C560_HUMAN
ID C560_HUMAN Reviewed; 169 AA.
AC Q99643; O75609; Q3C259; Q3C2D8; Q3C2H4; Q5VTH3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 206.
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 AltName: Full=Succinate-ubiquinone oxidoreductase cytochrome B large subunit;
DE Short=CYBL;
DE Flags: Precursor;
GN Name=SDHC; Synonyms=CYB560, SDH3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Au H.C., Raval P.J., Scheffler I.E.;
RT "The cDNA sequence of human CII-3, an integral membrane protein subunit of
RT complex II of the mitochondria electron transport chain.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9533030; DOI=10.1159/000134700;
RA Hirawake H., Taniwaki M., Tamura A., Kojima S., Kita K.;
RT "Cytochrome b in human complex II (succinate-ubiquinone oxidoreductase):
RT cDNA cloning of the components in liver mitochondria and chromosome
RT assignment of the genes for the large (SDHC) and small (SDHD) subunits to
RT 1q21 and 11q23.";
RL Cytogenet. Cell Genet. 79:132-138(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9714607; DOI=10.1016/s0378-1119(98)00186-3;
RA Elbehti-Green A., Au H.C., Mascarello J.T., Ream-Robinson D.,
RA Scheffler I.E.;
RT "Characterization of the human SDHC gene encoding one of the integral
RT membrane proteins of succinate-quinone oxidoreductase in mitochondria.";
RL Gene 213:133-140(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Peripheral blood;
RX PubMed=9851882; DOI=10.1006/mgme.1998.2752;
RA Wohllk N., Thomas P.M., Huang E., Cote G.J.;
RT "A human succinate-ubiquinone oxidoreductase CII-3 subunit gene ending in a
RT polymorphic dinucleotide repeat is located within the sulfonylurea receptor
RT (SUR) gene.";
RL Mol. Genet. Metab. 65:187-190(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
RA Hiatomi H., Kitano S., Kawano K., Hibi N.;
RT "Homo sapiens succinate dehydrogenase complex, subunit C mRNA, alternative
RT splicing variants.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Mammary gland, and Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INVOLVEMENT IN PGL3.
RX PubMed=11062460; DOI=10.1038/81551;
RA Niemann S., Mueller U.;
RT "Mutations in SDHC cause autosomal dominant paraganglioma, type 3.";
RL Nat. Genet. 26:268-270(2000).
RN [11]
RP INVOLVEMENT IN PGGSS.
RX PubMed=17804857; DOI=10.1056/nejmc071191;
RA McWhinney S.R., Pasini B., Stratakis C.A.;
RT "Familial gastrointestinal stromal tumors and germ-line mutations.";
RL N. Engl. J. Med. 357:1054-1056(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 -!- INTERACTION:
CC Q99643; Q92993: KAT5; NbExp=3; IntAct=EBI-1224539, EBI-399080;
CC Q99643; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1224539, EBI-11742507;
CC Q99643; P17252: PRKCA; NbExp=3; IntAct=EBI-1224539, EBI-1383528;
CC Q99643; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1224539, EBI-9090795;
CC Q99643; P61981: YWHAG; NbExp=3; IntAct=EBI-1224539, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q99643-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99643-2; Sequence=VSP_041383;
CC Name=3; Synonyms=CII-3b;
CC IsoId=Q99643-3; Sequence=VSP_041382;
CC Name=4;
CC IsoId=Q99643-4; Sequence=VSP_041382, VSP_041383;
CC Name=5;
CC IsoId=Q99643-5; Sequence=VSP_041381;
CC -!- DISEASE: Paragangliomas 3 (PGL3) [MIM:605373]: A neural crest tumor
CC usually derived from the chromoreceptor tissue of a paraganglion.
CC Paragangliomas can develop at various body sites, including the head,
CC neck, thorax and abdomen. Most commonly, they are located in the head
CC and neck region, specifically at the carotid bifurcation, the jugular
CC foramen, the vagal nerve, and in the middle ear.
