DHSD_CHICK
ID DHSD_CHICK Reviewed; 157 AA.
AC Q5ZIS0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE Short=CybS;
DE AltName: Full=Succinate dehydrogenase complex subunit D;
DE AltName: Full=Succinate-ubiquinone oxidoreductase cytochrome b small subunit;
DE AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;
DE Flags: Precursor;
GN Name=SDHD; ORFNames=RCJMB04_23p7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 55-157, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15805592; DOI=10.1107/s0907444905000181;
RA Huang L.-S., Borders T.M., Shen J.T., Wang C.-J., Berry E.A.;
RT "Crystallization of mitochondrial respiratory complex II from chicken
RT heart: a membrane-protein complex diffracting to 2.0 A.";
RL Acta Crystallogr. D 61:380-387(2005).
RN [3] {ECO:0007744|PDB:2H88, ECO:0007744|PDB:2H89}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 55-157 IN COMPLEXES WITH
RP UBIQUINONE AND HEME, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16935256; DOI=10.1016/j.bbabio.2006.06.015;
RA Huang L.-S., Shen J.T., Wang A.C., Berry E.A.;
RT "Crystallographic studies of the binding of ligands to the dicarboxylate
RT site of complex II, and the identity of the ligand in the 'oxaloacetate-
RT inhibited' state.";
RL Biochim. Biophys. Acta 1757:1073-1083(2006).
RN [4] {ECO:0007744|PDB:1YQ3, ECO:0007744|PDB:1YQ4, ECO:0007744|PDB:2FBW}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 55-157 IN COMPLEXES WITH
RP UBIQUINONE AND HEME, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16371358; DOI=10.1074/jbc.m511270200;
RA Huang L.-S., Sun G., Cobessi D., Wang A.C., Shen J.T., Tung E.Y.,
RA Anderson V.E., Berry E.A.;
RT "3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration
RT that, upon oxidation by complex II, forms a covalent adduct with a
RT catalytic base arginine in the active site of the enzyme.";
RL J. Biol. Chem. 281:5965-5972(2006).
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).
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Component of complex II composed of four subunits: the
CC flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome
CC b560 composed of SDHC and SDHD. {ECO:0000269|PubMed:15805592,
CC ECO:0000269|PubMed:16371358, ECO:0000269|PubMed:16935256}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
CC ECO:0000269|PubMed:16935256}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15805592, ECO:0000269|PubMed:16371358,
CC ECO:0000269|PubMed:16935256}.
CC -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR EMBL; AJ720714; CAG32373.1; -; mRNA.
DR RefSeq; NP_001006321.1; NM_001006321.1.
DR PDB; 1YQ3; X-ray; 2.20 A; D=55-157.
DR PDB; 1YQ4; X-ray; 2.33 A; D=55-157.
DR PDB; 2FBW; X-ray; 2.10 A; D/Q=55-157.
DR PDB; 2H88; X-ray; 1.74 A; D/Q=55-157.
DR PDB; 2H89; X-ray; 2.40 A; D=55-157.
DR PDB; 2WQY; X-ray; 2.10 A; D/Q=55-157.
DR PDB; 6MYO; X-ray; 2.20 A; D=55-157.
DR PDB; 6MYP; X-ray; 2.10 A; D=55-157.
DR PDB; 6MYQ; X-ray; 1.97 A; D=55-157.
DR PDB; 6MYR; X-ray; 2.15 A; D=55-157.
DR PDB; 6MYS; X-ray; 2.37 A; D=55-157.
DR PDB; 6MYT; X-ray; 2.27 A; D=55-157.
DR PDB; 6MYU; X-ray; 1.97 A; D=55-157.
DR PDBsum; 1YQ3; -.
DR PDBsum; 1YQ4; -.
DR PDBsum; 2FBW; -.
DR PDBsum; 2H88; -.
DR PDBsum; 2H89; -.
DR PDBsum; 2WQY; -.
DR PDBsum; 6MYO; -.
DR PDBsum; 6MYP; -.
DR PDBsum; 6MYQ; -.
DR PDBsum; 6MYR; -.
DR PDBsum; 6MYS; -.
DR PDBsum; 6MYT; -.
DR PDBsum; 6MYU; -.
DR AlphaFoldDB; Q5ZIS0; -.
DR SMR; Q5ZIS0; -.
DR STRING; 9031.ENSGALP00000012780; -.
DR PaxDb; Q5ZIS0; -.
DR GeneID; 419793; -.
DR KEGG; gga:419793; -.
DR CTD; 6392; -.
DR VEuPathDB; HostDB:geneid_419793; -.
DR eggNOG; KOG4097; Eukaryota.
DR InParanoid; Q5ZIS0; -.
DR OrthoDB; 1511215at2759; -.
DR PhylomeDB; Q5ZIS0; -.
DR UniPathway; UPA00223; -.
DR EvolutionaryTrace; Q5ZIS0; -.
DR PRO; PR:Q5ZIS0; -.
DR Proteomes; UP000000539; Unplaced.
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: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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..45
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 46..157
FT /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT small subunit, mitochondrial"
FT /id="PRO_0000343805"
FT TOPO_DOM 46..61
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..83
FT /note="Helical"
FT TOPO_DOM 84..88
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 89..109
FT /note="Helical"
FT TOPO_DOM 110..118
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 119..140
FT /note="Helical"
FT TOPO_DOM 141..157
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT BINDING 100
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_note="ligand shared with SDHC"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:16371358,
FT ECO:0000269|PubMed:16935256, ECO:0007744|PDB:1YQ3,
FT ECO:0007744|PDB:1YQ4, ECO:0007744|PDB:2FBW,
FT ECO:0007744|PDB:2H88, ECO:0007744|PDB:2H89"
FT BINDING 112
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with IP/SDHB"
FT /evidence="ECO:0000269|PubMed:16371358,
FT ECO:0000269|PubMed:16935256"
FT HELIX 59..83
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 87..112
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 116..143
FT /evidence="ECO:0007829|PDB:2H88"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:2H88"
SQ SEQUENCE 157 AA; 16435 MW; C4FE16246BD74AA0 CRC64;
MAALVLLRAG LARPRGVPTA LLRGTLLRHS AVLTAAADRS APARQSHGGA PQGHGSSKAA
SLHWTSERAV SALLLGLLPA AYLYPGPAVD YSLAAALTLH GHWGLGQVIT DYVHGDTPIK
VANTGLYVLS AITFTGLCYF NYYDVGICKA VAMLWSI
