ID   DHSD_MOUSE              Reviewed;         159 AA.
AC   Q9CXV1; A6H629; Q3UX11;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 2.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial;
DE            Short=CybS;
DE   AltName: Full=CII-4;
DE   AltName: Full=QPs3;
DE   AltName: Full=Succinate dehydrogenase complex subunit D;
DE   AltName: Full=Succinate-ubiquinone oxidoreductase cytochrome b small subunit;
DE   AltName: Full=Succinate-ubiquinone reductase membrane anchor subunit;
DE   Flags: Precursor;
GN   Name=Sdhd;
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=Egg, and Head;
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].
RC   TISSUE=Brain;
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=Brown adipose tissue, Heart, and Kidney;
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   -!- 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 CybS family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK013962; BAB29086.2; -; mRNA.
DR   EMBL; AK135970; BAE22752.1; -; mRNA.
DR   EMBL; BC145731; AAI45732.1; -; mRNA.
DR   EMBL; BC145733; AAI45734.1; -; mRNA.
DR   CCDS; CCDS40623.1; -.
DR   RefSeq; NP_080124.1; NM_025848.3.
DR   AlphaFoldDB; Q9CXV1; -.
DR   SMR; Q9CXV1; -.
DR   BioGRID; 211813; 6.
DR   ComplexPortal; CPX-562; Mitochondrial respiratory chain complex II.
DR   CORUM; Q9CXV1; -.
DR   STRING; 10090.ENSMUSP00000000175; -.
DR   SwissPalm; Q9CXV1; -.
DR   jPOST; Q9CXV1; -.
DR   MaxQB; Q9CXV1; -.
DR   PaxDb; 10090-ENSMUSP00000000175; -.
DR   PeptideAtlas; Q9CXV1; -.
DR   ProteomicsDB; 279866; -.
DR   Pumba; Q9CXV1; -.
DR   TopDownProteomics; Q9CXV1; -.
DR   DNASU; 66925; -.
DR   Ensembl; ENSMUST00000000175.6; ENSMUSP00000000175.5; ENSMUSG00000000171.6.
DR   GeneID; 66925; -.
DR   KEGG; mmu:66925; -.
DR   UCSC; uc009pjv.2; mouse.
DR   AGR; MGI:1914175; -.
DR   CTD; 6392; -.
DR   MGI; MGI:1914175; Sdhd.
DR   VEuPathDB; HostDB:ENSMUSG00000000171; -.
DR   eggNOG; KOG4097; Eukaryota.
DR   GeneTree; ENSGT00390000010003; -.
DR   HOGENOM; CLU_096618_1_1_1; -.
DR   InParanoid; Q9CXV1; -.
DR   OMA; YMLTARI; -.
DR   OrthoDB; 2782446at2759; -.
DR   PhylomeDB; Q9CXV1; -.
DR   TreeFam; TF313310; -.
DR   Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; -.
DR   BioGRID-ORCS; 66925; 23 hits in 80 CRISPR screens.
DR   ChiTaRS; Sdhd; mouse.
DR   PRO; PR:Q9CXV1; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9CXV1; Protein.
DR   Bgee; ENSMUSG00000000171; Expressed in right kidney and 287 other cell types or tissues.
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:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IMP:MGI.
DR   GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR   GO; GO:0071456; P:cellular response to hypoxia; IMP:MGI.
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:0050433; P:regulation of catecholamine secretion; IMP:MGI.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISO:MGI.
DR   CDD; cd03496; SQR_TypeC_CybS; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   InterPro; IPR007992; CybS.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   PANTHER; PTHR13337; SUCCINATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR13337:SF2; SUCCINATE DEHYDROGENASE [UBIQUINONE] CYTOCHROME B SMALL SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF05328; CybS; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
DR   Genevisible; Q9CXV1; 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..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..159
FT                   /note="Succinate dehydrogenase [ubiquinone] cytochrome b
FT                   small subunit, mitochondrial"
FT                   /id="PRO_0000006488"
FT   TOPO_DOM        57..63
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        64..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        86..90
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        112..120
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        121..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        143..159
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_note="ligand shared with SDHC"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:A5GZW8"
FT   BINDING         114
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /ligand_note="ligand shared with IP/SDHB"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   159 AA;  17014 MW;  CB3B3CB37E257A06 CRC64;
     MAVLLKLGVL CSGQGARALL LRSRVVRPAY VSAFLQDQPT QGRCGTQHIH LSPSHHSGSK
     AASLHWTSER VVSVLLLGLI PAGYLNPCSV VDYSLAAALT LHSHWGLGQV VTDYVHGDTL
     PKAARAGLLA LSALTFAGLC YFNYHDVGIC RAVAMLWKL
//