DHSD_ASCSU
ID DHSD_ASCSU Reviewed; 156 AA.
AC P92507;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE Short=CybS;
DE AltName: Full=Cytochrome b558 small subunit;
DE AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;
DE Flags: Precursor;
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RX PubMed=8764887; DOI=10.1016/0005-2728(96)00070-9;
RA Saruta F., Hirawake H., Takamiya S., Ma Y.-C., Aoki T., Sekimizu K.,
RA Kojima S., Kita K.;
RT "Cloning of a cDNA encoding the small subunit of cytochrome b558 (cybS) of
RT mitochondrial fumarate reductase (complex II) from adult Ascaris suum.";
RL Biochim. Biophys. Acta 1276:1-5(1996).
RN [2]
RP PROTEIN SEQUENCE OF 26-55.
RA Kita K., Takamiya S., Furushima R., Suzuki H., Ozawa T., Oya H.;
RL (In) Lenaz G., Barnabei O., Rabbi A., Battino M. (eds.);
RL Highlights in Ubiquinone Research, pp.174-177, Taylor and Francis, London
RL (1990).
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; D78158; BAA11233.1; -; mRNA.
DR PDB; 3VR8; X-ray; 2.81 A; D/H=1-156.
DR PDB; 3VR9; X-ray; 3.01 A; D/H=1-156.
DR PDB; 3VRA; X-ray; 3.44 A; D/H=1-156.
DR PDB; 3VRB; X-ray; 2.91 A; D/H=1-156.
DR PDB; 4YSX; X-ray; 2.25 A; D/H=1-156.
DR PDB; 4YSY; X-ray; 3.10 A; D/H=1-156.
DR PDB; 4YSZ; X-ray; 3.30 A; D/H=1-156.
DR PDB; 4YT0; X-ray; 3.66 A; D/H=1-156.
DR PDB; 4YTM; X-ray; 3.40 A; D/H=1-156.
DR PDB; 4YTN; X-ray; 3.00 A; D/H=1-156.
DR PDB; 5C2T; X-ray; 2.75 A; D/H=1-156.
DR PDB; 5C3J; X-ray; 2.80 A; D/H=1-156.
DR PDBsum; 3VR8; -.
DR PDBsum; 3VR9; -.
DR PDBsum; 3VRA; -.
DR PDBsum; 3VRB; -.
DR PDBsum; 4YSX; -.
DR PDBsum; 4YSY; -.
DR PDBsum; 4YSZ; -.
DR PDBsum; 4YT0; -.
DR PDBsum; 4YTM; -.
DR PDBsum; 4YTN; -.
DR PDBsum; 5C2T; -.
DR PDBsum; 5C3J; -.
DR AlphaFoldDB; P92507; -.
DR SMR; P92507; -.
DR EnsemblMetazoa; AgR001_g147_t01; AgR001_g147_t01; AgR001_g147.
DR EnsemblMetazoa; AgR001_g147_t02; AgR001_g147_t02; AgR001_g147.
DR BioCyc; MetaCyc:MON-18286; -.
DR BRENDA; 1.3.5.4; 474.
DR SABIO-RK; P92507; -.
DR UniPathway; UPA00223; -.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 26..156
FT /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT small subunit, mitochondrial"
FT /id="PRO_0000006490"
FT TOPO_DOM 26..57
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 79..83
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 105..117
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 118..139
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 140..156
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT BINDING 95
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 107
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with IP"
FT /evidence="ECO:0000250"
FT TURN 42..48
FT /evidence="ECO:0007829|PDB:4YSX"
FT HELIX 56..78
FT /evidence="ECO:0007829|PDB:4YSX"
FT HELIX 82..107
FT /evidence="ECO:0007829|PDB:4YSX"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:4YSX"
FT HELIX 115..142
FT /evidence="ECO:0007829|PDB:4YSX"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:4YSX"
SQ SEQUENCE 156 AA; 16996 MW; 6515299AF6CFA93F CRC64;
MLSAVRRAIP LSARILRTSL IQRCAGATSA AVTGAAPPQF DPIAAEKGFK PLHSHGTLFK
IERYFAAAMV PLIPAAYFIH GREMDLCLAL ALTLHVHWGV WGVVNDYGRP FVLGDTLAAA
VRVGAYIFTA CLLAGLLYFN EHDVGLTRAF EMVWEL
