FDX2_MOUSE
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 03-AUG-2022, entry version 148.
DE RecName: Full=Ferredoxin-2, mitochondrial;
DE AltName: Full=Adrenodoxin-like protein;
DE AltName: Full=Ferredoxin-1-like protein;
DE Flags: Precursor;
GN Name=Fdx2; 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: Essential for heme A and Fe/S protein biosynthesis.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_001039824.2. [Q9CPW2-1]
DR AlphaFoldDB; Q9CPW2; -.
DR SMR; Q9CPW2; -.
DR BioGRID; 426689; 1.
DR ComplexPortal; CPX-5823; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR STRING; 10090.ENSMUSP00000010348; -.
DR iPTMnet; Q9CPW2; -.
DR PhosphoSitePlus; Q9CPW2; -.
DR EPD; Q9CPW2; -.
DR MaxQB; Q9CPW2; -.
DR PaxDb; Q9CPW2; -.
DR PeptideAtlas; Q9CPW2; -.
DR PRIDE; Q9CPW2; -.
DR ProteomicsDB; 271737; -. [Q9CPW2-1]
DR ProteomicsDB; 271738; -. [Q9CPW2-2]
DR DNASU; 68165; -.
DR Ensembl; ENSMUST00000010348; ENSMUSP00000010348; ENSMUSG00000079677. [Q9CPW2-1]
DR GeneID; 68165; -.
DR KEGG; mmu:68165; -.
DR UCSC; uc009okb.1; mouse. [Q9CPW2-1]
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; ERRTHGW; -.
DR OrthoDB; 1380051at2759; -.
DR PhylomeDB; Q9CPW2; -.
DR TreeFam; TF354319; -.
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 76 CRISPR screens.
DR PRO; PR:Q9CPW2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CPW2; protein.
DR Bgee; ENSMUSG00000079677; Expressed in quadriceps femoris and 62 other tissues.
DR Genevisible; Q9CPW2; MM.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IC:ComplexPortal.
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 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; 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
