SDHF3_NEUCR
ID SDHF3_NEUCR Reviewed; 148 AA.
AC Q7SF55;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Succinate dehydrogenase assembly factor 3, mitochondrial {ECO:0000250|UniProtKB:Q04401};
DE Short=SDH assembly factor 3 {ECO:0000250|UniProtKB:Q04401};
DE Short=SDHAF3 {ECO:0000250|UniProtKB:Q04401};
DE AltName: Full=Acetate non-utilizing protein 17 {ECO:0000305};
DE Flags: Precursor;
GN Name=acu-17 {ECO:0000305}; ORFNames=B23L4.040, NCU09255;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Plays an essential role in the assembly of succinate
CC dehydrogenase (SDH), an enzyme complex (also referred to as respiratory
CC complex II) that is a component of both the tricarboxylic acid (TCA)
CC cycle and the mitochondrial electron transport chain, and which couples
CC the oxidation of succinate to fumarate with the reduction of ubiquinone
CC (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur
CC protein subunit of the SDH catalytic dimer, protecting it from the
CC deleterious effects of oxidants. May act together with SDHAF1.
CC {ECO:0000250|UniProtKB:Q04401, ECO:0000250|UniProtKB:Q8SZ16}.
CC -!- SUBUNIT: Interacts with the iron-sulfur protein subunit within the SDH
CC catalytic dimer. {ECO:0000250|UniProtKB:Q04401}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q04401}.
CC -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily.
CC {ECO:0000305}.
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DR EMBL; CM002236; EAA35454.1; -; Genomic_DNA.
DR EMBL; BX842628; CAE76306.1; -; Genomic_DNA.
DR RefSeq; XP_964690.1; XM_959597.2.
DR AlphaFoldDB; Q7SF55; -.
DR SMR; Q7SF55; -.
DR STRING; 5141.EFNCRP00000009061; -.
DR EnsemblFungi; EAA35454; EAA35454; NCU09255.
DR GeneID; 3880839; -.
DR KEGG; ncr:NCU09255; -.
DR VEuPathDB; FungiDB:NCU09255; -.
DR HOGENOM; CLU_102310_1_0_1; -.
DR InParanoid; Q7SF55; -.
DR OMA; INQLTHP; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR GO; GO:0006105; P:succinate metabolic process; IBA:GO_Central.
DR InterPro; IPR008381; SDHAF3/Sdh7.
DR PANTHER; PTHR13137; PTHR13137; 1.
PE 3: Inferred from homology;
KW Chaperone; Gluconeogenesis; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 13..148
FT /note="Succinate dehydrogenase assembly factor 3,
FT mitochondrial"
FT /id="PRO_0000042750"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 148 AA; 16883 MW; 9FD27C4816B9D0A3 CRC64;
MYALRPTLRR SAAAALTHSK NHNYGMTPGP LALLPPIYLY RRLLRAHRKY LPREMRLLGD
EYVKAEFRAH RSVDNPAHLI GFLTEWQLYA QKIEGNSWVG EKLDKGKVEK MSDEQIGQLY
ELMQAIQKRG TEGDLEDGDG GESGQKSQ