[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Ileum; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

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).
COFACTOR: Binds 1 3Fe-4S cluster (By similarity).
COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side (By similarity).
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

BC102067; AAI02068.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001035573.1; -.

UniGene

Bt.13128

3D structure databases

SMR

Q3T189; 37-275.

ModBase

Q3T189.

Protein-protein interaction databases

IntAct

Q3T189; -.

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.

Pfam

PF00111; Fer2; 1.
Pfam graphical view of domain structure.

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).

BLOCKS

Q3T189.

Genome annotation databases

Ensembl

ENSBTAG00000008314; Bos taurus. [Contig view]

GeneID

286840; -.

KEGG

bta:286840; -.

Phylogenomic databases

HOVERGEN

Q3T189; -.

Other

ProtoNet

Q3T189.

UniRef

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

Keywords

2Fe-2S; 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 28`	`28`	`Mitochondrion (By similarity).`
`CHAIN`	`29 280`	`252`	`Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial.`	`PRO_0000247594`
`DOMAIN`	`40 133`	`94`	`2Fe-2S ferredoxin-type.`
`DOMAIN`	`176 206`	`31`	`4Fe-4S ferredoxin-type.`
`METAL`	`93 93`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`98 98`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`101 101`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`113 113`		`Iron-sulfur 1 (2Fe-2S) (By similarity).`
`METAL`	`186 186`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`189 189`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`192 192`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`196 196`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`243 243`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`249 249`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`253 253`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`BINDING`	`201 201`		`Ubiquinone; shared with DHSD (By similarity).`

Sequence information

Length: 280 AA [This is the length of the unprocessed precursor]

Molecular weight: 31518 Da [This is the MW of the unprocessed precursor]

CRC64: BE51FF2193F8B6C5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVVALSLR RRFPAAALGG ARLQACRGAQ TAAAAAPRIK KFAIYRWDPD KTGDKPHMQT 

        70         80         90        100        110        120 
YEIDLNNCGP MVLDALIKIK NEIDSTLTFR RSCREGICGS CAMNINGGNT LACTRRIDTN 

       130        140        150        160        170        180 
LSKVSKIYPL PHMYVIKDLV PDLSNFYAQY KSIEPYLKKK DESQGGKEQY LQSIEDREKL 

       190        200        210        220        230        240 
DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDFTEER LAKLQDPFSL 

       250        260        270        280 
YRCHTIMNCT QTCPKGLNPG KAIAEIKKMM ATYKEKQASA

Q3T189 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