C560_BOVIN
ID C560_BOVIN Reviewed; 169 AA.
AC P35720; Q1JP77; Q3T194; Q9T2T6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Succinate dehydrogenase cytochrome b560 subunit, mitochondrial;
DE AltName: Full=Integral membrane protein CII-3;
DE AltName: Full=QPs-1;
DE Short=QPs1;
DE AltName: Full=Succinate dehydrogenase complex subunit C;
DE Flags: Precursor;
GN Name=SDHC; Synonyms=CYB560;
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], AND PROTEIN SEQUENCE OF 30-36.
RC TISSUE=Heart;
RX PubMed=7947903; DOI=10.1016/0005-2728(94)90035-3;
RA Cochran B., Capaldi R.A., Ackrell B.A.;
RT "The cDNA sequence of beef heart CII-3, a membrane-intrinsic subunit of
RT succinate-ubiquinone oxidoreductase.";
RL Biochim. Biophys. Acta 1188:162-166(1994).
RN [2]
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.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-169.
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 38-169.
RC TISSUE=Heart;
RX PubMed=1447196; DOI=10.1016/s0021-9258(18)35794-6;
RA Yu L., Wei Y.-Y., Usui S., Yu C.-A.;
RT "Cytochrome b560 (QPs1) of mitochondrial succinate-ubiquinone reductase.
RT Immunochemistry, cloning, and nucleotide sequencing.";
RL J. Biol. Chem. 267:24508-24515(1992).
RN [5]
RP PROTEIN SEQUENCE OF 30-169.
RC TISSUE=Heart;
RX PubMed=7890754; DOI=10.1074/jbc.270.11.6193;
RA Lee G.Y., He D.Y., Yu L., Yu C.A.;
RT "Identification of the ubiquinone-binding domain in QPs1 of succinate-
RT ubiquinone reductase.";
RL J. Biol. Chem. 270:6193-6198(1995).
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 -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:D0VWV4};
CC Note=The heme b is bound between the two transmembrane subunits SDHC
CC and SDHD. {ECO:0000250|UniProtKB:D0VWV4};
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.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the cytochrome b560 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; S74803; AAB32390.1; -; mRNA.
DR EMBL; BC102062; AAI02063.1; -; mRNA.
DR EMBL; BT025477; ABF57433.1; -; mRNA.
DR EMBL; M76747; AAA21608.1; -; mRNA.
DR PIR; A45159; A45159.
DR RefSeq; NP_787008.1; NM_175814.3.
DR AlphaFoldDB; P35720; -.
DR SMR; P35720; -.
DR CORUM; P35720; -.
DR IntAct; P35720; 4.
DR STRING; 9913.ENSBTAP00000021075; -.
DR PaxDb; P35720; -.
DR PeptideAtlas; P35720; -.
DR PRIDE; P35720; -.
DR Ensembl; ENSBTAT00000021075; ENSBTAP00000021075; ENSBTAG00000015853.
DR GeneID; 327696; -.
DR KEGG; bta:327696; -.
DR CTD; 6391; -.
DR VEuPathDB; HostDB:ENSBTAG00000015853; -.
DR VGNC; VGNC:34392; SDHC.
DR eggNOG; KOG0449; Eukaryota.
DR GeneTree; ENSGT00390000000566; -.
DR HOGENOM; CLU_094691_1_1_1; -.
DR InParanoid; P35720; -.
DR OMA; IPGGIPC; -.
DR OrthoDB; 1443173at2759; -.
DR TreeFam; TF313317; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000015853; Expressed in supraspinatus muscle and 106 other tissues.
DR ExpressionAtlas; P35720; baseline.
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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR018495; Succ_DH_cyt_bsu_CS.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR PANTHER; PTHR10978; PTHR10978; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1.
DR PROSITE; PS01000; SDH_CYT_1; 1.
DR PROSITE; PS01001; SDH_CYT_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7890754,
FT ECO:0000269|PubMed:7947903"
FT CHAIN 30..169
FT /note="Succinate dehydrogenase cytochrome b560 subunit,
FT mitochondrial"
FT /id="PRO_0000003632"
FT TOPO_DOM 30..62
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 63..92
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 93..112
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 113..137
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 138..144
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 145..166
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 167..169
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_note="ligand shared with SDHD"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:D0VWV4"
SQ SEQUENCE 169 AA; 18389 MW; CC2CFAD4380C4E27 CRC64;
MAALLLRHVG RHCLRAHLSP QLCIRNAVPL GTTAKEEMER FWSKNTTLNR PLSPHISIYG
WSLPMAMSIC HRGTGIALSA GVSLFGLSAL LVPGSFESHL EFVKSLCLGP ALIHTAKFAL
VFPLMYHTWN GIRHLMWDLG KGLTISQLHQ SGVAVLVLTV LSSVGLAAM
