SDHF1_SCHPO
ID SDHF1_SCHPO Reviewed; 79 AA.
AC Q9US02;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Succinate dehydrogenase assembly factor 1, mitochondrial {ECO:0000250|UniProtKB:Q3E785};
DE Short=SDH assembly factor 1 {ECO:0000250|UniProtKB:Q3E785};
DE Short=SDHAF1 {ECO:0000250|UniProtKB:Q3E785};
GN ORFNames=SPAC664.12c;
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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 SDHAF3.
CC {ECO:0000250|UniProtKB:Q3E785}.
CC -!- SUBUNIT: Interacts with sdh2 within an sdh1-sdh2 subcomplex.
CC {ECO:0000250|UniProtKB:Q3E785}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q3E785}.
CC -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB65813.1; -; Genomic_DNA.
DR PIR; T50242; T50242.
DR RefSeq; NP_593460.1; NM_001018893.2.
DR AlphaFoldDB; Q9US02; -.
DR SMR; Q9US02; -.
DR STRING; 4896.SPAC664.12c.1; -.
DR PaxDb; Q9US02; -.
DR EnsemblFungi; SPAC664.12c.1; SPAC664.12c.1:pep; SPAC664.12c.
DR GeneID; 2543362; -.
DR KEGG; spo:SPAC664.12c; -.
DR PomBase; SPAC664.12c; -.
DR VEuPathDB; FungiDB:SPAC664.12c; -.
DR eggNOG; KOG4620; Eukaryota.
DR HOGENOM; CLU_154777_1_1_1; -.
DR InParanoid; Q9US02; -.
DR OMA; WSEPGIR; -.
DR PhylomeDB; Q9US02; -.
DR PRO; PR:Q9US02; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; ISO:PomBase.
DR CDD; cd20268; Complex1_LYR_SDHAF1_LYRM8; 1.
DR InterPro; IPR008011; Complex1_LYR_dom.
DR InterPro; IPR045295; Complex1_LYR_SDHAF1_LYRM8.
DR Pfam; PF05347; Complex1_LYR; 1.
PE 3: Inferred from homology;
KW Chaperone; Mitochondrion; Reference proteome.
FT CHAIN 1..79
FT /note="Succinate dehydrogenase assembly factor 1,
FT mitochondrial"
FT /id="PRO_0000374046"
SQ SEQUENCE 79 AA; 9730 MW; D67451CB423124DF CRC64;
MALSGLQRQV IHFYRRCLHA AKAKEQPYNE RWMAFVHQEF RKNQTISKRD FFYIEHLLRV
GQRQYEAYSR PEVKDIHFS
