C560_CAEEL
ID C560_CAEEL Reviewed; 182 AA.
AC P41956;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Succinate dehydrogenase cytochrome b560 subunit, mitochondrial;
DE Flags: Precursor;
GN Name=mev-1; Synonyms=cyt-1; ORFNames=T07C4.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7907274; DOI=10.1016/0092-8674(94)90506-1;
RA Hengartner M.O., Horvitz H.R.;
RT "C. elegans cell survival gene ced-9 encodes a functional homolog of the
RT mammalian proto-oncogene bcl-2.";
RL Cell 76:665-676(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=16091039; DOI=10.1111/j.1365-2958.2005.04739.x;
RA Anyanful A., Dolan-Livengood J.M., Lewis T., Sheth S., Dezalia M.N.,
RA Sherman M.A., Kalman L.V., Benian G.M., Kalman D.;
RT "Paralysis and killing of Caenorhabditis elegans by enteropathogenic
RT Escherichia coli requires the bacterial tryptophanase gene.";
RL Mol. Microbiol. 57:988-1007(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) (By similarity). Mediates resistance to
CC enteropathogenic E.coli infection (PubMed:16091039).
CC {ECO:0000250|UniProtKB:D0VWV4, ECO:0000269|PubMed:16091039}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Component of complex II composed of four subunits: a
CC flavoprotein (FP), iron-sulfur protein (IP), and a cytochrome b560
CC composed of two integral membrane proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Is expressed at a constant level throughout
CC development.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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DR EMBL; L26545; AAA20081.1; -; Genomic_DNA.
DR EMBL; Z29443; CAA82572.1; -; Genomic_DNA.
DR PIR; B53189; B53189.
DR RefSeq; NP_499283.1; NM_066882.5.
DR AlphaFoldDB; P41956; -.
DR SMR; P41956; -.
DR BioGRID; 57058; 4.
DR STRING; 6239.T07C4.7.2; -.
DR EPD; P41956; -.
DR PaxDb; P41956; -.
DR PeptideAtlas; P41956; -.
DR EnsemblMetazoa; T07C4.7a.1; T07C4.7a.1; WBGene00003225.
DR UCSC; T07C4.7.1; c. elegans.
DR WormBase; T07C4.7a; CE00598; WBGene00003225; mev-1.
DR eggNOG; KOG0449; Eukaryota.
DR GeneTree; ENSGT00390000000566; -.
DR HOGENOM; CLU_094691_1_0_1; -.
DR InParanoid; P41956; -.
DR OMA; RISGCVM; -.
DR OrthoDB; 1443173at2759; -.
DR PhylomeDB; P41956; -.
DR Reactome; R-CEL-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; -.
DR PRO; PR:P41956; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003225; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; P41956; 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:0005739; C:mitochondrion; HDA:WormBase.
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:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:WormBase.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IMP:WormBase.
DR GO; GO:1902883; P:negative regulation of response to oxidative stress; IGI:UniProtKB.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:WormBase.
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; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..182
FT /note="Succinate dehydrogenase cytochrome b560 subunit,
FT mitochondrial"
FT /id="PRO_0000003637"
FT TRANSMEM 65..94
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 95..114
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT TRANSMEM 115..139
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 140..147
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250"
FT TRANSMEM 148..169
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 170..172
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with second transmembrane
FT protein subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 182 AA; 19982 MW; 5E3E6DA6B08E4C5F CRC64;
MINIPTAILC RLGARSSISR SFGTSIVTKS EAKTPIQKFG WEYLLKQRSK NRPIAPHLTV
YQPQLTWMLS GFHRISGCVM AGTLLVGGIG FAVLPFDFTA FVDFIRSWNL PCAVTAVFKY
IIAFPIIFHT LNGIRFLGFD LAKGVNNVGQ IYKSGYLVSG LSAILALAIV FNSCQNKSNK
TA
