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Protein

Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial

Gene

Sdha

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

Catalytic activityi

Succinate + a quinone = fumarate + a quinol.By similarity

Cofactori

FADBy similarity

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes fumarate from succinate (eukaryal route).By similarity
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (Sdhb), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (Sdhb), Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (Sdha), Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial (Sdhb)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes fumarate from succinate (eukaryal route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei275FADBy similarity1
Binding sitei296SubstrateBy similarity1
Binding sitei308SubstrateBy similarity1
Active sitei340Proton acceptorBy similarity1
Binding sitei407SubstrateBy similarity1
Binding sitei440FADBy similarity1
Binding sitei451SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi68 – 73FADBy similarity6
Nucleotide bindingi91 – 106FADBy similarityAdd BLAST16
Nucleotide bindingi456 – 457FADBy similarity2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport, Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-71403. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER01006.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC:1.3.5.1By similarity)
Alternative name(s):
Flavoprotein subunit of complex II
Short name:
Fp
Gene namesi
Name:Sdha
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1914195. Sdha.

Subcellular locationi

  • Mitochondrion inner membrane By similarity; Peripheral membrane protein By similarity; Matrix side By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 42MitochondrionBy similarityAdd BLAST42
ChainiPRO_000001033743 – 664Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrialAdd BLAST622

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei99Tele-8alpha-FAD histidineBy similarity1
Modified residuei167N6-acetyllysineCombined sources1
Modified residuei179N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei179N6-succinyllysine; alternateCombined sources1
Modified residuei182N6-acetyllysineCombined sources1 Publication1
Modified residuei215Phosphotyrosine; by SRCBy similarity1
Modified residuei250N6-acetyllysine; alternate1 Publication1
Modified residuei250N6-succinyllysine; alternateCombined sources1
Modified residuei335N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei335N6-succinyllysine; alternateCombined sources1
Modified residuei423N6-acetyllysineCombined sources1
Modified residuei480N6-acetyllysine1 Publication1
Modified residuei485N6-acetyllysine; alternate1 Publication1
Modified residuei485N6-succinyllysine; alternateCombined sources1
Modified residuei498N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei498N6-succinyllysine; alternateCombined sources1
Modified residuei517N6-acetyllysineCombined sources1
Modified residuei538N6-acetyllysine; alternateCombined sources1
Modified residuei538N6-succinyllysine; alternateCombined sources1
Modified residuei547N6-acetyllysine; alternateCombined sources1 Publication1
Modified residuei547N6-succinyllysine; alternateCombined sources1
Modified residuei550N6-acetyllysine1 Publication1
Modified residuei598N6-acetyllysine1 Publication1
Modified residuei608N6-acetyllysineCombined sources1 Publication1
Modified residuei615N6-succinyllysineCombined sources1
Modified residuei624N6-acetyllysine1 Publication1
Modified residuei633N6-acetyllysine1 Publication1
Modified residuei636N6-acetyllysineCombined sources1
Modified residuei647N6-acetyllysineCombined sources1

Post-translational modificationi

Acetylation of Lys-498 and Lys-538 is observed in liver mitochondria from fasted mice but not from fed mice. Deacetylated by SIRT3.1 Publication
Phosphorylation at Tyr-215 is important for efficient electron transfer in complex II and the prevention of ROS generation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8K2B3.
MaxQBiQ8K2B3.
PaxDbiQ8K2B3.
PeptideAtlasiQ8K2B3.
PRIDEiQ8K2B3.

2D gel databases

REPRODUCTION-2DPAGEQ8K2B3.

PTM databases

iPTMnetiQ8K2B3.
PhosphoSitePlusiQ8K2B3.
SwissPalmiQ8K2B3.

Expressioni

Gene expression databases

BgeeiENSMUSG00000021577.
GenevisibleiQ8K2B3. MM.

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 (By similarity). Interacts with SDHAF2/SDH5; interaction is required for FAD attachment (By similarity). Interacts with TRAP1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi211828. 1 interactor.
IntActiQ8K2B3. 7 interactors.
MINTiMINT-4122544.
STRINGi10090.ENSMUSP00000022062.

Structurei

3D structure databases

ProteinModelPortaliQ8K2B3.
SMRiQ8K2B3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2403. Eukaryota.
COG1053. LUCA.
GeneTreeiENSGT00390000010046.
HOVERGENiHBG001461.
InParanoidiQ8K2B3.
KOiK00234.
OMAiCWEEAHR.
OrthoDBiEOG091G041Z.
PhylomeDBiQ8K2B3.
TreeFamiTF300763.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR030664. SdhA/FrdA/AprA.
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]
PIRSFiPIRSF000171. SDHA_APRA_LASPO. 1 hit.
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF51905. SSF51905. 2 hits.
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.

