DHSD_SHEEP
ID DHSD_SHEEP Reviewed; 158 AA.
AC Q5G2C6; Q5G2C5; Q5G2C8; Q5G2C9; Q5G2D0; Q5G2D1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 60.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-19; GLN-37; SER-42; LYS-46;
RP ARG-55 AND SER-67.
RC TISSUE=Liver;
RX PubMed=15771746; DOI=10.1111/j.1365-2052.2005.01261.x;
RA Khatib H.;
RT "Characterization and analysis of the imprinting status of the ovine SDHD
RT and COPG2 genes.";
RL Anim. Genet. 36:186-188(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). {ECO:0000250}.
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: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; AY861373; AAW70029.1; -; mRNA.
DR EMBL; AY861374; AAW70030.1; -; mRNA.
DR EMBL; AY861375; AAW70031.1; -; mRNA.
DR EMBL; AY861376; AAW70032.1; -; mRNA.
DR EMBL; AY861377; AAW70033.1; -; mRNA.
DR EMBL; AY861378; AAW70034.1; -; mRNA.
DR EMBL; AY861379; AAW70035.1; -; mRNA.
DR RefSeq; NP_001072121.1; NM_001078653.1.
DR RefSeq; NP_001087250.1; NM_001093781.1.
DR AlphaFoldDB; Q5G2C6; -.
DR SMR; Q5G2C6; -.
DR GeneID; 780442; -.
DR GeneID; 780772; -.
DR KEGG; oas:780442; -.
DR KEGG; oas:780772; -.
DR OrthoDB; 1511215at2759; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000002356; 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: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.
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..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 56..158
FT /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT small subunit, mitochondrial"
FT /id="PRO_0000254579"
FT TOPO_DOM 56..62
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 85..89
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..119
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 120..141
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 142..158
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT BINDING 101
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:0000250|UniProtKB:A5GZW8"
FT BINDING 113
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /ligand_note="ligand shared with IP/SDHB"
FT /evidence="ECO:0000250"
FT VARIANT 19
FT /note="F -> L"
FT /evidence="ECO:0000269|PubMed:15771746"
FT VARIANT 37
FT /note="R -> Q"
FT /evidence="ECO:0000269|PubMed:15771746"
FT VARIANT 42
FT /note="W -> S"
FT /evidence="ECO:0000269|PubMed:15771746"
FT VARIANT 46
FT /note="Q -> K"
FT /evidence="ECO:0000269|PubMed:15771746"
FT VARIANT 55
FT /note="H -> R"
FT /evidence="ECO:0000269|PubMed:15771746"
FT VARIANT 67
FT /note="G -> S"
FT /evidence="ECO:0000269|PubMed:15771746"
SQ SEQUENCE 158 AA; 16995 MW; 246CE987F6937B44 CRC64;
MALSRLSVLC GVREGRALFL RTPVVRPALV SAFLQGRPAQ GWCGTQHIHL SPSHHSGSKA
ASLHWTGERV VSVLLLGLIP AAYLNPCSAM DYSLAATLTL HSHWGIGQVV TDYVHGDAVQ
KAAKTGLLVL SAFTFAGLCY FNYHDVGICK AVAMLWKL
