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Q0QF01 (SDHA_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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] flavoprotein subunit, mitochondrial

EC=1.3.5.1
Alternative name(s):
Flavoprotein subunit of complex II
Short name=Fp
Gene names
Name:SDHA
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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). Can act as a tumor suppressor By similarity.

Catalytic activity

Succinate + a quinone = fumarate + a quinol.

Cofactor

FAD. Ref.4

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. Interacts with SDHAF2/SDH5; interaction is required for FAD attachment By similarity. Interacts with TRAP1 By similarity. Ref.1 Ref.4

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Ref.1.

Post-translational modification

Phosphorylation at Tyr-215 is important for efficient electron transfer in complex II and the prevention of ROS generation By similarity.

Deacetylated by SIRT3 By similarity.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.

Sequence caution

The sequence ABI29191.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Mitochondrion Ref.1
Chain43 – 664622Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
PRO_0000391718

Regions

Nucleotide binding68 – 736FAD
Nucleotide binding91 – 10616FAD
Nucleotide binding456 – 4572FAD

Sites

Binding site2751FAD
Binding site2961Substrate
Binding site3081Substrate
Binding site4071Substrate
Binding site4401FAD
Binding site4511Substrate

Amino acid modifications

Modified residue991Tele-8alpha-FAD histidine
Modified residue1671N6-acetyllysine By similarity
Modified residue1791N6-acetyllysine; alternate By similarity
Modified residue1791N6-succinyllysine; alternate By similarity
Modified residue1821N6-acetyllysine By similarity
Modified residue2151Phosphotyrosine; by SRC By similarity
Modified residue3351N6-acetyllysine; alternate By similarity
Modified residue3351N6-succinyllysine; alternate By similarity
Modified residue4801N6-acetyllysine By similarity
Modified residue4851N6-acetyllysine; alternate By similarity
Modified residue4851N6-succinyllysine; alternate By similarity
Modified residue4981N6-acetyllysine; alternate By similarity
Modified residue4981N6-succinyllysine; alternate By similarity
Modified residue5171N6-acetyllysine By similarity
Modified residue5381N6-acetyllysine; alternate By similarity
Modified residue5381N6-succinyllysine; alternate By similarity
Modified residue5501N6-acetyllysine By similarity
Modified residue5981N6-acetyllysine By similarity
Modified residue6081N6-acetyllysine By similarity
Modified residue6151N6-succinyllysine By similarity
Modified residue6241N6-acetyllysine By similarity
Modified residue6331N6-acetyllysine By similarity
Modified residue6361N6-acetyllysine By similarity
Modified residue6471N6-acetyllysine By similarity

Experimental info

Sequence conflict165 – 1717DGKIYQR → LQESARG in ABI29191. Ref.3
Sequence conflict2221L → S no nucleotide entry Ref.1
Sequence conflict2351I → T no nucleotide entry Ref.1
Sequence conflict3581G → N no nucleotide entry Ref.1
Sequence conflict4531G → E no nucleotide entry Ref.1
Sequence conflict5091S → W in ABD77326. Ref.2
Sequence conflict5661L → P in ABD77326. Ref.2

Secondary structure

....................................................................................................................... 664
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q0QF01 [UniParc].

Last modified March 2, 2010. Version 2.
Checksum: 0120E14F7F6F60EE

FASTA66472,832
        10         20         30         40         50         60 
MSGVRAVSRL LRARRLALTW AQPAASPIGA RSFHFTVDGN KRSSAKVSDA ISTQYPVVDH 

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

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

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

       250        260        270        280        290        300 
DGSIHRIRAR NTVVATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI 

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

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

       430        440        450        460        470        480 
VLRHVNGQDQ VVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IAESCRPGDK 

       490        500        510        520        530        540 
VPSIKPNAGE ESVMNLDKLR FANGTIRTSE LRLSMQKSMQ SHAAVFRVGS VLQEGCEKIL 

       550        560        570        580        590        600 
RLYGDLQHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDFKER 

       610        620        630        640        650        660 
VDEYDYSKPI QGQQKKPFQE HWRKHTLSYV DVKTGKVSLE YRPVIDKTLN EADCATVPPA 


IRSY 

« Hide

References

[1]"Preliminary molecular characterization and crystallization of mitochondrial respiratory complex II from porcine heart."
Huo X., Su D., Wang A., Zhai Y., Xu J., Li X., Bartlam M., Sun F., Rao Z.
FEBS J. 274:1524-1529(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-47, SUBUNIT, SUBCELLULAR LOCATION.
Tissue: Heart.
[2]"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 59-599.
Tissue: Liver.
[3]"Selection of reference genes for gene expression studies in pig tissues using SYBR green qPCR."
Nygard A.B., Jorgensen C.B., Cirera S., Fredholm M.
BMC Mol. Biol. 8:67-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 165-663.
[4]"Crystal structure of mitochondrial respiratory membrane protein complex II."
Sun F., Huo X., Zhai Y., Wang A., Xu J., Su D., Bartlam M., Rao Z.
Cell 121:1043-1057(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND SUBSTRATE ANALOG 3-NITROPROPIONATE, COFACTOR, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ402993 mRNA. Translation: ABD77326.1.
DQ845177 mRNA. Translation: ABI29191.1. Different initiation.
UniGeneSsc.24988.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZOYX-ray2.40A43-599[»]
1ZP0X-ray3.50A43-664[»]
3ABVX-ray3.24A43-664[»]
3AE1X-ray3.14A43-664[»]
3AE2X-ray3.10A43-664[»]
3AE3X-ray3.35A43-664[»]
3AE4X-ray2.91A43-664[»]
3AE5X-ray3.41A43-664[»]
3AE6X-ray3.40A43-664[»]
3AE7X-ray3.62A43-664[»]
3AE8X-ray3.40A43-664[»]
3AE9X-ray3.31A43-664[»]
3AEAX-ray3.39A43-664[»]
3AEBX-ray3.00A43-664[»]
3AECX-ray3.61A43-664[»]
3AEDX-ray3.52A43-664[»]
3AEEX-ray3.22A43-664[»]
3AEFX-ray2.80A43-664[»]
3AEGX-ray3.27A43-664[»]
3SFDX-ray2.61A43-664[»]
3SFEX-ray2.81A43-664[»]
ProteinModelPortalQ0QF01.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ0QF01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG001461.

Enzyme and pathway databases

UniPathwayUPA00223; UER01006.

Family and domain databases

Gene3D1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProIPR003953. FAD_bind_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR027477. Succ_DH/fumarate_Rdtase_cat.
IPR011281. Succ_DH_flav_su_fwd.
IPR014006. Succ_Dhase_FrdA_Gneg.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ0QF01.

Entry information

Entry nameSDHA_PIG
AccessionPrimary (citable) accession number: Q0QF01
Secondary accession number(s): A0SNV1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 2, 2010
Last modified: July 9, 2014
This is version 47 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways