C560_MOUSE
ID C560_MOUSE Reviewed; 169 AA.
AC Q9CZB0; Q544Q9; Q99JP2; Q9DCU7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
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 Flags: Precursor;
GN Name=Sdhc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Embryo, Kidney, and Muellerian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250}.
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. {ECO:0000250}.
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; AK002459; BAB22116.1; -; mRNA.
DR EMBL; AK012818; BAB28491.1; -; mRNA.
DR EMBL; AK032458; BAC27878.1; -; mRNA.
DR EMBL; AK135503; BAE22557.1; -; mRNA.
DR EMBL; BC005779; AAH05779.1; -; mRNA.
DR CCDS; CCDS35772.1; -.
DR RefSeq; NP_079597.2; NM_025321.3.
DR AlphaFoldDB; Q9CZB0; -.
DR SMR; Q9CZB0; -.
DR BioGRID; 211179; 1.
DR ComplexPortal; CPX-562; Mitochondrial respiratory chain complex II.
DR CORUM; Q9CZB0; -.
DR IntAct; Q9CZB0; 3.
DR STRING; 10090.ENSMUSP00000106968; -.
DR iPTMnet; Q9CZB0; -.
DR PhosphoSitePlus; Q9CZB0; -.
DR SwissPalm; Q9CZB0; -.
DR jPOST; Q9CZB0; -.
DR MaxQB; Q9CZB0; -.
DR PaxDb; Q9CZB0; -.
DR PeptideAtlas; Q9CZB0; -.
DR PRIDE; Q9CZB0; -.
DR ProteomicsDB; 281718; -.
DR Antibodypedia; 34309; 194 antibodies from 26 providers.
DR DNASU; 66052; -.
DR Ensembl; ENSMUST00000111336; ENSMUSP00000106968; ENSMUSG00000058076.
DR GeneID; 66052; -.
DR KEGG; mmu:66052; -.
DR UCSC; uc007dnb.2; mouse.
DR CTD; 6391; -.
DR MGI; MGI:1913302; Sdhc.
DR VEuPathDB; HostDB:ENSMUSG00000058076; -.
DR eggNOG; KOG0449; Eukaryota.
DR GeneTree; ENSGT00390000000566; -.
DR HOGENOM; CLU_094691_1_1_1; -.
DR InParanoid; Q9CZB0; -.
DR OMA; IPGGIPC; -.
DR OrthoDB; 1443173at2759; -.
DR PhylomeDB; Q9CZB0; -.
DR TreeFam; TF313317; -.
DR Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; -.
DR BioGRID-ORCS; 66052; 21 hits in 75 CRISPR screens.
DR ChiTaRS; Sdhc; mouse.
DR PRO; PR:Q9CZB0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CZB0; protein.
DR Bgee; ENSMUSG00000058076; Expressed in soleus muscle and 271 other tissues.
DR ExpressionAtlas; Q9CZB0; baseline and differential.
DR Genevisible; Q9CZB0; MM.
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; IDA:MGI.
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:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IC:ComplexPortal.
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 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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 30..169
FT /note="Succinate dehydrogenase cytochrome b560 subunit,
FT mitochondrial"
FT /id="PRO_0000003635"
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 CONFLICT 4
FT /note="F -> L (in Ref. 2; AAH05779)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="S -> G (in Ref. 2; AAH05779)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="L -> R (in Ref. 1; BAB22116)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="L -> V (in Ref. 2; AAH05779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 169 AA; 18382 MW; D9BFBCF936D0B9F5 CRC64;
MAAFLLRHVS RHCLRAHLNA QLCIRNAAPL GTTAKEEMER FWKKNTSSNR PLSPHLTIYK
WSLPMALSVC HRGSGIALSG GVSLFGLSAL LLPGNFESYL MFVKSLCLGP TLIYSAKFVL
VFPLMYHSLN GIRHLLWDLG KGLAIPQVWL SGVAVVVLAV LSSGGLAAL
