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Q0QF01

- SDHA_PIG

UniProt

Q0QF01 - SDHA_PIG

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Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

SDHA

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.

Cofactori

FAD.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei275 – 2751FAD1 Publication
Binding sitei296 – 2961Substrate
Binding sitei308 – 3081Substrate
Binding sitei407 – 4071Substrate
Binding sitei440 – 4401FAD1 Publication
Binding sitei451 – 4511Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi68 – 736FAD1 Publication
Nucleotide bindingi91 – 10616FAD1 PublicationAdd
BLAST
Nucleotide bindingi456 – 4572FAD1 Publication

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

GO - Biological processi

  1. electron transport chain Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC:1.3.5.1)
Alternative name(s):
Flavoprotein subunit of complex II
Short name:
Fp
Gene namesi
Name:SDHA
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Mitochondrion inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Matrix side 1 Publication

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB
  2. mitochondrial respiratory chain complex II Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242Mitochondrion1 PublicationAdd
BLAST
Chaini43 – 664622Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialPRO_0000391718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Tele-8alpha-FAD histidine
Modified residuei167 – 1671N6-acetyllysineBy similarity
Modified residuei179 – 1791N6-acetyllysine; alternateBy similarity
Modified residuei179 – 1791N6-succinyllysine; alternateBy similarity
Modified residuei182 – 1821N6-acetyllysineBy similarity
Modified residuei215 – 2151Phosphotyrosine; by SRCBy similarity
Modified residuei335 – 3351N6-acetyllysine; alternateBy similarity
Modified residuei335 – 3351N6-succinyllysine; alternateBy similarity
Modified residuei480 – 4801N6-acetyllysineBy similarity
Modified residuei485 – 4851N6-acetyllysine; alternateBy similarity
Modified residuei485 – 4851N6-succinyllysine; alternateBy similarity
Modified residuei498 – 4981N6-acetyllysine; alternateBy similarity
Modified residuei498 – 4981N6-succinyllysine; alternateBy similarity
Modified residuei517 – 5171N6-acetyllysineBy similarity
Modified residuei538 – 5381N6-acetyllysine; alternateBy similarity
Modified residuei538 – 5381N6-succinyllysine; alternateBy similarity
Modified residuei550 – 5501N6-acetyllysineBy similarity
Modified residuei598 – 5981N6-acetyllysineBy similarity
Modified residuei608 – 6081N6-acetyllysineBy similarity
Modified residuei615 – 6151N6-succinyllysineBy similarity
Modified residuei624 – 6241N6-acetyllysineBy similarity
Modified residuei633 – 6331N6-acetyllysineBy similarity
Modified residuei636 – 6361N6-acetyllysineBy similarity
Modified residuei647 – 6471N6-acetyllysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ0QF01.

Interactioni

Subunit structurei

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).By similarity

Structurei

Secondary structure

1
664
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 615
Beta strandi63 – 675
Helixi71 – 8212
Beta strandi87 – 937
Helixi95 – 973
Helixi99 – 1024
Beta strandi113 – 1153
Helixi119 – 12911
Turni130 – 1323
Helixi136 – 15621
Beta strandi166 – 1683
Beta strandi170 – 1789
Turni179 – 1824
Beta strandi185 – 1906
Helixi196 – 20813
Turni209 – 2124
Beta strandi214 – 2174
Beta strandi219 – 2279
Beta strandi230 – 2389
Turni239 – 2413
Beta strandi244 – 2485
Beta strandi250 – 2545
Helixi260 – 2623
Beta strandi263 – 2686
Helixi275 – 2828
Beta strandi287 – 2893
Beta strandi293 – 2975
Turni301 – 3033
Helixi310 – 3145
Beta strandi317 – 3193
Beta strandi323 – 3253
Turni327 – 3293
Turni332 – 3365
Helixi340 – 35314
Beta strandi357 – 3615
Beta strandi365 – 3673
Beta strandi369 – 3713
Helixi375 – 3784
Helixi381 – 39111
Turni395 – 3973
Beta strandi398 – 4025
Beta strandi405 – 4095
Beta strandi412 – 4154
Beta strandi419 – 4257
Beta strandi428 – 43710
Helixi439 – 4413
Beta strandi442 – 4443
Helixi456 – 47419
Turni486 – 4894
Helixi490 – 50011
Beta strandi505 – 5073
Helixi508 – 52215
Beta strandi523 – 5275
Helixi529 – 54517
Beta strandi548 – 5503
Helixi560 – 58425
Beta strandi587 – 5893
Beta strandi594 – 5963
Beta strandi610 – 6134
Helixi618 – 6203
Beta strandi624 – 6285
Turni632 – 6343
Beta strandi639 – 6435
Turni651 – 6533

