ID   SDHF3_KLULA             Reviewed;         129 AA.
AC   Q6CUY0; Q8X1Y8;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
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   Flags: Precursor;
GN   OrderedLocusNames=KLLA0C01430g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-128.
RA   Lamas-Maceiras M.;
RL   Thesis (2001), Universidad de La coruna, Spain.
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; CR382123; CAH01110.1; -; Genomic_DNA.
DR   EMBL; AJ312189; CAC85376.1; -; Genomic_DNA.
DR   RefSeq; XP_452259.1; XM_452259.1.
DR   AlphaFoldDB; Q6CUY0; -.
DR   SMR; Q6CUY0; -.
DR   STRING; 28985.XP_452259.1; -.
DR   EnsemblFungi; CAH01110; CAH01110; KLLA0_C01430g.
DR   GeneID; 2892688; -.
DR   KEGG; kla:KLLA0_C01430g; -.
DR   eggNOG; KOG4100; Eukaryota.
DR   HOGENOM; CLU_102310_1_0_1; -.
DR   InParanoid; Q6CUY0; -.
DR   OMA; LTEWQMY; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0015976; P:carbon utilization; IEA:EnsemblFungi.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IEA:EnsemblFungi.
DR   GO; GO:0006111; P:regulation of gluconeogenesis; IEA:EnsemblFungi.
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..21
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..129
FT                   /note="Succinate dehydrogenase assembly factor 3,
FT                   mitochondrial"
FT                   /id="PRO_0000042748"
SQ   SEQUENCE   129 AA;  15155 MW;  483BE15CD81D760B CRC64;
     MQVNHLLRQA VKQTTRAGRL GSRKPHKPLL PPLQLYRRIL REHRNLPTMQ RELGDQYVKN
     EFKLHKSTDN PLYIVGFLAS WQDYLHMITR GEWEEGTLST DLLEKMSPEQ VTQLYELMKE
     AEQLKSGGE