Q9CXV1 (DHSD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
Short name=CybS

Alternative name(s):
CII-4
QPs3
Succinate dehydrogenase complex subunit D
Succinate-ubiquinone oxidoreductase cytochrome b small subunit
Succinate-ubiquinone reductase membrane anchor subunit

Gene names

Name:

Sdhd

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	159 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Subunit structure	Component of complex II composed of four subunits: the flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome b560 composed of SDHC and SDHD By similarity.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the CybS family.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial respiratory chain complex II Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	heme binding Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquinone binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 56	56	Mitochondrion Potential
	Chain	57 – 159	103	Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial		PRO_0000006488
Regions
	Topological domain	57 – 63	7	Mitochondrial matrix By similarity
	Transmembrane	64 – 85	22	Helical; By similarity
	Topological domain	86 – 90	5	Mitochondrial intermembrane By similarity
	Transmembrane	91 – 111	21	Helical; By similarity
	Topological domain	112 – 120	9	Mitochondrial matrix By similarity
	Transmembrane	121 – 142	22	Helical; By similarity
	Topological domain	143 – 159	17	Mitochondrial intermembrane By similarity
Sites
	Metal binding	102	1	Iron (heme axial ligand); shared with SDHC By similarity
	Binding site	114	1	Ubiquinone; shared with IP/SDHB By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9CXV1 [UniParc]. Last modified March 1, 2003. Version 2. Checksum: CB3B3CB37E257A06	FASTA	159	17,014
	10 20 30 40 50 60 MAVLLKLGVL CSGQGARALL LRSRVVRPAY VSAFLQDQPT QGRCGTQHIH LSPSHHSGSK 70 80 90 100 110 120 AASLHWTSER VVSVLLLGLI PAGYLNPCSV VDYSLAAALT LHSHWGLGQV VTDYVHGDTL 130 140 150 PKAARAGLLA LSALTFAGLC YFNYHDVGIC RAVAMLWKL

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Egg and Head.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK013962 mRNA. Translation: BAB29086.2. AK135970 mRNA. Translation: BAE22752.1. BC145731 mRNA. Translation: AAI45732.1. BC145733 mRNA. Translation: AAI45734.1.
IPI	IPI00187452.
RefSeq	NP_080124.1. NM_025848.3.
UniGene	Mm.10406.
3D structure databases
ProteinModelPortal	Q9CXV1.
SMR	Q9CXV1. Positions 59-159.
ModBase	Search...
Proteomic databases
PaxDb	Q9CXV1.
PRIDE	Q9CXV1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000000175; ENSMUSP00000000175; ENSMUSG00000000171.
GeneID	66925.
KEGG	mmu:66925.
UCSC	uc009pjv.2. mouse.
Organism-specific databases
CTD	6392.
MGI	MGI:1914175. Sdhd.
Phylogenomic databases
eggNOG	NOG264646.
GeneTree	ENSGT00390000010003.
HOGENOM	HOG000290645.
HOVERGEN	HBG003003.
InParanoid	A6H629.
KO	K00237.
OMA	LTLHSHW.
OrthoDB	EOG4STS5Z.
Enzyme and pathway databases
UniPathway	UPA00223.
Gene expression databases
Bgee	Q9CXV1.
Genevestigator	Q9CXV1.
GermOnline	ENSMUSG00000000171. Mus musculus.
Family and domain databases
InterPro	IPR007992. CybS. [Graphical view]
PANTHER	PTHR13337. PTHR13337. 1 hit.
Pfam	PF05328. CybS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SDHD. mouse.
NextBio	323033.
SOURCE	Search...

Entry information

Entry name

DHSD_MOUSE

Accession

Primary (citable) accession number: Q9CXV1
Secondary accession number(s): A6H629, Q3UX11

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program