ID   SDHF3_SCHPO             Reviewed;         115 AA.
AC   Q9P7Y2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 102.
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   ORFNames=SPBP23A10.03c {ECO:0000312|PomBase:SPBP23A10.03c};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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 sdh2 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 sdh2 within an sdh1-sdh2 subcomplex.
CC       {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; CU329671; CAB66431.1; -; Genomic_DNA.
DR   PIR; T50390; T50390.
DR   RefSeq; NP_595815.1; NM_001021719.2.
DR   AlphaFoldDB; Q9P7Y2; -.
DR   SMR; Q9P7Y2; -.
DR   STRING; 4896.SPBP23A10.03c.1; -.
DR   MaxQB; Q9P7Y2; -.
DR   PaxDb; Q9P7Y2; -.
DR   EnsemblFungi; SPBP23A10.03c.1; SPBP23A10.03c.1:pep; SPBP23A10.03c.
DR   GeneID; 2541309; -.
DR   KEGG; spo:SPBP23A10.03c; -.
DR   PomBase; SPBP23A10.03c; -.
DR   VEuPathDB; FungiDB:SPBP23A10.03c; -.
DR   eggNOG; KOG4100; Eukaryota.
DR   HOGENOM; CLU_102310_1_0_1; -.
DR   InParanoid; Q9P7Y2; -.
DR   OMA; INQLTHP; -.
DR   PhylomeDB; Q9P7Y2; -.
DR   PRO; PR:Q9P7Y2; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISO:PomBase.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; ISO:PomBase.
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; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..115
FT                   /note="Succinate dehydrogenase assembly factor 3,
FT                   mitochondrial"
FT                   /id="PRO_0000042751"
SQ   SEQUENCE   115 AA;  13641 MW;  68A5FD8310836C13 CRC64;
     MNNITKLMKQ KNILTPPLPL YRRVLRAHRY HLGAEERALG DEYVKAEFRR HRNVTNPLHL
     VGFLSSWERY ADALENESWK QEKYSNTDLL ESLNDQQIGQ LYELSKALQE QKKSE