[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain cortex; Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K.; "Isolation and characterization of cDNA for macaque neurological disease genes."; Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Flavoprotein (FP) 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: FAD (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).
MISCELLANEOUS: The complex, present in mitochondria, can be degraded to form EC 1.3.99.1, which no longer reacts with ubiquinone.
SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

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

AB083328; BAC20607.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P10444; 1NEK. [HSSP ENTRY / PDB]

SMR

Q8HXW3; 54-664.

ModBase

Q8HXW3.

Ontologies

GO:0005739;	Cellular component: mitochondrion (inferred from sequence or structural similarity from UniProtKB).
GO:0000104;	Molecular function: succinate dehydrogenase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0055114;	Biological process: oxidation reduction (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003953; FAD_bind2_N.
IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR003952; FRD_SDH_FAD_BS.
IPR004112; Fum_Rdtase/Succ_DHase_flav_C.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR011281; Succ_DHase_flav_su_fwd.
IPR014006; Succ_Dhase_frdA_Gneg.
Graphical view of domain structure.

Pfam

PF00890; FAD_binding_2; 1.
PF02910; Succ_DH_flav_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00368; FADPNR.
PR00411; PNDRDTASEI.

TIGRFAMs

TIGR01816; sdhA_forward; 1.
TIGR01812; sdhA_frdA_Gneg; 1.

PROSITE

PS00504; FRD_SDH_FAD_BINDING; 1.

BLOCKS

Q8HXW3.

Phylogenomic databases

HOVERGEN

Q8HXW3; -.

Other

ProtoNet

Q8HXW3.

UniRef

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

Keywords

Acetylation; Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein; Transit peptide; Transport; Tricarboxylic acid cycle.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 43`	`43`	`Mitochondrion (By similarity).`
`CHAIN`	`44 664`	`621`	`Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial.`	`PRO_0000010336`
`NP_BIND`	`91 106`	`16`	`FAD (By similarity).`
`ACT_SITE`	`340 340`		`Proton acceptor (By similarity).`
`BINDING`	`296 296`		`Substrate (By similarity).`
`BINDING`	`308 308`		`Substrate (By similarity).`
`BINDING`	`407 407`		`Substrate (By similarity).`
`BINDING`	`451 451`		`Substrate (By similarity).`
`MOD_RES`	`99 99`		`Tele-8alpha-FAD histidine (By similarity).`
`MOD_RES`	`179 179`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`252 252`		`Phosphothreonine (By similarity).`
`MOD_RES`	`485 485`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`498 498`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`538 538`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`547 547`		`N6-acetyllysine (By similarity).`

Sequence information

Length: 664 AA [This is the length of the unprocessed precursor]

Molecular weight: 72965 Da [This is the MW of the unprocessed precursor]

CRC64: 181C2C8E463DF802 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGVRRLSRL LSTRRLALAK AWPAVLQTGT RGFHFTVDGN KRASAKVSDS ISAQYPVVDH 

        70         80         90        100        110        120 
EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR 

       130        140        150        160        170        180 
WHFYDTVKGS DWLGDQDAIH YMTEQAPAAV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF 

       190        200        210        220        230        240 
GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENRE CRGVIALCIE 

       250        260        270        280        290        300 
DGSIHRIRAK NTVVATGGYG RTYFSCTSAH TSTGDGTAMI TRAGLPCQDL EFVQFHPTGI 

       310        320        330        340        350        360 
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE 

       370        380        390        400        410        420 
KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ 

       430        440        450        460        470        480 
VLRHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLWDL VVFGRACALS IEESCRPGDK 

       490        500        510        520        530        540 
VPPIKPNAGE ESVMNLDKLR FADGSIRTSE LRLSMQKSMQ NHAAVFRVGS VLQEGCGKIS 

       550        560        570        580        590        600 
KLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKAR 

       610        620        630        640        650        660 
IDEYDYSKPI QGQQKKPFEE HWRKHTLSYV DVSTGKVTLE YRPVIDKTLN EADCATVPPA 


IRSY

Q8HXW3 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