SDHF3_YEAST
ID SDHF3_YEAST Reviewed; 133 AA.
AC Q04401; D6VTD2; Q02562;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Succinate dehydrogenase assembly factor 3, mitochondrial {ECO:0000303|PubMed:24954417};
DE Short=SDH assembly factor 3;
DE Short=SDHAF3 {ECO:0000303|PubMed:24954417};
DE AltName: Full=Acetate non-utilizing protein 9 {ECO:0000303|PubMed:8878673};
DE Flags: Precursor;
GN Name=SDH7 {ECO:0000303|PubMed:24954417};
GN Synonyms=ACN9 {ECO:0000303|PubMed:8878673};
GN OrderedLocusNames=YDR511W {ECO:0000312|SGD:S000002919}; ORFNames=D9719.16;
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 [GENOMIC DNA].
RC STRAIN=YNN 214;
RA Meluh P.B., Koshland D.E.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=8878673; DOI=10.1093/genetics/144.1.57;
RA McCammon M.T.;
RT "Mutants of Saccharomyces cerevisiae with defects in acetate metabolism:
RT isolation and characterization of Acn- mutants.";
RL Genetics 144:57-69(1996).
RN [6]
RP FUNCTION.
RX PubMed=10328823; DOI=10.1006/abbi.1999.1163;
RA Dennis R.A., Rhodey M., McCammon M.T.;
RT "Yeast mutants of glucose metabolism with defects in the coordinate
RT regulation of carbon assimilation.";
RL Arch. Biochem. Biophys. 365:279-288(1999).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10103055; DOI=10.1046/j.1432-1327.1999.00267.x;
RA Dennis R.A., McCammon M.T.;
RT "Acn9 is a novel protein of gluconeogenesis that is located in the
RT mitochondrial intermembrane space.";
RL Eur. J. Biochem. 261:236-243(1999).
RN [8]
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 [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [11]
RP IDENTIFICATION OF MATURE N-TERMINUS, AND MASS SPECTROMETRY.
RX PubMed=19837041; DOI=10.1016/j.cell.2009.07.045;
RA Vogtle F.N., Wortelkamp S., Zahedi R.P., Becker D., Leidhold C.,
RA Gevaert K., Kellermann J., Voos W., Sickmann A., Pfanner N., Meisinger C.;
RT "Global analysis of the mitochondrial N-proteome identifies a processing
RT peptidase critical for protein stability.";
RL Cell 139:428-439(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SDH2.
RX PubMed=24954417; DOI=10.1016/j.cmet.2014.05.014;
RA Na U., Yu W., Cox J., Bricker D.K., Brockmann K., Rutter J., Thummel C.S.,
RA Winge D.R.;
RT "The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur
RT subunit of succinate dehydrogenase.";
RL Cell Metab. 20:253-266(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. Promotes maturation of the iron-sulfur
CC protein subunit SDH2 of the SDH catalytic dimer, protecting it from the
CC deleterious effects of oxidants. Acts together with SDHAF1 (SDH6).
CC {ECO:0000269|PubMed:24954417}.
CC -!- SUBUNIT: Interacts with SDH2 within an SDH1-SDH2 subcomplex.
CC {ECO:0000269|PubMed:24954417}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:10103055}. Mitochondrion matrix
CC {ECO:0000269|PubMed:24954417}.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily.
CC {ECO:0000305}.
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DR EMBL; U27233; AAB01676.1; -; Genomic_DNA.
DR EMBL; U33057; AAB64952.1; -; Genomic_DNA.
DR EMBL; AY558175; AAS56501.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12342.1; -; Genomic_DNA.
DR PIR; S69568; S69568.
DR RefSeq; NP_010799.3; NM_001180819.3.
DR AlphaFoldDB; Q04401; -.
DR SMR; Q04401; -.
DR BioGRID; 32562; 47.
DR DIP; DIP-2752N; -.
DR IntAct; Q04401; 3.
DR MINT; Q04401; -.
DR STRING; 4932.YDR511W; -.
DR iPTMnet; Q04401; -.
DR MaxQB; Q04401; -.
DR PaxDb; Q04401; -.
DR PRIDE; Q04401; -.
DR EnsemblFungi; YDR511W_mRNA; YDR511W; YDR511W.
DR GeneID; 852123; -.
DR KEGG; sce:YDR511W; -.
DR SGD; S000002919; SDH7.
DR VEuPathDB; FungiDB:YDR511W; -.
DR eggNOG; KOG4100; Eukaryota.
DR GeneTree; ENSGT00390000010029; -.
DR HOGENOM; CLU_102310_1_1_1; -.
DR InParanoid; Q04401; -.
DR OMA; LTEWQMY; -.
DR BioCyc; YEAST:G3O-30031-MON; -.
DR PRO; PR:Q04401; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04401; protein.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0015976; P:carbon utilization; IMP:SGD.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IPI:SGD.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:SGD.
DR GO; GO:0006105; P:succinate metabolic process; IBA:GO_Central.
DR InterPro; IPR008381; SDHAF3/Sdh7.
DR PANTHER; PTHR13137; PTHR13137; 1.
PE 1: Evidence at protein level;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19837041"
FT CHAIN 13..133
FT /note="Succinate dehydrogenase assembly factor 3,
FT mitochondrial"
FT /id="PRO_0000042652"
FT CONFLICT 13
FT /note="A -> G (in Ref. 1; AAB01676)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="S -> R (in Ref. 1; AAB01676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 133 AA; 15783 MW; 340F408ED251A12D CRC64;
MNNKLIYRSV RFATHNSQLL LPPLVLYRRI LRQHKLLPGP QREMGDQYVR NEFKLHKDID
NPLHIVGFLA SWQDYLHMIS NGKWKDATLS SETLEKLSPE QTVQLYELMK ETQKLHQDNE
IESSKDVKRN NKD