CC {ECO:0000269|PubMed:11062460}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Paraganglioma and gastric stromal sarcoma (PGGSS)
CC [MIM:606864]: Gastrointestinal stromal tumors may be sporadic or
CC inherited in an autosomal dominant manner, alone or as a component of a
CC syndrome associated with other tumors, such as in the context of
CC neurofibromatosis type 1 (NF1). Patients have both gastrointestinal
CC stromal tumors and paragangliomas. Susceptibility to the tumors was
CC inherited in an apparently autosomal dominant manner, with incomplete
CC penetrance. {ECO:0000269|PubMed:17804857}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SDHCID389.html";
CC -!- WEB RESOURCE: Name=TCA Cycle Gene Mutation Database;
CC URL="https://databases.lovd.nl/shared/genes/SDHC";
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DR EMBL; U57877; AAB41838.1; -; mRNA.
DR EMBL; D49737; BAA31998.1; -; mRNA.
DR EMBL; AF039594; AAC27993.1; -; Genomic_DNA.
DR EMBL; AF039589; AAC27993.1; JOINED; Genomic_DNA.
DR EMBL; AF039590; AAC27993.1; JOINED; Genomic_DNA.
DR EMBL; AF039591; AAC27993.1; JOINED; Genomic_DNA.
DR EMBL; AF039592; AAC27993.1; JOINED; Genomic_DNA.
DR EMBL; AF039593; AAC27993.1; JOINED; Genomic_DNA.
DR EMBL; AF081495; AAC31940.1; -; Genomic_DNA.
DR EMBL; AB201252; BAE46977.1; -; mRNA.
DR EMBL; AB211234; BAE46978.1; -; mRNA.
DR EMBL; AB211235; BAE46979.1; -; mRNA.
DR EMBL; AB212048; BAE46980.1; -; mRNA.
DR EMBL; AK294305; BAG57586.1; -; mRNA.
DR EMBL; AL592295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52600.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52604.1; -; Genomic_DNA.
DR EMBL; BC020808; AAH20808.1; -; mRNA.
DR EMBL; BC033626; AAH33626.1; -; mRNA.
DR EMBL; BC066329; AAH66329.1; -; mRNA.
DR CCDS; CCDS1230.1; -. [Q99643-1]
DR CCDS; CCDS41431.1; -. [Q99643-2]
DR CCDS; CCDS41432.1; -. [Q99643-5]
DR CCDS; CCDS44263.1; -. [Q99643-3]
DR CCDS; CCDS60330.1; -. [Q99643-4]
DR RefSeq; NP_001030588.1; NM_001035511.1. [Q99643-2]
DR RefSeq; NP_001030589.1; NM_001035512.1. [Q99643-3]
DR RefSeq; NP_001030590.1; NM_001035513.1. [Q99643-5]
DR RefSeq; NP_001265101.1; NM_001278172.1. [Q99643-4]
DR RefSeq; NP_002992.1; NM_003001.3. [Q99643-1]
DR AlphaFoldDB; Q99643; -.
DR SMR; Q99643; -.
DR BioGRID; 112292; 44.
DR ComplexPortal; CPX-561; Mitochondrial respiratory chain complex II.
DR IntAct; Q99643; 15.
DR MINT; Q99643; -.
DR STRING; 9606.ENSP00000356953; -.
DR DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR DrugBank; DB00139; Succinic acid.
DR DrugBank; DB08689; Ubiquinone Q1.
DR TCDB; 3.D.10.1.7; the prokaryotic succinate dehydrogenase (sdh) family.
DR iPTMnet; Q99643; -.
DR PhosphoSitePlus; Q99643; -.
DR SwissPalm; Q99643; -.
DR BioMuta; SDHC; -.
DR DMDM; 5915811; -.
DR EPD; Q99643; -.
DR jPOST; Q99643; -.
DR MassIVE; Q99643; -.
DR MaxQB; Q99643; -.
DR PaxDb; Q99643; -.
DR PeptideAtlas; Q99643; -.
DR PRIDE; Q99643; -.
DR ProteomicsDB; 78373; -. [Q99643-1]
DR ProteomicsDB; 78374; -. [Q99643-2]
DR ProteomicsDB; 78375; -. [Q99643-3]
DR ProteomicsDB; 78376; -. [Q99643-4]
DR ProteomicsDB; 78377; -. [Q99643-5]
DR TopDownProteomics; Q99643-1; -. [Q99643-1]
DR Antibodypedia; 34309; 194 antibodies from 26 providers.
DR DNASU; 6391; -.
