DHSD_PIG
ID DHSD_PIG Reviewed; 159 AA.
AC A5GZW8; A7E1T4; A7E1T8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE Short=CybS;
DE AltName: Full=CII-4;
DE AltName: Full=QPs3;
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Longissimus dorsi muscle;
RX PubMed=17651329; DOI=10.1111/j.1439-0388.2007.00667.x;
RA Guimaraes S.E.F., Rothschild M.F., Ciobanu D., Stahl C.H., Lonergan S.M.;
RT "SNP discovery, expression and association analysis for the SDHD gene in
RT pigs.";
RL J. Anim. Breed. Genet. 124:246-253(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Longissimus dorsi muscle;
RA Zhu Z., Li K., Zhao S.;
RT "Molecular cloning, characterizations and expression profiles of porcine
RT CAV3 gene.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 57-159 IN COMPLEXES WITH HEME AND
RP UBIQUINONE, AND SUBUNIT.
RX PubMed=15989954; DOI=10.1016/j.cell.2005.05.025;
RA Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z.;
RT "Crystal structure of mitochondrial respiratory membrane protein complex
RT II.";
RL Cell 121:1043-1057(2005).
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:15989954}.
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; DQ486897; ABF29393.1; -; mRNA.
DR EMBL; AY682832; AAW29970.1; -; mRNA.
DR EMBL; AY682219; AAW30631.1; -; mRNA.
DR EMBL; AY682222; AAW30633.1; -; mRNA.
DR RefSeq; NP_001090985.1; NM_001097516.1.
DR PDB; 1ZOY; X-ray; 2.40 A; D=57-159.
DR PDB; 1ZP0; X-ray; 3.50 A; D=57-159.
DR PDB; 3ABV; X-ray; 3.24 A; D=57-159.
DR PDB; 3AE1; X-ray; 3.14 A; D=57-159.
DR PDB; 3AE2; X-ray; 3.10 A; D=57-159.
DR PDB; 3AE3; X-ray; 3.35 A; D=57-159.
DR PDB; 3AE4; X-ray; 2.91 A; D=57-159.
DR PDB; 3AE5; X-ray; 3.41 A; D=57-159.
DR PDB; 3AE6; X-ray; 3.40 A; D=57-159.
DR PDB; 3AE7; X-ray; 3.62 A; D=57-159.
DR PDB; 3AE8; X-ray; 3.40 A; D=57-159.
DR PDB; 3AE9; X-ray; 3.31 A; D=57-159.
DR PDB; 3AEA; X-ray; 3.39 A; D=57-159.
DR PDB; 3AEB; X-ray; 3.00 A; D=57-159.
DR PDB; 3AEC; X-ray; 3.61 A; D=57-159.
DR PDB; 3AED; X-ray; 3.52 A; D=57-159.
DR PDB; 3AEE; X-ray; 3.22 A; D=57-159.
DR PDB; 3AEF; X-ray; 2.80 A; D=57-159.
DR PDB; 3AEG; X-ray; 3.27 A; D=57-159.
DR PDB; 3SFD; X-ray; 2.61 A; D=57-159.
DR PDB; 3SFE; X-ray; 2.81 A; D=57-159.
DR PDB; 4YTP; X-ray; 3.10 A; D=1-159.
DR PDB; 4YXD; X-ray; 3.00 A; D=1-159.
DR PDBsum; 1ZOY; -.
DR PDBsum; 1ZP0; -.
DR PDBsum; 3ABV; -.
DR PDBsum; 3AE1; -.
DR PDBsum; 3AE2; -.
DR PDBsum; 3AE3; -.
DR PDBsum; 3AE4; -.
DR PDBsum; 3AE5; -.
DR PDBsum; 3AE6; -.
DR PDBsum; 3AE7; -.
DR PDBsum; 3AE8; -.
DR PDBsum; 3AE9; -.
DR PDBsum; 3AEA; -.
DR PDBsum; 3AEB; -.
DR PDBsum; 3AEC; -.
DR PDBsum; 3AED; -.
DR PDBsum; 3AEE; -.
DR PDBsum; 3AEF; -.
DR PDBsum; 3AEG; -.
DR PDBsum; 3SFD; -.
DR PDBsum; 3SFE; -.
DR PDBsum; 4YTP; -.
DR PDBsum; 4YXD; -.
DR AlphaFoldDB; A5GZW8; -.
DR SMR; A5GZW8; -.
DR STRING; 9823.ENSSSCP00000015958; -.
DR BindingDB; A5GZW8; -.
DR ChEMBL; CHEMBL2366564; -.
DR PaxDb; A5GZW8; -.
DR PeptideAtlas; A5GZW8; -.
DR GeneID; 100048954; -.
DR KEGG; ssc:100048954; -.
DR CTD; 6392; -.
DR eggNOG; KOG4097; Eukaryota.
DR InParanoid; A5GZW8; -.
DR OrthoDB; 1511215at2759; -.
DR UniPathway; UPA00223; -.
DR EvolutionaryTrace; A5GZW8; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048039; F:ubiquinone binding; IDA: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.
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..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..159
FT /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT small subunit, mitochondrial"
FT /id="PRO_0000343804"
FT TOPO_DOM 37..63
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..85
FT /note="Helical"
FT TOPO_DOM 86..90
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 91..111
FT /note="Helical"
FT TOPO_DOM 112..120
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..142
FT /note="Helical"
FT TOPO_DOM 143..159
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT BINDING 102
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:15989954,
FT ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0"
FT BINDING 114
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with IP/SDHB"
FT /evidence="ECO:0000269|PubMed:15989954"
FT CONFLICT 123
FT /note="V -> A (in Ref. 1; AAW29970 and 2; ABF29393)"
FT /evidence="ECO:0000305"
FT HELIX 61..85
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 89..114
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 118..144
FT /evidence="ECO:0007829|PDB:1ZOY"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1ZOY"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:1ZOY"
SQ SEQUENCE 159 AA; 17005 MW; 9D70540010B0F8E3 CRC64;
MATLWRLSVL CGARGGGALV LRTSVVRPAH VSAFLQDRHT PGWCGVQHIH LSPSHQASSK
AASLHWTGER VVSVLLLGLL PAAYLNPCSA MDYSLAAALT LHGHWGIGQV VTDYVRGDAL
QKVAKAGLLA LSAFTFAGLC YFNYHDVGIC KAVAMLWKL
