C560_CAEBR
ID C560_CAEBR Reviewed; 184 AA.
AC P41955; A8WL36;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Succinate dehydrogenase cytochrome b560 subunit, mitochondrial;
DE Flags: Precursor;
GN Name=mev-1; Synonyms=cyt-1; ORFNames=CBG24607;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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). Mediates resistance to enteropathogenic E.coli
CC infection (By similarity). {ECO:0000250|UniProtKB:D0VWV4,
CC ECO:0000250|UniProtKB:P41956}.
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 transmembrane 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; L26546; AAA20078.1; -; Unassigned_DNA.
DR EMBL; HE601354; CAP21181.1; -; Genomic_DNA.
DR RefSeq; XP_002641307.1; XM_002641261.1.
DR AlphaFoldDB; P41955; -.
DR SMR; P41955; -.
DR STRING; 6238.CBG24607; -.
DR EnsemblMetazoa; CBG24607.1; CBG24607.1; WBGene00042677.
DR GeneID; 8583299; -.
DR KEGG; cbr:CBG_24607; -.
DR CTD; 8583299; -.
DR WormBase; CBG24607; CBP12971; WBGene00042677; Cbr-mev-1.
DR eggNOG; KOG0449; Eukaryota.
DR HOGENOM; CLU_094691_1_0_1; -.
DR InParanoid; P41955; -.
DR OMA; RISGCVM; -.
DR OrthoDB; 1443173at2759; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000008549; Chromosome III.
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:0050829; P:defense response to Gram-negative bacterium; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:0045087; P:innate immune response; IEA:EnsemblMetazoa.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR GO; GO:1902883; P:negative regulation of response to oxidative stress; IEA:EnsemblMetazoa.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IEA:EnsemblMetazoa.
DR GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblMetazoa.
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 ?..184
FT /note="Succinate dehydrogenase cytochrome b560 subunit,
FT mitochondrial"
FT /id="PRO_0000003636"
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 subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 184 AA; 20244 MW; C1F14CB9E7BA8E5D CRC64;
MINIPTSILC RLGARSAISR SFGTSVVTKS EAKTPIQKFG WEYLKKQRDM KRPIAPHLTI
YQPQLTWMLS GFHRISGCVM AGTLLVGGLG FAVLPLDFTT FVEYIRGWNL PCAVTAVFKY
IIAFPIIFHT LNGIRFLGFD LAKGVDNIGQ VYKSGWLVFG VSAVIALAIV INSCQNKSKA
VKTA