Q8K2B3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVGAVSRL LRGRRLALTG AWPGTLQKQT CGFHFSVGEN KKASAKVSDA
60 70 80 90 100
ISTQYPVVDH EFDAVVVGAG GAGLRAAFGL SEAGFNTACL 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 DGSIHRIRAK
260 270 280 290 300
NTVIATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI
310 320 330 340 350
YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE
360 370 380 390 400
IREGRGCGPE KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI
410 420 430 440 450
PVLPTVHYNM GGIPTNYKGQ VLKHVNGQDQ IVPGLYACGE AACASVHGAN
460 470 480 490 500
RLGANSLLDL VVFGRACALS IAESCRPGDK VPSIKANAGE ESVMNLDKLR
510 520 530 540 550
FADGSIRTSE LRLNMQKSMQ NHAAVFRVGS VLQEGCEKIS QLYGDLKHLK
560 570 580 590 600
TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR
610 620 630 640 650
VDEYDYSKPI QGQQKKPFGE HWRKHTLSYV DIKTGKVTLE YRPVIDKTLN
660
EADCATVPPA IRSY
Length:664
Mass (Da):72,585
Last modified:October 1, 2002 - v1
Checksum:iDDCE1535163C9449
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti69A → V in BAE26754 (PubMed:16141072).Curated1
Sequence conflicti246R → Q in BAE26754 (PubMed:16141072).Curated1
Sequence conflicti428Q → R in BAE26754 (PubMed:16141072).Curated1
Sequence conflicti501F → L in ABD77308 (PubMed:16751257).Curated1
Sequence conflicti517K → M in ABD77308 (PubMed:16751257).Curated1
Sequence conflicti571L → M in ABD77308 (PubMed:16751257).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029520 mRNA. Translation: BAC26491.1.
AK034928 mRNA. Translation: BAC28884.1.
AK049590 mRNA. Translation: BAC33831.1.
AK050475 mRNA. Translation: BAC34276.1.
AK075990 mRNA. Translation: BAC36101.1.
AK145923 mRNA. Translation: BAE26754.1.
AK147286 mRNA. Translation: BAE27822.1.
AK147624 mRNA. Translation: BAE28032.1.
AK153085 mRNA. Translation: BAE31710.1.
AK162148 mRNA. Translation: BAE36754.1.
AK169254 mRNA. Translation: BAE41018.1.
AK004362 mRNA. Translation: BAE43173.1.
BC011301 mRNA. Translation: AAH11301.1.
BC031849 mRNA. Translation: AAH31849.1.
DQ402975 mRNA. Translation: ABD77308.1.
AF095938 mRNA. Translation: AAC72373.1.
CCDSiCCDS26643.1.
RefSeqiNP_075770.1. NM_023281.1.
UniGeneiMm.158231.

Genome annotation databases

EnsembliENSMUST00000022062; ENSMUSP00000022062; ENSMUSG00000021577.
GeneIDi66945.
KEGGimmu:66945.
UCSCiuc007rfa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029520 mRNA. Translation: BAC26491.1.
AK034928 mRNA. Translation: BAC28884.1.
AK049590 mRNA. Translation: BAC33831.1.
AK050475 mRNA. Translation: BAC34276.1.
AK075990 mRNA. Translation: BAC36101.1.
AK145923 mRNA. Translation: BAE26754.1.
AK147286 mRNA. Translation: BAE27822.1.
AK147624 mRNA. Translation: BAE28032.1.
AK153085 mRNA. Translation: BAE31710.1.
AK162148 mRNA. Translation: BAE36754.1.
AK169254 mRNA. Translation: BAE41018.1.
AK004362 mRNA. Translation: BAE43173.1.
BC011301 mRNA. Translation: AAH11301.1.
BC031849 mRNA. Translation: AAH31849.1.
DQ402975 mRNA. Translation: ABD77308.1.
AF095938 mRNA. Translation: AAC72373.1.
CCDSiCCDS26643.1.
RefSeqiNP_075770.1. NM_023281.1.
UniGeneiMm.158231.

3D structure databases

ProteinModelPortaliQ8K2B3.
SMRiQ8K2B3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211828. 1 interactor.
IntActiQ8K2B3. 7 interactors.
MINTiMINT-4122544.
STRINGi10090.ENSMUSP00000022062.

PTM databases

iPTMnetiQ8K2B3.
PhosphoSitePlusiQ8K2B3.
SwissPalmiQ8K2B3.

2D gel databases

REPRODUCTION-2DPAGEQ8K2B3.

Proteomic databases

EPDiQ8K2B3.
MaxQBiQ8K2B3.
PaxDbiQ8K2B3.
PeptideAtlasiQ8K2B3.
PRIDEiQ8K2B3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022062; ENSMUSP00000022062; ENSMUSG00000021577.
GeneIDi66945.
KEGGimmu:66945.
UCSCiuc007rfa.1. mouse.

Organism-specific databases

CTDi6389.
MGIiMGI:1914195. Sdha.

Phylogenomic databases

eggNOGiKOG2403. Eukaryota.
COG1053. LUCA.
GeneTreeiENSGT00390000010046.
HOVERGENiHBG001461.
InParanoidiQ8K2B3.
KOiK00234.
OMAiCWEEAHR.
OrthoDBiEOG091G041Z.
PhylomeDBiQ8K2B3.
TreeFamiTF300763.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01006.
ReactomeiR-MMU-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiSdha. mouse.
PROiQ8K2B3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000021577.
GenevisibleiQ8K2B3. MM.

Family and domain databases

Gene3Di1.20.58.100. 1 hit.
3.50.50.60. 2 hits.
3.90.700.10. 1 hit.
InterProiIPR003953. FAD-binding_2.
IPR023753. FAD/NAD-binding_dom.
IPR003952. FRD_SDH_FAD_BS.
IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
IPR030664. SdhA/FrdA/AprA.
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]
PIRSFiPIRSF000171. SDHA_APRA_LASPO. 1 hit.
SUPFAMiSSF46977. SSF46977. 1 hit.
SSF51905. SSF51905. 2 hits.
SSF56425. SSF56425. 1 hit.
TIGRFAMsiTIGR01816. sdhA_forward. 1 hit.
TIGR01812. sdhA_frdA_Gneg. 1 hit.
PROSITEiPS00504. FRD_SDH_FAD_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSDHA_MOUSE
AccessioniPrimary (citable) accession number: Q8K2B3
Secondary accession number(s): Q0QF19
, Q3UH25, Q3UKP7, Q3V4B1, Q921P5, Q9Z1Z4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: October 1, 2002
Last modified: November 30, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.