DHSD_MOUSE
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 03-AUG-2022, entry version 133.
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}.
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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; Q9CXV1; -.
DR PeptideAtlas; Q9CXV1; -.
DR PRIDE; Q9CXV1; -.
DR ProteomicsDB; 279866; -.
DR TopDownProteomics; Q9CXV1; -.
DR DNASU; 66925; -.
DR Ensembl; ENSMUST00000000175; ENSMUSP00000000175; ENSMUSG00000000171.
DR GeneID; 66925; -.
DR KEGG; mmu:66925; -.
DR UCSC; uc009pjv.2; mouse.
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; KLERLWA; -.
DR OrthoDB; 1511215at2759; -.
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 75 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 284 other tissues.
DR Genevisible; Q9CXV1; 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: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; IC: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; -; 1.
DR InterPro; IPR007992; CybS.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR13337; PTHR13337; 1.
DR SUPFAM; SSF81343; SSF81343; 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..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
