SDHF2_YEAST
ID SDHF2_YEAST Reviewed; 162 AA.
AC Q08230; D6W1Z6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Succinate dehydrogenase assembly factor 2, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03057, ECO:0000303|PubMed:23062074};
DE Short=SDH assembly factor 2 {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDHAF2 {ECO:0000255|HAMAP-Rule:MF_03057, ECO:0000303|PubMed:23062074};
DE Flags: Precursor;
GN Name=SDH5 {ECO:0000255|HAMAP-Rule:MF_03057, ECO:0000303|PubMed:19628817};
GN Synonyms=EMI5 {ECO:0000303|PubMed:12586695};
GN OrderedLocusNames=YOL071W {ECO:0000312|SGD:S000005432};
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 FUNCTION.
RX PubMed=12432101; DOI=10.1073/pnas.202604399;
RA Deutschbauer A.M., Williams R.M., Chu A.M., Davis R.W.;
RT "Parallel phenotypic analysis of sporulation and postgermination growth in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15530-15535(2002).
RN [4]
RP FUNCTION.
RX PubMed=12586695; DOI=10.1093/genetics/163.1.47;
RA Enyenihi A.H., Saunders W.S.;
RT "Large-scale functional genomic analysis of sporulation and meiosis in
RT Saccharomyces cerevisiae.";
RL Genetics 163:47-54(2003).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP SDH1.
RX PubMed=19628817; DOI=10.1126/science.1175689;
RA Hao H.-X., Khalimonchuk O., Schraders M., Dephoure N., Bayley J.-P.,
RA Kunst H., Devilee P., Cremers C.W.R.J., Schiffman J.D., Bentz B.G.,
RA Gygi S.P., Winge D.R., Kremer H., Rutter J.;
RT "SDH5, a gene required for flavination of succinate dehydrogenase, is
RT mutated in paraganglioma.";
RL Science 325:1139-1142(2009).
RN [10]
RP STRUCTURE BY NMR OF 1-54, FUNCTION, AND MUTAGENESIS OF ARG-68; TYR-71;
RP 98-GLU-GLU-99 AND TRP-113.
RX PubMed=23062074; DOI=10.1021/bi301171u;
RA Eletsky A., Jeong M.Y., Kim H., Lee H.W., Xiao R., Pagliarini D.J.,
RA Prestegard J.H., Winge D.R., Montelione G.T., Szyperski T.;
RT "Solution NMR structure of yeast succinate dehydrogenase flavinylation
RT factor Sdh5 reveals a putative Sdh1 binding site.";
RL Biochemistry 51:8475-8477(2012).
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. Required for flavinylation (covalent
CC attachment of FAD) of the flavoprotein subunit SDH1 of the SDH
CC catalytic dimer. It is unclear whether it participates in the chemistry
CC of FAD attachment (enzymatic function) or acts as a chaperone that
CC maintains SDH1 in a conformation that is susceptible to autocatalytic
CC FAD attachment (PubMed:19628817). Does not bind FAD or FADH(2) in vitro
CC (PubMed:23062074). Involved in sporulation (PubMed:12432101). Required
CC for the full activation of the early meiotic inducer IME1
CC (PubMed:12586695). {ECO:0000255|HAMAP-Rule:MF_03057,
CC ECO:0000269|PubMed:12432101, ECO:0000269|PubMed:12586695,
CC ECO:0000269|PubMed:19628817, ECO:0000269|PubMed:23062074}.
CC -!- SUBUNIT: Interacts with SDH1 within the SDH catalytic dimer.
CC {ECO:0000255|HAMAP-Rule:MF_03057, ECO:0000269|PubMed:19628817}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03057, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:19628817}.
CC -!- DISRUPTION PHENOTYPE: Respiratory deficient phenotype: viable on
CC glucose medium, but is inviable on non-fermentable carbon sources such
CC as glycerol. Cells lack SDH activity due to a complete loss of FAD
CC cofactor attachment of SDH1. {ECO:0000269|PubMed:19628817}.
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03057}.
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DR EMBL; Z74813; CAA99081.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10712.1; -; Genomic_DNA.
DR PIR; S66764; S66764.
DR RefSeq; NP_014570.1; NM_001183326.1.
DR PDB; 2LM4; NMR; -; A=55-152.
DR PDBsum; 2LM4; -.
DR AlphaFoldDB; Q08230; -.
DR BMRB; Q08230; -.
DR SMR; Q08230; -.
DR BioGRID; 34330; 102.
DR DIP; DIP-61727N; -.
DR IntAct; Q08230; 1.
DR STRING; 4932.YOL071W; -.
DR MaxQB; Q08230; -.
DR PaxDb; Q08230; -.
DR PRIDE; Q08230; -.
DR DNASU; 854083; -.
DR EnsemblFungi; YOL071W_mRNA; YOL071W; YOL071W.
DR GeneID; 854083; -.
DR KEGG; sce:YOL071W; -.
DR SGD; S000005432; SDH5.
DR VEuPathDB; FungiDB:YOL071W; -.
DR eggNOG; KOG3326; Eukaryota.
DR GeneTree; ENSGT00390000001149; -.
DR HOGENOM; CLU_103054_0_1_1; -.
DR InParanoid; Q08230; -.
DR OMA; YGKPQNP; -.
DR BioCyc; YEAST:G3O-33476-MON; -.
DR PRO; PR:Q08230; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08230; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0030437; P:ascospore formation; HMP:SGD.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IMP:UniProtKB.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; HMP:SGD.
DR GO; GO:0017013; P:protein flavinylation; IMP:UniProtKB.
DR GO; GO:0018293; P:protein-FAD linkage; IMP:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IPI:SGD.
DR Gene3D; 1.10.150.250; -; 1.
DR HAMAP; MF_03057; SDHAF2; 1.
DR InterPro; IPR005631; SDH.
DR InterPro; IPR036714; SDH_sf.
DR InterPro; IPR028882; SDHAF2.
DR Pfam; PF03937; Sdh5; 1.
DR SUPFAM; SSF109910; SSF109910; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19837041"
FT CHAIN 36..162
FT /note="Succinate dehydrogenase assembly factor 2,
FT mitochondrial"
FT /id="PRO_0000007814"
FT MUTAGEN 68
FT /note="R->E: Loss of covalent FAD in SDH1."
FT /evidence="ECO:0000269|PubMed:23062074"
FT MUTAGEN 71
FT /note="Y->D: Loss of covalent FAD in SDH1."
FT /evidence="ECO:0000269|PubMed:23062074"
FT MUTAGEN 98..99
FT /note="EE->KK: No effect."
FT /evidence="ECO:0000269|PubMed:23062074"
FT MUTAGEN 113
FT /note="W->A: Loss of covalent FAD in SDH1."
FT /evidence="ECO:0000269|PubMed:23062074"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:2LM4"
FT HELIX 79..95
FT /evidence="ECO:0007829|PDB:2LM4"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2LM4"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:2LM4"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:2LM4"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2LM4"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:2LM4"
SQ SEQUENCE 162 AA; 19042 MW; 8CDF8E943D46A12D CRC64;
MHNMFPALTK TLSLQGYKII NSQTGSAAWS CGRRWFSSDK DDHDDVVTRI KIAPIKRTNE
PLDKKRARLI YQSRKRGILE TDLLLSGFAA KYLKKMNEEE LEEYDSLLNE LDWDIYYWAT
KNFKTSPLPD KWANSKLLKQ LQEFSENKEK EILSMPDLSK YQ
