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Q9CXV1 (DHSD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length159 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5656Mitochondrion Potential
Chain57 – 159103Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
PRO_0000006488

Regions

Topological domain57 – 637Mitochondrial matrix By similarity
Transmembrane64 – 8522Helical; By similarity
Topological domain86 – 905Mitochondrial intermembrane By similarity
Transmembrane91 – 11121Helical; By similarity
Topological domain112 – 1209Mitochondrial matrix By similarity
Transmembrane121 – 14222Helical; By similarity
Topological domain143 – 15917Mitochondrial intermembrane By similarity

Sites

Metal binding1021Iron (heme axial ligand); shared with SDHC By similarity
Binding site1141Ubiquinone; shared with IP/SDHB By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CXV1 [UniParc].

Last modified March 1, 2003. Version 2.
Checksum: CB3B3CB37E257A06

FASTA15917,014
        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 

« Hide

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. expand/collapse author list , 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.
CCDSCCDS40623.1.
RefSeqNP_080124.1. NM_025848.3.
UniGeneMm.10406.

3D structure databases

ProteinModelPortalQ9CXV1.
SMRQ9CXV1. Positions 59-159.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9CXV1.
PRIDEQ9CXV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000175; ENSMUSP00000000175; ENSMUSG00000000171.
GeneID66925.
KEGGmmu:66925.
UCSCuc009pjv.2. mouse.

Organism-specific databases

CTD6392.
MGIMGI:1914175. Sdhd.

Phylogenomic databases

eggNOGNOG264646.
GeneTreeENSGT00390000010003.
HOGENOMHOG000290645.
HOVERGENHBG003003.
InParanoidA6H629.
KOK00237.
OMAHTGFGNI.
OrthoDBEOG7M6D94.
PhylomeDBQ9CXV1.
TreeFamTF313310.

Enzyme and pathway databases

UniPathwayUPA00223.

Gene expression databases

BgeeQ9CXV1.
GenevestigatorQ9CXV1.

Family and domain databases

InterProIPR007992. CybS.
[Graphical view]
PANTHERPTHR13337. PTHR13337. 1 hit.
PfamPF05328. CybS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSDHD. mouse.
NextBio323033.
PROQ9CXV1.
SOURCESearch...

Entry information

Entry nameDHSD_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot