LOCUS       NM_001397406            1012 bp    mRNA    linear   PRI 12-NOV-2024
DEFINITION  Homo sapiens ferredoxin 2 (FDX2), mRNA; nuclear gene for
            mitochondrial product.
ACCESSION   NM_001397406 NM_001031734
VERSION     NM_001397406.1
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1012)
  AUTHORS   Grifagni,D., Doni,D., Susini,B., Fonseca,B.M., Louro,R.O.,
            Costantini,P. and Ciofi-Baffoni,S.
  TITLE     Unraveling the molecular determinants of a rare human mitochondrial
            disorder caused by the P144L mutation of FDX2
  JOURNAL   Protein Sci 33 (11), e5197 (2024)
   PUBMED   39467201
  REMARK    GeneRIF: Unraveling the molecular determinants of a rare human
            mitochondrial disorder caused by the P144L mutation of FDX2.
REFERENCE   2  (bases 1 to 1012)
  AUTHORS   Schulz,V., Basu,S., Freibert,S.A., Webert,H., Boss,L.,
            Muhlenhoff,U., Pierrel,F., Essen,L.O., Warui,D.M., Booker,S.J.,
            Stehling,O. and Lill,R.
  TITLE     Functional spectrum and specificity of mitochondrial ferredoxins
            FDX1 and FDX2
  JOURNAL   Nat Chem Biol 19 (2), 206-217 (2023)
   PUBMED   36280795
  REMARK    GeneRIF: Functional spectrum and specificity of mitochondrial
            ferredoxins FDX1 and FDX2.
REFERENCE   3  (bases 1 to 1012)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (bases 1 to 1012)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   5  (bases 1 to 1012)
  AUTHORS   Gervason,S., Larkem,D., Mansour,A.B., Botzanowski,T., Muller,C.S.,
            Pecqueur,L., Le Pavec,G., Delaunay-Moisan,A., Brun,O., Agramunt,J.,
            Grandas,A., Fontecave,M., Schunemann,V., Cianferani,S., Sizun,C.,
            Toledano,M.B. and D'Autreaux,B.
  TITLE     Physiologically relevant reconstitution of iron-sulfur cluster
            biosynthesis uncovers persulfide-processing functions of
            ferredoxin-2 and frataxin
  JOURNAL   Nat Commun 10 (1), 3566 (2019)
   PUBMED   31395877
  REMARK    GeneRIF: By binding zinc-free ISCU, iron drives persulfide uptake
            from NFS1 and allows persulfide reduction into sulfide by FDX2,
            thereby coordinating sulfide production with its availability to
            generate Fe-S clusters. FXN stimulates the whole process by
            accelerating persulfide transfer. This reconstitution recapitulates
            physiological conditions which provides a model for Fe-S cluster
            biosynthesis on the scaffold protein ISCU.
            Publication Status: Online-Only
REFERENCE   6  (bases 1 to 1012)
  AUTHORS   Qi,W., Li,J. and Cowan,J.A.
  TITLE     Human ferredoxin-2 displays a unique conformational change
  JOURNAL   Dalton Trans 42 (9), 3088-3091 (2013)
   PUBMED   23208207
  REMARK    GeneRIF: unique conformational change is observed when holo hFd2 is
            warmed to physiological temperatures, or higher
REFERENCE   7  (bases 1 to 1012)
  AUTHORS   Shi,Y., Ghosh,M., Kovtunovych,G., Crooks,D.R. and Rouault,T.A.
  TITLE     Both human ferredoxins 1 and 2 and ferredoxin reductase are
            important for iron-sulfur cluster biogenesis
  JOURNAL   Biochim Biophys Acta 1823 (2), 484-492 (2012)
   PUBMED   22101253
REFERENCE   8  (bases 1 to 1012)
  AUTHORS   Hendrickson,S.L., Lautenberger,J.A., Chinn,L.W., Malasky,M.,
            Sezgin,E., Kingsley,L.A., Goedert,J.J., Kirk,G.D., Gomperts,E.D.,
            Buchbinder,S.P., Troyer,J.L. and O'Brien,S.J.
  TITLE     Genetic variants in nuclear-encoded mitochondrial genes influence
            AIDS progression
  JOURNAL   PLoS One 5 (9), e12862 (2010)
   PUBMED   20877624
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Online-Only
REFERENCE   9  (bases 1 to 1012)
  AUTHORS   Sheftel,A.D., Stehling,O., Pierik,A.J., Elsasser,H.P.,
            Muhlenhoff,U., Webert,H., Hobler,A., Hannemann,F., Bernhardt,R. and
            Lill,R.
  TITLE     Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with
            distinct roles in steroidogenesis, heme, and Fe/S cluster
            biosynthesis
  JOURNAL   Proc Natl Acad Sci U S A 107 (26), 11775-11780 (2010)
   PUBMED   20547883
REFERENCE   10 (bases 1 to 1012)
  AUTHORS   Chang,C.Y., Wu,D.A., Mohandas,T.K. and Chung,B.C.