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ0QF01.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ0QF01.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOVERGENiHBG001461.
InParanoidiQ0QF01.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProiIPR003953. 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]
PfamiPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q0QF01-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGVRAVSRL LRARRLALTW AQPAASPIGA RSFHFTVDGN KRSSAKVSDA
60 70 80 90 100
ISTQYPVVDH EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT
110 120 130 140 150
VAAQGGINAA LGNMEEDNWR WHFYDTVKGS DWLGDQDAIH YMTEQAPASV
160 170 180 190 200
VELENYGMPF SRTEDGKIYQ RAFGGQSLKF GKGGQAHRCC CVADRTGHSL
210 220 230 240 250
LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE DGSIHRIRAR
260 270 280 290 300
NTVVATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI
310 320 330 340 350
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE
360 370 380 390 400
IREGRGCGPE KDHVYLQLHH LPPEQLAVRL PGISETAMIF AGVDVTKEPI
410 420 430 440 450
PVLPTVHYNM GGIPTNYKGQ VLRHVNGQDQ VVPGLYACGE AACASVHGAN
460 470 480 490 500
RLGANSLLDL VVFGRACALS IAESCRPGDK VPSIKPNAGE ESVMNLDKLR
510 520 530 540 550
FANGTIRTSE LRLSMQKSMQ SHAAVFRVGS VLQEGCEKIL RLYGDLQHLK
560 570 580 590 600
TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDFKER
610 620 630 640 650
VDEYDYSKPI QGQQKKPFQE HWRKHTLSYV DVKTGKVSLE YRPVIDKTLN
660
EADCATVPPA IRSY
Length:664
Mass (Da):72,832
Last modified:March 2, 2010 - v2
Checksum:i0120E14F7F6F60EE
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1717DGKIYQR → LQESARG in ABI29191. (PubMed:17697375)Curated
Sequence conflicti222 – 2221L → S no nucleotide entry (PubMed:17480203)Curated
Sequence conflicti235 – 2351I → T no nucleotide entry (PubMed:17480203)Curated
Sequence conflicti358 – 3581G → N no nucleotide entry (PubMed:17480203)Curated
Sequence conflicti453 – 4531G → E no nucleotide entry (PubMed:17480203)Curated
Sequence conflicti509 – 5091S → W in ABD77326. (PubMed:16751257)Curated
Sequence conflicti566 – 5661L → P in ABD77326. (PubMed:16751257)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ402993 mRNA. Translation: ABD77326.1.
DQ845177 mRNA. Translation: ABI29191.1. Different initiation.
UniGeneiSsc.24988.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
DQ402993 mRNA. Translation: ABD77326.1 .
DQ845177 mRNA. Translation: ABI29191.1 . Different initiation.
UniGenei Ssc.24988.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZOY X-ray 2.40 A 43-599 [» ]
1ZP0 X-ray 3.50 A 43-664 [» ]
3ABV X-ray 3.24 A 43-664 [» ]
3AE1 X-ray 3.14 A 43-664 [» ]
3AE2 X-ray 3.10 A 43-664 [» ]
3AE3 X-ray 3.35 A 43-664 [» ]
3AE4 X-ray 2.91 A 43-664 [» ]
3AE5 X-ray 3.41 A 43-664 [» ]
3AE6 X-ray 3.40 A 43-664 [» ]
3AE7 X-ray 3.62 A 43-664 [» ]
3AE8 X-ray 3.40 A 43-664 [» ]
3AE9 X-ray 3.31 A 43-664 [» ]
3AEA X-ray 3.39 A 43-664 [» ]
3AEB X-ray 3.00 A 43-664 [» ]
3AEC X-ray 3.61 A 43-664 [» ]
3AED X-ray 3.52 A 43-664 [» ]
3AEE X-ray 3.22 A 43-664 [» ]
3AEF X-ray 2.80 A 43-664 [» ]
3AEG X-ray 3.27 A 43-664 [» ]
3SFD X-ray 2.61 A 43-664 [» ]
3SFE X-ray 2.81 A 43-664 [» ]
ProteinModelPortali Q0QF01.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q0QF01.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG001461.
InParanoidi Q0QF01.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01006 .

Miscellaneous databases

EvolutionaryTracei Q0QF01.

Family and domain databases

Gene3Di 1.20.58.100. 1 hit.
3.90.700.10. 1 hit.
InterProi IPR003953. 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 ]
Pfami PF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF46977. SSF46977. 1 hit.
SSF56425. SSF56425. 1 hit.
TIGRFAMsi TIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEi PS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiSDHA_PIG
AccessioniPrimary (citable) accession number: Q0QF01
Secondary accession number(s): A0SNV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 2, 2010
Last modified: October 29, 2014
This is version 49 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3