DHSDB_DANRE
ID DHSDB_DANRE Reviewed; 158 AA.
AC Q68FN7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit B, mitochondrial;
DE Short=CybS-B;
DE AltName: Full=Succinate dehydrogenase complex subunit D-B;
DE AltName: Full=Succinate-ubiquinone oxidoreductase cytochrome b small subunit B;
DE AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit B;
DE Flags: Precursor;
GN Name=sdhdb; Synonyms=sdhd, sdhda; ORFNames=zgc:100986;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2004) 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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC079507; AAH79507.1; -; mRNA.
DR RefSeq; NP_001004004.1; NM_001004004.2.
DR AlphaFoldDB; Q68FN7; -.
DR SMR; Q68FN7; -.
DR STRING; 7955.ENSDARP00000039864; -.
DR PaxDb; Q68FN7; -.
DR Ensembl; ENSDART00000039865; ENSDARP00000039864; ENSDARG00000030139.
DR GeneID; 445500; -.
DR KEGG; dre:445500; -.
DR CTD; 445500; -.
DR ZFIN; ZDB-GENE-040822-17; sdhdb.
DR eggNOG; KOG4097; Eukaryota.
DR GeneTree; ENSGT00390000010003; -.
DR HOGENOM; CLU_096618_1_1_1; -.
DR InParanoid; Q68FN7; -.
DR OMA; KLERLWA; -.
DR OrthoDB; 1511215at2759; -.
DR PhylomeDB; Q68FN7; -.
DR TreeFam; TF313310; -.
DR Reactome; R-DRE-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; -.
DR PRO; PR:Q68FN7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 15.
DR Bgee; ENSDARG00000030139; Expressed in heart and 28 other tissues.
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 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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..158
FT /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT small subunit B, mitochondrial"
FT /id="PRO_0000343806"
FT TOPO_DOM 30..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"
SQ SEQUENCE 158 AA; 16973 MW; 02A16CE57C169009 CRC64;
MAALVRISSL CHRGVSPLLF RPSSLIRPLA VQQKDHDCSY LISARIHATP SNYAGSGSKA
ATMHWTGERI LSIALLSLAP VAYFCPSPAV DYSLAAALTL HGHWGLGQVV TDYVHGDAKI
KMANAGLFVL STVTFAGLCY FNYHDVGICK AVALLWSK