction stimulates cysteine desulfurase activity, and serves
CC       as a reductant for Fe-S cluster assembly.
CC       {ECO:0000250|UniProtKB:Q6P4F2}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H1K1}.
CC       Mitochondrion matrix {ECO:0000250|UniProtKB:P10109}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CPW2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CPW2-2; Sequence=VSP_032498;
CC   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26771.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK008401; BAB25650.1; -; mRNA.
DR   EMBL; AK010211; BAB26771.1; ALT_FRAME; mRNA.
DR   EMBL; AK020979; BAB32267.1; -; mRNA.
DR   EMBL; BC061189; AAH61189.1; -; mRNA.
DR   CCDS; CCDS22892.1; -. [Q9CPW2-1]
DR   RefSeq; NP_001034913.1; NM_001039824.3. [Q9CPW2-1]
DR   AlphaFoldDB; Q9CPW2; -.
DR   SMR; Q9CPW2; -.
DR   BioGRID; 426689; 1.
DR   ComplexPortal; CPX-5823; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR   FunCoup; Q9CPW2; 1091.
DR   STRING; 10090.ENSMUSP00000010348; -.
DR   iPTMnet; Q9CPW2; -.
DR   PhosphoSitePlus; Q9CPW2; -.
DR   PaxDb; 10090-ENSMUSP00000010348; -.
DR   PeptideAtlas; Q9CPW2; -.
DR   ProteomicsDB; 271737; -. [Q9CPW2-1]
DR   ProteomicsDB; 271738; -. [Q9CPW2-2]
DR   Pumba; Q9CPW2; -.
DR   DNASU; 68165; -.
DR   Ensembl; ENSMUST00000010348.7; ENSMUSP00000010348.6; ENSMUSG00000079677.3. [Q9CPW2-1]
DR   GeneID; 68165; -.
DR   KEGG; mmu:68165; -.
DR   UCSC; uc009okb.1; mouse. [Q9CPW2-1]
DR   AGR; MGI:1915415; -.
DR   CTD; 112812; -.
DR   MGI; MGI:1915415; Fdx2.
DR   VEuPathDB; HostDB:ENSMUSG00000079677; -.
DR   eggNOG; KOG3309; Eukaryota.
DR   GeneTree; ENSGT00940000161143; -.
DR   HOGENOM; CLU_082632_0_2_1; -.
DR   InParanoid; Q9CPW2; -.
DR   OMA; RGCHWAC; -.
DR   OrthoDB; 268593at2759; -.
DR   PhylomeDB; Q9CPW2; -.
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; 68165; 29 hits in 80 CRISPR screens.
DR   PRO; PR:Q9CPW2; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9CPW2; protein.
DR   Bgee; ENSMUSG00000079677; Expressed in quadriceps femoris and 64 other cell types or tissues.
DR   GO; GO:1990229; C:iron-sulfur cluster assembly complex; NAS:ComplexPortal.
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; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; ISS:UniProtKB.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; ISS:UniProtKB.
DR   GO; GO:0044572; P:[4Fe-4S] cluster assembly; ISS:UniProtKB.
DR   GO; GO:1904322; P:cellular response to forskolin; IEA:UniProtKB-ARBA.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; NAS:ComplexPortal.
DR   GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB.
DR   CDD; cd00207; fer2; 1.
DR   FunFam; 3.10.20.30:FF:000013; Adrenodoxin, mitochondrial; 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-like.
DR   InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   PANTHER; PTHR23426:SF65; FERREDOXIN-2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR23426; FERREDOXIN/ADRENODOXIN; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00355; ADRENODOXIN.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00814; ADX; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Alternative splicing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Mitochondrion; Reference proteome; Transit peptide;
KW   Transport.
FT   TRANSIT         1..43
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..174
FT                   /note="Ferredoxin-2, mitochondrial"
FT                   /id="PRO_0000325953"
FT   DOMAIN          59..161
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   REGION          26..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         96
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         102
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         105
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         142
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   VAR_SEQ         1..126
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032498"
FT   CONFLICT        11
FT                   /note="A -> G (in Ref. 1; BAB26771)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   174 AA;  18766 MW;  F0E2506668F7038A CRC64;
     MAASMARGVS ARVLLRAAGG SWGPRAGHAA VTSRTFGTTG ERRAGEEAAD SPELPRDVVN
     VVFVDRSGKR IPVRGKVGDN VLYLAQRHGV DLEGACEASL ACSTCHVYVS EAHLDLLPPP
     EEREDDMLDM APLLQENSRL GCQIVLTPEL EGVEFALPKI TRNFYVDGHI PKPH
//