Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P21913 (DHSB_RAT)

Last modified June 16, 2009. Version 85. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Synonyms:	Sdh1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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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 transcript level.

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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 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.

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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
Gene Ontology (GO)
Biological process	respiratory electron transport chain Inferred from mutant phenotype. Source: RGD succinate metabolic process Inferred from mutant phenotype. Source: RGD transport Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from direct assay. Source: RGD
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate dehydrogenase (ubiquinone) activity Inferred from mutant phenotype. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 30

Mitochondrion By similarity

Chain

31 – 282

252

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

PRO_0000158693

Regions

Domain

56 – 135

2Fe-2S ferredoxin-type

Domain

178 – 208

4Fe-4S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

100

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

103

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

115

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

188

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

191

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

194

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

198

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

245

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

251

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

255

Iron-sulfur 2 (4Fe-4S) By similarity

Binding site

203

Ubiquinone; shared with DHSD By similarity

Experimental info

Sequence conflict

122 – 124

DLG → NLN Ref.4

Sequence conflict

153

K → R Ref.4

Sequence conflict

178

D → E Ref.4

Sequence conflict

227

E → D Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P21913-1 [UniParc].

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

282

31,830

        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

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References

	« Hide 'large scale' referencesShow '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: 15489334] [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: 16751257] [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: 2494655] [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)

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Cross-references

Sequence databases
	CH473968 Genomic DNA. Translation: EDL80954.1. BC158620 mRNA. Translation: AAI58621.1. DQ403001 mRNA. Translation: ABD77134.1.
IPI	IPI00785564.
PIR	B32394.
RefSeq	NP_001094009.1.
UniGene	Rn.3902
3D structure databases
HSSP	HSSP built from PDB template 1NEK based on UniProtKB P07014.
SMR	P21913. Positions 1-143.
ModBase	Search...
Proteomic databases
PRIDE	P21913.
Genome annotation databases
Ensembl	ENSRNOG00000007967. Rattus norvegicus. [Contig view]
GeneID	298596.
KEGG	rno:298596.
Organism-specific databases
RGD	1308598. Sdhb.
Phylogenomic databases
HOVERGEN	P21913.
OMA	P21913. ASIEPWL.
Enzyme and pathway databases
BRENDA	1.3.5.1. 248.
Gene expression databases
ArrayExpress	P21913.
GermOnline	ENSRNOG00000007967. Rattus norvegicus.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. IPR012285. Fum_reductase_C. IPR004489. Succ_DH/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.
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]
ProtoNet	Search...

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Entry information

Entry name

DHSB_RAT

Accession

Primary (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:	June 16, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents