Reviewed, UniProtKB/Swiss-Prot Q9CQA3 (DHSB_MOUSE)

Names and origin

Protein names

Recommended name:
    Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
    EC=1.3.5.1
Alternative name(s):
    Iron-sulfur subunit of complex II
      Short name=Ip

Gene names

Name:

Sdhb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Iron-sulfur protein (IP) 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.
Catalytic activity	Succinate + ubiquinone = fumarate + ubiquinol.
Cofactor	Binds 1 2Fe-2S cluster By similarity. Binds 1 3Fe-4S cluster By similarity. Binds 1 4Fe-4S cluster 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; Peripheral membrane protein; Matrix sideBy similarity.
Sequence similarities	Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport Tricarboxylic acid cycle
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Transit peptide	1 – 30	30	Mitochondrion By similarity
	Chain	31 – 282	252	Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
Regions
	Domain	42 – 135	94	2Fe-2S ferredoxin-type
	Domain	178 – 208	31	4Fe-4S ferredoxin-type
Sites
	Metal binding	95	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	100	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	103	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	115	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	188	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	191	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	194	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	198	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	245	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	251	1	Iron-sulfur 3 (3Fe-4S) By similarity
	Metal binding	255	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Binding site	203	1	Ubiquinone; shared with DHSD By similarity
Experimental info
	Sequence conflict	40	1	R → K in BAB22534. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9CQA3-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: A8616A911427AF8E	FASTA	282	31,814
	10 20 30 40 50 60 MAATVGVSLK RGFPAAVLGR VGLQFQACRG AQTAAAAAPR IKKFAIYRWD PDKTGDKPRM 70 80 90 100 110 120 QTYEVDLNKC GPMVLDALIK IKNEVDSTLT FRRSCREGIC GSCAMNINGG NTLACTRRID 130 140 150 160 170 180 TDLSKVSKIY PLPHMYVIKD LVPDLSNFYA QYKSIEPYLK KKDESQEGKQ QYLQSIEDRE 190 200 210 220 230 240 KLDGLYECIL CACCSTSCPS YWWNGDKYLG PAVLMQAYRW MIDSRDDFTE ERLAKLQDPF 250 260 270 280 SVYRCHTIMN CTQTCPKGLN PGKAIAEIKK MMATYKEKRA LA

References

	« Hide 'large scale' referencesShow 'large scale' 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Amnion, Bone marrow, Brain and Tongue.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and FVB/N. Tissue: Brain and Colon.
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 49-92; 118-125; 129-153; 170-179; 208-232 AND 245-257, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK003052 mRNA. Translation: BAB22534.1. AK003533 mRNA. Translation: BAB22842.1. AK009660 mRNA. Translation: BAB26422.1. AK153045 mRNA. Translation: BAE31674.1. AK169252 mRNA. Translation: BAE41016.1. BC013509 mRNA. Translation: AAH13509.1. BC051934 mRNA. Translation: AAH51934.1.
PIR	PT0094.
RefSeq	NP_075863.2.
UniGene	Mm.246965
3D structure databases
HSSP	HSSP built from PDB template 1NEK based on UniProtKB P07014.
SMR	Q9CQA3. Positions 39-277.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9CQA3.
2-D gel databases
REPRODUCTION-2DPAGE	Q9CQA3.
Genome annotation databases
Ensembl	ENSMUSG00000009863. Mus musculus. [Contig view]
GeneID	67680.
KEGG	mmu:67680.
NMPDR	fig|10090.3.peg.10709.
Organism-specific databases
MGI	MGI:1914930. Sdhb.
Phylogenomic databases
HOGENOM	Q9CQA3.
HOVERGEN	Q9CQA3.
Gene expression databases
ArrayExpress	Q9CQA3.
GermOnline	ENSMUSG00000009863. Mus musculus.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR001450. 4Fe4S_Fe_S_bd. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR004489. Succ_DHase/fum_Rdtase_Fe-S. [Graphical view]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
Pfam	PF00111. Fer2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00384. dhsB. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS00198. 4FE4S_FER_1. 1 hit. PS51379. 4FE4S_FER_2. 1 hit. [Graphical view]
ProDom	Q9CQA3. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

DHSB_MOUSE

Accession

Primary (citable) accession number: Q9CQA3
Secondary accession number(s): Q3TF82, Q9DC91

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	June 1, 2001
Last modified:	July 22, 2008
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)