C560_CRIGR
ID C560_CRIGR Reviewed; 169 AA.
AC P70097;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 Flags: Precursor;
GN Name=SDHC;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7592812; DOI=10.1074/jbc.270.44.26104;
RA Oostveen F.G., Au H.C., Meijer P.J., Scheffler I.E.;
RT "A Chinese hamster mutant cell line with a defect in the integral membrane
RT protein CII-3 of complex II of the mitochondrial electron transport
RT chain.";
RL J. Biol. Chem. 270:26104-26108(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). {ECO:0000269|PubMed:7592812}.
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 {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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DR EMBL; U31241; AAB07265.1; -; mRNA.
DR RefSeq; NP_001233755.1; NM_001246826.1.
DR AlphaFoldDB; P70097; -.
DR SMR; P70097; -.
DR STRING; 10029.XP_007645573.1; -.
DR PRIDE; P70097; -.
DR Ensembl; ENSCGRT00001028993; ENSCGRP00001024747; ENSCGRG00001022557.
DR GeneID; 100689402; -.
DR KEGG; cge:100689402; -.
DR CTD; 6391; -.
DR eggNOG; KOG0449; Eukaryota.
DR GeneTree; ENSGT00390000000566; -.
DR OMA; IPGGIPC; -.
DR OrthoDB; 1443173at2759; -.
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: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: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 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..169
FT /note="Succinate dehydrogenase cytochrome b560 subunit,
FT mitochondrial"
FT /id="PRO_0000003633"
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; 18498 MW; 0429BBD8E509885D CRC64;
MAALLLRHVG RHCLRAHLNS QICLRNAVPL GTTAKEEMER FWNKNTSSKR PVSPHLTIYR
WSLPMVMSIC HRGTGVALSG GVSLFGLSAL LLPGNFESYL MFIKSLCLGP ALIHSAKFVL
VFPLMYHSLN GIRHLIWDLG KGLSISQVYQ SGVAVLMLAV LSSVGLAAM