DR Ensembl; ENST00000342751.8; ENSP00000356952.3; ENSG00000143252.16. [Q99643-2]
DR Ensembl; ENST00000367975.7; ENSP00000356953.3; ENSG00000143252.16. [Q99643-1]
DR Ensembl; ENST00000392169.6; ENSP00000376009.2; ENSG00000143252.16. [Q99643-5]
DR Ensembl; ENST00000432287.6; ENSP00000390558.2; ENSG00000143252.16. [Q99643-3]
DR Ensembl; ENST00000513009.5; ENSP00000423260.1; ENSG00000143252.16. [Q99643-4]
DR GeneID; 6391; -.
DR KEGG; hsa:6391; -.
DR MANE-Select; ENST00000367975.7; ENSP00000356953.3; NM_003001.5; NP_002992.1.
DR UCSC; uc001gag.4; human. [Q99643-1]
DR CTD; 6391; -.
DR DisGeNET; 6391; -.
DR GeneCards; SDHC; -.
DR GeneReviews; SDHC; -.
DR HGNC; HGNC:10682; SDHC.
DR HPA; ENSG00000143252; Low tissue specificity.
DR MalaCards; SDHC; -.
DR MIM; 602413; gene.
DR MIM; 605373; phenotype.
DR MIM; 606864; phenotype.
DR neXtProt; NX_Q99643; -.
DR OpenTargets; ENSG00000143252; -.
DR Orphanet; 97286; Carney-Stratakis syndrome.
DR Orphanet; 201; Cowden syndrome.
DR Orphanet; 44890; Gastrointestinal stromal tumor.
DR Orphanet; 29072; Hereditary pheochromocytoma-paraganglioma.
DR PharmGKB; PA35607; -.
DR VEuPathDB; HostDB:ENSG00000143252; -.
DR eggNOG; KOG0449; Eukaryota.
DR GeneTree; ENSGT00390000000566; -.
DR HOGENOM; CLU_094691_1_1_1; -.
DR InParanoid; Q99643; -.
DR OMA; IPGGIPC; -.
DR OrthoDB; 507784at2759; -.
DR PhylomeDB; Q99643; -.
DR TreeFam; TF313317; -.
DR BioCyc; MetaCyc:HS07014-MON; -.
DR BRENDA; 1.3.5.1; 2681.
DR PathwayCommons; Q99643; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR SignaLink; Q99643; -.
DR SIGNOR; Q99643; -.
DR UniPathway; UPA00223; -.
DR BioGRID-ORCS; 6391; 585 hits in 1055 CRISPR screens.
DR ChiTaRS; SDHC; human.
DR GeneWiki; Succinate_dehydrogenase_complex_subunit_C; -.
DR GenomeRNAi; 6391; -.
DR Pharos; Q99643; Tbio.
DR PRO; PR:Q99643; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99643; protein.
DR Bgee; ENSG00000143252; Expressed in islet of Langerhans and 98 other tissues.
DR ExpressionAtlas; Q99643; baseline and differential.
DR Genevisible; Q99643; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
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; TAS: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:0009060; P:aerobic respiration; TAS:UniProtKB.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:UniProtKB.
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 Alternative splicing; 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:0000250"
FT CHAIN 30..169
FT /note="Succinate dehydrogenase cytochrome b560 subunit,
FT mitochondrial"
FT /id="PRO_0000003634"
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"
FT VAR_SEQ 7..59
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_041381"
FT VAR_SEQ 27..60
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:9851882, ECO:0000303|Ref.5"
FT /id="VSP_041382"
FT VAR_SEQ 81..169
FT /note="GVSLFGMSALLLPGNFESYLELVKSLCLGPALIHTAKFALVFPLMYHTWNGI
FT RHLMWDLGKGLKIPQLYQSGVVVLVLTVLSSMGLAAM -> DVGPRKRPEDSPAIPVWS
FT GCPGSYCVVLYGAGSHVKKGGSQHHLPTHYYIHPSFCLSFLSPAWEKFSLFV (in
FT isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.5"
FT /id="VSP_041383"
SQ SEQUENCE 169 AA; 18610 MW; DF7CBD6D0CD49500 CRC64;
MAALLLRHVG RHCLRAHFSP QLCIRNAVPL GTTAKEEMER FWNKNIGSNR PLSPHITIYS
WSLPMAMSIC HRGTGIALSA GVSLFGMSAL LLPGNFESYL ELVKSLCLGP ALIHTAKFAL
VFPLMYHTWN GIRHLMWDLG KGLKIPQLYQ SGVVVLVLTV LSSMGLAAM
