DHSD_YEAST
ID DHSD_YEAST Reviewed; 181 AA.
AC P37298; D6VSG0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE Short=CybS;
DE AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;
DE Flags: Precursor;
GN Name=SDH4; Synonyms=ACN18; OrderedLocusNames=YDR178W; ORFNames=YD9395.11;
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, AND PROTEIN SEQUENCE OF 32-62.
RC STRAIN=S288c / GRF88;
RX PubMed=8120006; DOI=10.1016/s0021-9258(17)37406-9;
RA Bullis B.L., Lemire B.D.;
RT "Isolation and characterization of the Saccharomyces cerevisiae SDH4 gene
RT encoding a membrane anchor subunit of succinate dehydrogenase.";
RL J. Biol. Chem. 269:6543-6549(1994).
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 MUTAGENESIS OF PHE-100; SER-102 AND HIS-130.
RX PubMed=11279023; DOI=10.1074/jbc.m100184200;
RA Oyedotun K.S., Lemire B.D.;
RT "The quinone-binding sites of the Saccharomyces cerevisiae succinate-
RT ubiquinone oxidoreductase.";
RL J. Biol. Chem. 276:16936-16943(2001).
RN [6]
RP REVIEW ON SUCCINATE DEHYDROGENASE.
RX PubMed=11803020; DOI=10.1016/s0005-2728(01)00229-8;
RA Lemire B.D., Oyedotun K.S.;
RT "The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone
RT oxidoreductase.";
RL Biochim. Biophys. Acta 1553:102-116(2002).
RN [7]
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 [8]
RP MUTAGENESIS OF CYS-109.
RX PubMed=14672930; DOI=10.1074/jbc.m311877200;
RA Oyedotun K.S., Yau P.F., Lemire B.D.;
RT "Identification of the heme axial ligands in the cytochrome b562 of the
RT Saccharomyces cerevisiae succinate dehydrogenase.";
RL J. Biol. Chem. 279:9432-9439(2004).
RN [9]
RP MUTAGENESIS OF TYR-120.
RX PubMed=17208193; DOI=10.1016/j.bbabio.2006.11.017;
RA Silkin Y., Oyedotun K.S., Lemire B.D.;
RT "The role of Sdh4p Tyr-89 in ubiquinone reduction by the Saccharomyces
RT cerevisiae succinate dehydrogenase.";
RL Biochim. Biophys. Acta 1767:143-150(2007).
RN [10]
RP 3D-STRUCTURE MODELING OF 32-181.
RX PubMed=14672929; DOI=10.1074/jbc.m311876200;
RA Oyedotun K.S., Lemire B.D.;
RT "The quaternary structure of the Saccharomyces cerevisiae succinate
RT dehydrogenase. Homology modeling, cofactor docking, and molecular dynamics
RT simulation studies.";
RL J. Biol. Chem. 279:9424-9431(2004).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH)
CC that is involved in system II of the mitochondrial electron transport
CC chain and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). SDH3 and SDH4 form the membrane dimer that
CC anchors the catalytic dimer formed by SDH1 and SDH2 to the matrix
CC surface of the mitochondrial inner membrane. Electrons originating from
CC the catalytic dimer enter the membrane dimer for ubiquinone reduction.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Forms part of complex II containing four subunits: a
CC flavoprotein (FP), an iron-sulfur protein (IP) and a cytochrome b
CC composed of a large and a small subunit.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- MISCELLANEOUS: Present with 7920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR EMBL; L26333; AAA19637.1; -; Unassigned_RNA.
DR EMBL; Z46727; CAA86683.1; -; Genomic_DNA.
DR EMBL; AY557671; AAS55997.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12020.1; -; Genomic_DNA.
DR PIR; A54380; A54380.
DR RefSeq; NP_010463.1; NM_001180485.1.
DR AlphaFoldDB; P37298; -.
DR SMR; P37298; -.
DR BioGRID; 32231; 98.
DR ComplexPortal; CPX-565; Mitochondrial respiratory chain complex II.
DR DIP; DIP-5704N; -.
DR IntAct; P37298; 4.
DR MINT; P37298; -.
DR STRING; 4932.YDR178W; -.
DR ChEMBL; CHEMBL3308955; -.
DR iPTMnet; P37298; -.
DR MaxQB; P37298; -.
DR PaxDb; P37298; -.
DR PRIDE; P37298; -.
DR EnsemblFungi; YDR178W_mRNA; YDR178W; YDR178W.
DR GeneID; 851758; -.
DR KEGG; sce:YDR178W; -.
DR SGD; S000002585; SDH4.
DR VEuPathDB; FungiDB:YDR178W; -.
DR eggNOG; KOG4097; Eukaryota.
DR GeneTree; ENSGT00940000176639; -.
DR HOGENOM; CLU_096618_0_0_1; -.
DR InParanoid; P37298; -.
DR OMA; EFNSCIT; -.
DR BioCyc; MetaCyc:YDR178W-MON; -.
DR BioCyc; YEAST:YDR178W-MON; -.
DR UniPathway; UPA00223; -.
DR PRO; PR:P37298; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P37298; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR GO; GO:0045333; P:cellular respiration; IMP:SGD.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IDA:ComplexPortal.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:ComplexPortal.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:ComplexPortal.
DR CDD; cd03496; SQR_TypeC_CybS; 1.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR007992; CybS.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR13337; PTHR13337; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Quinone;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8120006"
FT CHAIN 32..181
FT /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT small subunit, mitochondrial"
FT /id="PRO_0000006496"
FT TOPO_DOM 32..66
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..98
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..127
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..181
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 109
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 120
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with IP/SDHB"
FT /evidence="ECO:0000250"
FT MUTAGEN 100
FT /note="F->V: Impairs respiratory growth and reduces quinone
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:11279023"
FT MUTAGEN 102
FT /note="S->A: Impairs respiratory growth and reduces quinone
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:11279023"
FT MUTAGEN 109
FT /note="C->A: Decreases SDH cytochrome b content."
FT /evidence="ECO:0000269|PubMed:14672930"
FT MUTAGEN 120
FT /note="Y->C: Abolishes quinone reductase activity. Little
FT effect on complex assembly."
FT /evidence="ECO:0000269|PubMed:17208193"
FT MUTAGEN 130
FT /note="H->L: Reduces SDH FAD content. Probably impairs
FT complex assembly."
FT /evidence="ECO:0000269|PubMed:11279023"
SQ SEQUENCE 181 AA; 20249 MW; 80D76A32E7E6DA70 CRC64;
MMLPRSMKFM TGRRIFHTAT VRAFQSTAKK SLTIPFLPVL PQKPGGVRGT PNDAYVPPPE
NKLEGSYHWY MEKIFALSVV PLATTAMLTT GPLSTAADSF FSVMLLGYCY MEFNSCITDY
ISERVYGVWH KYAMYMLGLG SAVSLFGIYK LETENDGVVG LVKSLWDSSE KDNSQKIEAK
K
