[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Heart; Weinreich D.M.; "OXPHOS genes in mammals and the molecular clock."; Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[2]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF OF 39-290, SUBUNIT, AND SUBCELLULAR LOCATION. DOI=10.1107/S0907444905000181; PubMed=15805592 [NCBI, ExPASy, EBI, Israel, Japan] Huang L.-S., Borders T.M., Shen J.T., Wang C.-J., Berry E.A.; "Crystallization of mitochondrial respiratory complex II from chicken heart: a membrane-protein complex diffracting to 2.0 A."; Acta Crystallogr. D 61:380-387(2005).
[3]	X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF OF 39-290 IN COMPLEX WITH UBIQUINONE AND IRON-SULFUR CENTERS, SUBUNIT, AND SUBCELLULAR LOCATION. DOI=10.1016/j.bbabio.2006.06.015; PubMed=16935256 [NCBI, ExPASy, EBI, Israel, Japan] Huang L.-S., Shen J.T., Wang A.C., Berry E.A.; "Crystallographic studies of the binding of ligands to the dicarboxylate site of complex II, and the identity of the ligand in the 'oxaloacetate-inhibited' state."; Biochim. Biophys. Acta 1757:1073-1083(2006).
[4]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 39-290 IN COMPLEX WITH UBIQUINONE AND IRON-SULFUR CENTERS, SUBUNIT, AND SUBCELLULAR LOCATION. DOI=10.1074/jbc.M511270200; PubMed=16371358 [NCBI, ExPASy, EBI, Israel, Japan] Huang L.-S., Sun G., Cobessi D., Wang A.C., Shen J.T., Tung E.Y., Anderson V.E., Berry E.A.; "3-nitropropionic acid is a suicide inhibitor of mitochondrial respiration that, upon oxidation by complex II, forms a covalent adduct with a catalytic base arginine in the active site of the enzyme."; J. Biol. Chem. 281:5965-5972(2006).

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).
CATALYTIC ACTIVITY: Succinate + ubiquinone = fumarate + ubiquinol.
COFACTOR: Binds 1 2Fe-2S cluster.
COFACTOR: Binds 1 3Fe-4S cluster.
COFACTOR: Binds 1 4Fe-4S cluster.
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle .
SUBUNIT: 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.
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF095937; AAC72372.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001074344.1; -.

3D structure databases

PDB

1YQ3; X-ray; 2.20 A; B=39-290.	[ExPASy / RCSB / EBI]
1YQ4; X-ray; 2.33 A; B=39-290.	[ExPASy / RCSB / EBI]
2FBW; X-ray; 2.10 A; B/O=39-290.	[ExPASy / RCSB / EBI]
2H88; X-ray; 1.74 A; B/O=39-290.	[ExPASy / RCSB / EBI]
2H89; X-ray; 2.40 A; B=39-290.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1YQ3; -.
1YQ4; -.
2FBW; -.
2H88; -.
2H89; -.

ModBase

Q9YHT2.

Ontologies

GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051537;	Molecular function: 2 iron, 2 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051538;	Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008177;	Molecular function: succinate dehydrogenase (ubiquinone) activity (inferred from electronic annotation from EC).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006099;	Biological process: tricarboxylic acid cycle (inferred from electronic annotation from InterPro).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:3.10.20.30; Ferredoxin_fold; 1.
G3DSA:1.10.1060.10; Fum_reductase_C; 1.

TIGRFAMs

TIGR00384; dhsB; 1.

PROSITE

PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS00198; 4FE4S_FER_1; 1.
PS51379; 4FE4S_FER_2; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q9YHT2.

Genome annotation databases

Ensembl

ENSGALG00000000508; Gallus gallus. [Contig view]

GeneID

770063; -.

KEGG

gga:770063; -.

Phylogenomic databases

HOGENOM

Q9YHT2; -.

HOVERGEN

Q9YHT2; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

2Fe-2S; 3D-structure; 3Fe-4S; 4Fe-4S; Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Transit peptide; Transport; Tricarboxylic acid cycle.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 38`	`38`	`Mitochondrion.`
`CHAIN`	`39 290`	`252`	`Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial.`	`PRO_0000343800`
`DOMAIN`	`50 143`	`94`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`186 216`	`31`	`4Fe-4S ferredoxin-type.`
`METAL`	`103 103`		`Iron-sulfur 1 (2Fe-2S).`
`METAL`	`108 108`		`Iron-sulfur 1 (2Fe-2S).`
`METAL`	`111 111`		`Iron-sulfur 1 (2Fe-2S).`
`METAL`	`123 123`		`Iron-sulfur 1 (2Fe-2S).`
`METAL`	`196 196`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`199 199`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`202 202`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`206 206`		`Iron-sulfur 3 (3Fe-4S).`
`METAL`	`253 253`		`Iron-sulfur 3 (3Fe-4S).`
`METAL`	`259 259`		`Iron-sulfur 3 (3Fe-4S).`
`METAL`	`263 263`		`Iron-sulfur 2 (4Fe-4S).`
`BINDING`	`211 211`		`Ubiquinone; shared with DHSD.`
`STRAND`	`49 56`	`8`
`STRAND`	`67 74`	`8`
`HELIX`	`75 77`	`3`
`HELIX`	`82 92`	`11`
`STRAND`	`104 108`	`5`
`STRAND`	`112 115`	`4`
`STRAND`	`118 121`	`4`
`HELIX`	`122 124`	`3`
`STRAND`	`133 138`	`6`
`STRAND`	`144 147`	`4`
`HELIX`	`154 162`	`9`
`TURN`	`173 177`	`5`
`HELIX`	`184 188`	`5`
`TURN`	`189 195`	`7`
`HELIX`	`203 205`	`3`
`HELIX`	`207 212`	`6`
`TURN`	`213 215`	`3`
`HELIX`	`219 229`	`11`
`HELIX`	`237 242`	`6`
`STRAND`	`246 248`	`3`
`TURN`	`249 252`	`4`
`HELIX`	`258 262`	`5`
`HELIX`	`269 282`	`14`

Sequence information

Length: 290 AA [This is the length of the unprocessed precursor]

Molecular weight: 32597 Da [This is the MW of the unprocessed precursor]

CRC64: 313E698866B3FDFC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAAVVGVSL RRGVPARFLR AGLRPVRGLE AVHGICRGAQ TAAAATSRIK KFSIYRWDPD 

        70         80         90        100        110        120 
KPGDKPRMQT YEVDLNKCGP MVLDALIKIK NELDSTLTFR RSCREGICGS CAMNIAGGNT 

       130        140        150        160        170        180 
LACTKKIDPD LSKTTKIYPL PHMYVVKDLV PDLSNFYAQY KSIEPYLKKK DESKQGKEQY 

       190        200        210        220        230        240 
LQSIEDRQKL DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDYTEER 

       250        260        270        280        290 
LAQLQDPFSL YRCHTIMNCT RTCPKGLNPG KAIAEIKKMM ATYKEKAAAA

Q9YHT2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools