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Q0QF01

- SDHA_PIG

UniProt

Q0QF01 - SDHA_PIG

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
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 2 (02 Mar 2010)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. succinate dehydrogenase (ubiquinone) activity Source: UniProtKB-EC

    GO - Biological processi

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

    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

    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.

    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

    MSGVRAVSRL LRARRLALTW AQPAASPIGA RSFHFTVDGN KRSSAKVSDA    50
    ISTQYPVVDH EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT 100
    VAAQGGINAA LGNMEEDNWR WHFYDTVKGS DWLGDQDAIH YMTEQAPASV 150
    VELENYGMPF SRTEDGKIYQ RAFGGQSLKF GKGGQAHRCC CVADRTGHSL 200
    LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE DGSIHRIRAR 250
    NTVVATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI 300
    YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE 350
    IREGRGCGPE KDHVYLQLHH LPPEQLAVRL PGISETAMIF AGVDVTKEPI 400
    PVLPTVHYNM GGIPTNYKGQ VLRHVNGQDQ VVPGLYACGE AACASVHGAN 450
    RLGANSLLDL VVFGRACALS IAESCRPGDK VPSIKPNAGE ESVMNLDKLR 500
    FANGTIRTSE LRLSMQKSMQ SHAAVFRVGS VLQEGCEKIL RLYGDLQHLK 550
    TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDFKER 600
    VDEYDYSKPI QGQQKKPFQE HWRKHTLSYV DVKTGKVSLE YRPVIDKTLN 650
    EADCATVPPA IRSY 664
    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.

    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 1, 2014
    This is version 48 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