SDHA_MESAU
ID SDHA_MESAU Reviewed; 551 AA.
AC Q0QF17;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial {ECO:0000250|UniProtKB:P31040};
DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE AltName: Full=Flavoprotein subunit of complex II {ECO:0000250|UniProtKB:P31040};
DE Short=Fp {ECO:0000250|UniProtKB:P31040};
DE Flags: Fragment;
GN Name=SDHA {ECO:0000312|EMBL:ABD77310.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1] {ECO:0000312|EMBL:ABD77310.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver {ECO:0000312|EMBL:ABD77310.1};
RX PubMed=16751257; DOI=10.1093/molbev/msl027;
RA Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT "Housekeeping genes for phylogenetic analysis of eutherian relationships.";
RL Mol. Biol. Evol. 23:1493-1503(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
CC -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH)
CC that is involved in complex II of the mitochondrial electron transport
CC chain and is responsible for transferring electrons from succinate to
CC ubiquinone (coenzyme Q). Can act as a tumor suppressor.
CC {ECO:0000250|UniProtKB:P31040}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + succinate = a quinol + fumarate;
CC Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1;
CC Evidence={ECO:0000250|UniProtKB:P31040};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q0QF01};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate
CC from succinate (eukaryal route): step 1/1.
CC {ECO:0000250|UniProtKB:P31040}.
CC -!- SUBUNIT: Component of complex II composed of four subunits: the
CC flavoprotein (FP) SDHA, iron-sulfur protein (IP) SDHB, and a cytochrome
CC b560 composed of SDHC and SDHD (By similarity). Interacts with
CC SDHAF2/SDH5; interaction is required for FAD attachment (By
CC similarity). Interacts with TRAP1 (By similarity). Interacts with LACC1
CC (By similarity). {ECO:0000250|UniProtKB:P31040,
CC ECO:0000250|UniProtKB:Q0QF01}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q0QF01}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q0QF01}; Matrix side
CC {ECO:0000250|UniProtKB:Q0QF01}.
CC -!- PTM: Acetylated. Deacetylated by SIRT3. {ECO:0000250|UniProtKB:Q8K2B3}.
CC -!- PTM: Phosphorylation at Tyr-157 is important for efficient electron
CC transfer in complex II and the prevention of ROS generation.
CC {ECO:0000250|UniProtKB:P31040}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC FRD/SDH subfamily. {ECO:0000255}.
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DR EMBL; DQ402977; ABD77310.1; -; mRNA.
DR STRING; 10036.XP_005065480.1; -.
DR eggNOG; KOG2403; Eukaryota.
DR UniPathway; UPA00223; UER01006.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR Gene3D; 3.90.700.10; -; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR003952; FRD_SDH_FAD_BS.
DR InterPro; IPR037099; Fum_R/Succ_DH_flav-like_C_sf.
DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR InterPro; IPR030664; SdhA/FrdA/AprA.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
DR PANTHER; PTHR11632; PTHR11632; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF02910; Succ_DH_flav_C; 1.
DR SUPFAM; SSF46977; SSF46977; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF56425; SSF56425; 1.
DR TIGRFAMs; TIGR01816; sdhA_forward; 1.
DR TIGRFAMs; TIGR01812; sdhA_frdA_Gneg; 1.
DR PROSITE; PS00504; FRD_SDH_FAD_BINDING; 1.
PE 1: Evidence at protein level;
KW Acetylation; Electron transport; FAD; Flavoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transport; Tricarboxylic acid cycle;
KW Tumor suppressor.
FT CHAIN <1..>551
FT /note="Succinate dehydrogenase [ubiquinone] flavoprotein
FT subunit, mitochondrial"
FT /id="PRO_0000394746"
FT ACT_SITE 282
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9YHT1"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT BINDING 33..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT BINDING 217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT BINDING 382
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT BINDING 398..399
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT MOD_RES 41
FT /note="Tele-8alpha-FAD histidine"
FT /evidence="ECO:0000250|UniProtKB:Q0QF01"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 121
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31040"
FT MOD_RES 121
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 157
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P31040"
FT MOD_RES 192
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 192
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 277
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31040"
FT MOD_RES 277
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 365
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 422
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 427
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 427
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 440
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 440
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 459
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 480
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 489
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 489
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 492
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT MOD_RES 540
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K2B3"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:ABD77310.1"
FT NON_TER 551
FT /evidence="ECO:0000312|EMBL:ABD77310.1"
SQ SEQUENCE 551 AA; 60045 MW; 13CB219D31B9B678 CRC64;
DHEFDAVVVG AGGAGLRAAF GLSEAGFNTA CGTKLFPTRS HTVAAQGGIN AALGNMEEDN
WRWHFYDTVK GSDWLGDQDA IHYMTEQAPA SVVELENYGM PFSTTEDGKI YQRAFGGQSL
KFGKGGQAHR SCCVADRTGH SLLHTLYGRS LRYDTSYFVE NFALDLLMEN GECRGVIALC
IEDGSIHRIR AKNTVIATGG YGRTYFSCTS AHTSTGDGTA MVTRAGLPCQ DLEFIQFHPT
GIYGAGCLIT EGCRGEGGIL INSQGERFME RYAPVAKDLA SRDVVSRSMT LEIREGRSWG
PEKDHVYLQL HHLPPEQLAT RLPGISETAM IFAGVDVTKE PIPVLPTVHY NMGGIPTNYK
GQVLKHVNGQ DQVVPGLYAC GEAACASVHG AIRLGANSLL DLVVFGRACA LSIAESCSPG
DKVPPIKANA GEESVMNLDK LRFADGSIRT SELRLSMQKS MQSHAAVFRV GSVLQEGCEK
ISQLYGELKH LKTFDRGMVW NTDLVETLEL QNLMLCALQT IYGAEARKES RGAHAREDYK
VRVDEYDYYX A
