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   27-MAR-2024, entry version 159.
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,
RC   Pancreas, 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   GlyGen; Q9CZB0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9CZB0; -.
DR   PhosphoSitePlus; Q9CZB0; -.
DR   SwissPalm; Q9CZB0; -.
DR   jPOST; Q9CZB0; -.
DR   MaxQB; Q9CZB0; -.
DR   PaxDb; 10090-ENSMUSP00000106968; -.
DR   PeptideAtlas; Q9CZB0; -.
DR   ProteomicsDB; 281718; -.
DR   Pumba; Q9CZB0; -.
DR   Antibodypedia; 34309; 202 antibodies from 25 providers.
DR   DNASU; 66052; -.
DR   Ensembl; ENSMUST00000111336.10; ENSMUSP00000106968.4; ENSMUSG00000058076.13.
DR   GeneID; 66052; -.
DR   KEGG; mmu:66052; -.
DR   UCSC; uc007dnb.2; mouse.
DR   AGR; MGI:1913302; -.
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; MNGIRHL; -.
DR   OrthoDB; 2787330at2759; -.
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 80 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 274 other cell types or tissues.
DR   ExpressionAtlas; Q9CZB0; baseline and differential.
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:0045257; C:succinate dehydrogenase complex (ubiquinone); 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:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; 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; NAS:ComplexPortal.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; NAS:ComplexPortal.
DR   CDD; cd03499; SQR_TypeC_SdhC; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   Gene3D; 1.20.5.540; Single helix bin; 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   NCBIfam; TIGR02970; succ_dehyd_cytB; 1.
DR   PANTHER; PTHR10978; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT; 1.
DR   PANTHER; PTHR10978:SF5; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
DR   PROSITE; PS01000; SDH_CYT_1; 1.
DR   PROSITE; PS01001; SDH_CYT_2; 1.
DR   Genevisible; Q9CZB0; MM.
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
//