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P21913 (SDHB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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] 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
Synonyms:Sdh1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 + a quinone = fumarate + a quinol.

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; fumarate from succinate (eukaryal route): step 1/1.

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 side By 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 processElectron transport
Transport
Tricarboxylic acid cycle
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   Ligand2Fe-2S
3Fe-4S
4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrespiratory electron transport chain

Inferred from mutant phenotype PubMed 16520240. Source: RGD

succinate metabolic process

Inferred from mutant phenotype PubMed 16520240. Source: RGD

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial inner membrane

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial respiratory chain complex II

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_function2 iron, 2 sulfur cluster binding

Inferred from sequence or structural similarity. Source: UniProtKB

3 iron, 4 sulfur cluster binding

Inferred from sequence or structural similarity. Source: UniProtKB

4 iron, 4 sulfur cluster binding

Inferred from sequence or structural similarity. Source: UniProtKB

electron carrier activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

succinate dehydrogenase (ubiquinone) activity

Inferred from mutant phenotype PubMed 16520240. Source: RGD

ubiquinone binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion By similarity
Chain31 – 282252Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
PRO_0000158693

Regions

Domain56 – 135802Fe-2S ferredoxin-type
Domain178 – 208314Fe-4S ferredoxin-type

Sites

Metal binding951Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1001Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1031Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1151Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding1881Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1911Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1941Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1981Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2451Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2511Iron-sulfur 3 (3Fe-4S) By similarity
Metal binding2551Iron-sulfur 2 (4Fe-4S) By similarity
Binding site2031Ubiquinone; shared with DHSD By similarity

Amino acid modifications

Modified residue531N6-acetyllysine By similarity
Modified residue571N6-acetyllysine By similarity

Experimental info

Sequence conflict122 – 1243DLG → NLN no nucleotide entry Ref.4
Sequence conflict1531K → R no nucleotide entry Ref.4
Sequence conflict1781D → E no nucleotide entry Ref.4
Sequence conflict2271E → D no nucleotide entry Ref.4

Sequences

Sequence LengthMass (Da)Tools
P21913 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: 6600EBC8201529A9

FASTA28231,830
        10         20         30         40         50         60 
MAAVVGVSLK RGFSATALGR VGLQFQACRE AQTAAAAAPR IKTFAIYRWD PDKAGDKPRM 

        70         80         90        100        110        120 
QTYKVDLNKC GPMVLDALIK IKNEIDSTLT FRRSCREGIC GSCAMNINGG NTLACTRRID 

       130        140        150        160        170        180 
TDLGKVSKIY PLPHMYVIKD LVPDLSNFYA QYKSIEPYLK KKDESQEGKQ QYLQSIEDRE 

       190        200        210        220        230        240 
KLDGLYECIL CACCSTSCPS YWWNGDKYLG PAVLMQAYRW MIDSRDEFTE ERLAKLQDPF 

       250        260        270        280 
SLYRCHTIMN CTQTCPKGLN PGKAIAEIKK MMATYKEKRA LA 

« Hide

References

« Hide 'large scale' references
[1]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[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: Placenta.
[3]"Housekeeping genes for phylogenetic analysis of eutherian relationships."
Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-257.
Tissue: Liver.
[4]"Use of the DNA polymerase chain reaction for homology probing: isolation of partial cDNA or genomic clones encoding the iron-sulfur protein of succinate dehydrogenase from several species."
Gould S.J., Subramani S., Scheffler I.E.
Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-251.
Tissue: Brain cortex.
[5]Erratum
Gould S.J., Subramani S., Scheffler I.E.
Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH473968 Genomic DNA. Translation: EDL80954.1.
BC158620 mRNA. Translation: AAI58621.1.
DQ403001 mRNA. Translation: ABD77134.1.
PIRB32394.
RefSeqNP_001094009.1. NM_001100539.1.
UniGeneRn.3902.

3D structure databases

ProteinModelPortalP21913.
SMRP21913. Positions 39-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000010593.

PTM databases

PhosphoSiteP21913.

Proteomic databases

PaxDbP21913.
PRIDEP21913.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010593; ENSRNOP00000010593; ENSRNOG00000007967.
GeneID298596.
KEGGrno:298596.
UCSCRGD:1308598. rat.

Organism-specific databases

CTD6390.
RGD1308598. Sdhb.

Phylogenomic databases

eggNOGCOG0479.
GeneTreeENSGT00390000013558.
HOGENOMHOG000160590.
HOVERGENHBG005483.
InParanoidQ0QEZ3.
KOK00235.
OMAEWRAMSA.
OrthoDBEOG7H4DTN.
PhylomeDBP21913.
TreeFamTF300754.

Enzyme and pathway databases

SABIO-RKP21913.
UniPathwayUPA00223; UER01006.

Gene expression databases

GenevestigatorP21913.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR012675. Beta-grasp_dom.
IPR009051. Helical_ferredxn.
IPR004489. Succ_DH/fum_Rdtase_Fe-S.
IPR025192. Succ_DH/fum_Rdtase_N.
[Graphical view]
PfamPF13085. Fer2_3. 1 hit.
[Graphical view]
SUPFAMSSF46548. SSF46548. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR00384. dhsB. 1 hit.
PROSITEPS00197. 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]
ProtoNetSearch...

Other

NextBio644032.
PROP21913.

Entry information

Entry nameSDHB_RAT
AccessionPrimary (citable) accession number: P21913
Secondary accession number(s): B0BMZ2, Q0QEZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: September 2, 2008
Last modified: May 14, 2014
This is version 126 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