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DHSD_DROME
ID   DHSD_DROME              Reviewed;         182 AA.
AC   Q9VCI5;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE            Short=CybS;
DE   AltName: Full=Succinate dehydrogenase complex subunit D {ECO:0000312|FlyBase:FBgn0039112};
DE   AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;
DE   Flags: Precursor;
GN   Name=SdhD {ECO:0000312|FlyBase:FBgn0039112};
GN   ORFNames=CG10219 {ECO:0000312|FlyBase:FBgn0039112};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH)
CC       that is involved in complex II of the mitochondrial electron transport
CC       chain and is responsible for transferring electrons from succinate to
CC       ubiquinone (coenzyme Q). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR   EMBL; AE014297; AAF56180.1; -; Genomic_DNA.
DR   EMBL; AY071388; AAL49010.1; -; mRNA.
DR   EMBL; AY071617; AAL49239.1; -; mRNA.
DR   RefSeq; NP_651181.1; NM_142924.3.
DR   AlphaFoldDB; Q9VCI5; -.
DR   SMR; Q9VCI5; -.
DR   BioGRID; 67746; 6.
DR   IntAct; Q9VCI5; 5.
DR   STRING; 7227.FBpp0083857; -.
DR   PaxDb; Q9VCI5; -.
DR   PRIDE; Q9VCI5; -.
DR   DNASU; 42808; -.
DR   EnsemblMetazoa; FBtr0084466; FBpp0083857; FBgn0039112.
DR   GeneID; 42808; -.
DR   KEGG; dme:Dmel_CG10219; -.
DR   UCSC; CG10219-RA; d. melanogaster.
DR   CTD; 6392; -.
DR   FlyBase; FBgn0039112; SdhD.
DR   VEuPathDB; VectorBase:FBgn0039112; -.
DR   eggNOG; KOG4097; Eukaryota.
DR   GeneTree; ENSGT00390000010003; -.
DR   HOGENOM; CLU_096618_1_0_1; -.
DR   InParanoid; Q9VCI5; -.
DR   OMA; KAFEMIW; -.
DR   OrthoDB; 1511215at2759; -.
DR   PhylomeDB; Q9VCI5; -.
DR   Reactome; R-DME-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; -.
DR   BioGRID-ORCS; 42808; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 42808; -.
DR   PRO; PR:Q9VCI5; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0039112; Expressed in mouthpart and 24 other tissues.
DR   Genevisible; Q9VCI5; DM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:FlyBase.
DR   GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR   GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
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.
DR   SUPFAM; SSF81343; SSF81343; 1.
PE   2: Evidence at transcript level;
KW   Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transmembrane; Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..182
FT                   /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT                   small subunit, mitochondrial"
FT                   /id="PRO_0000006492"
FT   TOPO_DOM        1..71
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..101
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..135
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..182
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   BINDING         113
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_note="ligand shared with large subunit"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         125
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /ligand_note="ligand shared with IP"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   182 AA;  19300 MW;  53E26354C9CC35BA CRC64;
     MSLSLLLRGA VRCNAANLVK SARITPLKSY STLVANVQRK AVVQPLAVAK IVAPVVREIS
     VSAPRMASAG SSHTLLWTVE RIVSAGLLAV IPAAFIAPSQ VLDALMAISV VIHTHWGVEA
     MVVDYMRPSV VGNVLPKVAH IALIIISVAT LGGLFYFIQN DVGLANGIKR FWAIKGKDAE
     KA
 
 
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