DHSD_BOVIN
ID DHSD_BOVIN Reviewed; 158 AA.
AC Q95123; Q3T0U6; Q5UAB3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 134.
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 reductase membrane anchor subunit;
DE Flags: Precursor;
GN Name=SDHD; Synonyms=SDH4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=9211943; DOI=10.1074/jbc.272.28.17867;
RA Shenoy S.K., Yu L., Yu C.-A.;
RT "The smallest membrane anchoring subunit (QPs3) of bovine heart
RT mitochondrial succinate-ubiquinone reductase. Cloning, sequencing,
RT topology, and Q-binding domain.";
RL J. Biol. Chem. 272:17867-17872(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Khatib H.;
RT "Bovine succinate dehydrogenase complex, subunit D, integral membrane
RT protein (SDHD).";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR EMBL; U50987; AAB09426.1; -; mRNA.
DR EMBL; AY770191; AAV41841.1; -; mRNA.
DR EMBL; BC102257; AAI02258.1; -; mRNA.
DR RefSeq; NP_776604.1; NM_174179.2.
DR AlphaFoldDB; Q95123; -.
DR SMR; Q95123; -.
DR CORUM; Q95123; -.
DR IntAct; Q95123; 2.
DR STRING; 9913.ENSBTAP00000021636; -.
DR PaxDb; Q95123; -.
DR PRIDE; Q95123; -.
DR GeneID; 281481; -.
DR KEGG; bta:281481; -.
DR CTD; 6392; -.
DR eggNOG; KOG4097; Eukaryota.
DR InParanoid; Q95123; -.
DR OrthoDB; 1511215at2759; -.
DR TreeFam; TF313310; -.
DR Proteomes; UP000009136; 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-KW.
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_0000006486"
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:0000255"
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 CONFLICT 2
FT /note="A -> AA (in Ref. 3; AAI02258)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="R -> K (in Ref. 1; AAB09426)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 17124 MW; 3661E9BDF0A46F44 CRC64;
MALWRLSVLC GAREGRALFL RTPVVRPALV SAFLQDRPAQ GWCGTQHIHL SPSHHSGSKA
ASLHWTGERV VSVLLLGLIP AAYLNPCSAM DYSLAATLTL HSHWGIGQVV TDYVHGDAVQ
KAAKTGLLVL SAFTFAGLCY FNYHDVGICK AVAMLWKL