  TITLE     Structure, sequence, chromosomal location, and evolution of the
            human ferredoxin gene family
  JOURNAL   DNA Cell Biol 9 (3), 205-212 (1990)
   PUBMED   2340092
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC011511.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Nov 15, 2021 this sequence version replaced NM_001031734.4.
            
            Summary: This gene encodes a member of the ferredoxin family. The
            encoded protein contains a 2Fe-2S ferredoxin-type domain and is
            essential for heme A and Fe/S protein biosynthesis. Mutation in
            FDX1L gene is associated with mitochondrial muscle myopathy.
            [provided by RefSeq, Sep 2014].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC063460.1, DA243025.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            CDS uses downstream in-frame AUG   :: upstream AUG and CDS
                                                  extension is not conserved
            gene product(s) localized to mito. :: reported by MitoCarta
            MANE Ensembl match                 :: ENST00000393708.3/
                                                  ENSP00000377311.5
            RefSeq Select criteria             :: based on single
                                                  protein-coding transcript
            ##RefSeq-Attributes-END##
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-164               AC011511.12        130495-130658       c
            165-219             AC011511.12        130348-130402       c
            220-326             AC011511.12        130029-130135       c
            327-414             AC011511.12        125496-125583       c
            415-1012            AC011511.12        124688-125285       c
FEATURES             Location/Qualifiers
     source          1..1012
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.2"
     gene            1..1012
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /note="ferredoxin 2"
                     /db_xref="GeneID:112812"
                     /db_xref="HGNC:HGNC:30546"
                     /db_xref="MIM:614585"
     exon            1..164
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /inference="alignment:Splign:2.1.0"
     CDS             20..571
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /note="adrenodoxin-like protein, mitochondrial; ferredoxin
                     1 like"
                     /codon_start=1
                     /product="ferredoxin-2, mitochondrial"
                     /protein_id="NP_001384335.1"
                     /db_xref="CCDS:CCDS32905.3"
                     /db_xref="GeneID:112812"
                     /db_xref="HGNC:HGNC:30546"
                     /db_xref="MIM:614585"
                     /translation="MAASMARGGVSARVLLQAARGTWWNRPGGTSGSGEGVALGTTRK
                     FQATGSRPAGEEDAGGPERPGDVVNVVFVDRSGQRIPVSGRVGDNVLHLAQRHGVDLE
                     GACEASLACSTCHVYVSEDHLDLLPPPEEREDDMLDMAPLLQENSRLGCQIVLTPELE
                     GAEFTLPKITRNFYVDGHVPKPH"
     exon            165..219
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /inference="alignment:Splign:2.1.0"
     exon            220..326
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /inference="alignment:Splign:2.1.0"
     exon            327..414
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /inference="alignment:Splign:2.1.0"
     exon            415..1012
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /inference="alignment:Splign:2.1.0"
     regulatory      823..828
                     /regulatory_class="polyA_signal_sequence"
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /note="hexamer: AATAAA"
     polyA_site      842
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /note="major polyA site"
     regulatory      993..998
                     /regulatory_class="polyA_signal_sequence"
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
                     /note="hexamer: TATAAA"
     polyA_site      1012
                     /gene="FDX2"
                     /gene_synonym="FDX1L; MEOAL"
ORIGIN      
        1 gagtcacgtg atgcatgtca tggccgcctc catggcccgg ggaggcgtga gtgccagggt
       61 tctactgcag gctgccaggg gcacctggtg gaacagacct gggggcactt ccgggtcggg
      121 ggagggggtg gcgctgggga caaccagaaa gtttcaagcg acaggctcgc gcccggctgg
      181 agaggaggac gcgggcggcc cggagcggcc cggggacgtg gtgaacgtgg tgttcgtaga
      241 ccgctcaggc cagcggatcc cagtgagtgg cagagtcggg gacaatgttc ttcacctggc
      301 ccagcgccac ggggtggacc tggaaggggc ctgtgaagcc tccctggcct gctccacctg
      361 ccatgtgtat gtgagtgaag accacctgga tctcctgcct cctcccgagg agagggaaga
      421 cgacatgcta gacatggccc ccctcctcca ggagaactcg cggctgggct gccagattgt
      481 gctgacaccg gagctggaag gagcggaatt caccctgccc aagatcacca ggaacttcta
      541 cgtggatggc catgtcccca agccccactg acatgaacac ctggaccatt ccacattgcc
      601 atggccccag ggcccagatt gagggaatag ccaggtgcca gccctgccca gagtgcggac
      661 aggcccggga gagacgtgga agcccctgtg aaggacaaca cccctgcttg ggagagagtc
      721 ccatgtccag gctctggtgg ggacagggcc cctagtgggg tggccttccc caggcccctg
      781 agaatcaggg tttgagtagg agtggactca tattggagct gcaataaatc gataacacag
      841 gccccagcat gttgagtgtc cttgggggac agatctgggg tctacaggtg gctcacacct
      901 gtaatcctag cactttggga agccaagatg ggaggatcac ttgaggccag gagcttaaga
      961 ccatcctggg caacatggcg agacctcgtc tctataaaaa cagtaaaaat ta
//
