SDHF4_YEAST
ID SDHF4_YEAST Reviewed; 138 AA.
AC P38345; D6VQR5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Succinate dehydrogenase assembly factor 4, mitochondrial {ECO:0000303|PubMed:24954416};
DE Short=SDH assembly factor 4 {ECO:0000303|PubMed:24954416};
DE Short=SDHAF4 {ECO:0000303|PubMed:24954416};
DE AltName: Full=Found in mitochondrial proteome protein 21 {ECO:0000303|PubMed:14576278};
DE Flags: Precursor;
GN Name=SDH8 {ECO:0000303|PubMed:24954416};
GN Synonyms=FMP21 {ECO:0000303|PubMed:14576278};
GN OrderedLocusNames=YBR269C {ECO:0000312|SGD:S000000473}; ORFNames=YBR1737;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SEQUENCE REVISION TO 120 AND 123.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SDH1.
RX PubMed=24954416; DOI=10.1016/j.cmet.2014.05.012;
RA Van Vranken J.G., Bricker D.K., Dephoure N., Gygi S.P., Cox J.E.,
RA Thummel C.S., Rutter J.;
RT "SDHAF4 promotes mitochondrial succinate dehydrogenase activity and
RT prevents neurodegeneration.";
RL Cell Metab. 20:241-252(2014).
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. Binds to the flavoprotein subunit SDH1 in
CC its FAD-bound form, blocking the generation of excess reactive oxigen
CC species (ROS) and facilitating its assembly with the iron-sulfur
CC protein subunit SDH2 into the SDH catalytic dimer.
CC {ECO:0000269|PubMed:24954416}.
CC -!- SUBUNIT: Interacts with SDH1 in its FAD-bound form.
CC {ECO:0000269|PubMed:24954416}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:24954416}.
CC -!- SIMILARITY: Belongs to the SDHAF4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA85232.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z36138; CAA85232.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006936; DAA07385.1; -; Genomic_DNA.
DR PIR; S46150; S46150.
DR RefSeq; NP_009828.2; NM_001178617.1.
DR AlphaFoldDB; P38345; -.
DR SMR; P38345; -.
DR BioGRID; 32964; 59.
DR DIP; DIP-4772N; -.
DR IntAct; P38345; 1.
DR STRING; 4932.YBR269C; -.
DR iPTMnet; P38345; -.
DR MaxQB; P38345; -.
DR PaxDb; P38345; -.
DR PRIDE; P38345; -.
DR EnsemblFungi; YBR269C_mRNA; YBR269C; YBR269C.
DR GeneID; 852572; -.
DR KEGG; sce:YBR269C; -.
DR SGD; S000000473; SDH8.
DR VEuPathDB; FungiDB:YBR269C; -.
DR eggNOG; ENOG502S6UN; Eukaryota.
DR HOGENOM; CLU_101052_1_0_1; -.
DR InParanoid; P38345; -.
DR OMA; GGDWSYN; -.
DR BioCyc; YEAST:G3O-29190-MON; -.
DR PRO; PR:P38345; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38345; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0008047; F:enzyme activator activity; IMP:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; IMP:SGD.
DR GO; GO:0045333; P:cellular respiration; IGI:UniProtKB.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IMP:SGD.
DR GO; GO:1904231; P:positive regulation of succinate dehydrogenase activity; IMP:UniProtKB.
DR InterPro; IPR012875; SDHF4.
DR Pfam; PF07896; DUF1674; 1.
PE 1: Evidence at protein level;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 33..138
FT /note="Succinate dehydrogenase assembly factor 4,
FT mitochondrial"
FT /id="PRO_0000041936"
FT REGION 71..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 138 AA; 15504 MW; 62289A10A10FBC6E CRC64;
MLCAIKSTGY RYPRTGALNL LRGRPFNMAT RKITTERIPG PPKLPREEQE EFERLQRIAT
SQEAIDQYNA QATGDRTKES LNSPLLTKND IGSFSPEFSK TIPEFEGDVN PKTGEVGGPK
QDPLRHGDYS FNGRVTDF
