GenomeNet

Database: UniProt/SWISS-PROT
Entry: SDHA_PONAB
LinkDB: SDHA_PONAB
Original site: SDHA_PONAB 
ID   SDHA_PONAB              Reviewed;         664 AA.
AC   Q5R616;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JAN-2019, entry version 99.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE            EC=1.3.5.1 {ECO:0000250|UniProtKB:P31040};
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=Fp;
DE   Flags: Precursor;
GN   Name=SDHA;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Flavoprotein (FP) subunit of succinate dehydrogenase
CC       (SDH) that is involved in complex II of the mitochondrial electron
CC       transport chain and is responsible for transferring electrons from
CC       succinate to ubiquinone (coenzyme Q). Can act as a tumor
CC       suppressor. {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;
CC       fumarate 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
CC       cytochrome b560 composed of SDHC and SDHD (By similarity).
CC       Interacts with SDHAF2/SDH5; interaction is required for FAD
CC       attachment (By similarity). Interacts with TRAP1 (By similarity).
CC       {ECO:0000250|UniProtKB:P31040, 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.
CC       {ECO:0000250|UniProtKB:Q8K2B3}.
CC   -!- PTM: Phosphorylation at Tyr-215 is important for efficient
CC       electron transfer in complex II and the prevention of ROS
CC       generation. {ECO:0000250|UniProtKB:P31040}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily. {ECO:0000305}.
DR   EMBL; CR860684; CAH92800.1; -; mRNA.
DR   RefSeq; NP_001126633.1; NM_001133161.1.
DR   UniGene; Pab.17994; -.
DR   ProteinModelPortal; Q5R616; -.
DR   SMR; Q5R616; -.
DR   STRING; 9601.ENSPPYP00000017089; -.
DR   PRIDE; Q5R616; -.
DR   GeneID; 100173631; -.
DR   KEGG; pon:100173631; -.
DR   CTD; 6389; -.
DR   eggNOG; KOG2403; Eukaryota.
DR   eggNOG; COG1053; LUCA.
DR   HOVERGEN; HBG001461; -.
DR   InParanoid; Q5R616; -.
DR   KO; K00234; -.
DR   OrthoDB; 606981at2759; -.
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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:0055114; P:oxidation-reduction process; ISS:UniProtKB.
DR   GO; GO:0022904; P:respiratory electron transport chain; ISS:UniProtKB.
DR   GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB.
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; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR011281; Succ_DH_flav_su_fwd.
DR   InterPro; IPR014006; Succ_Dhase_FrdA_Gneg.
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   2: Evidence at transcript level;
KW   Acetylation; Complete proteome; Electron transport; FAD; Flavoprotein;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle; Tumor suppressor.
FT   TRANSIT       1     42       Mitochondrion.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   CHAIN        43    664       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000272304.
FT   NP_BIND      68     73       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   NP_BIND      91    106       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   NP_BIND     456    457       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   ACT_SITE    340    340       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:Q9YHT1}.
FT   BINDING     275    275       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     296    296       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     308    308       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     407    407       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     440    440       FAD. {ECO:0000250|UniProtKB:Q0QF01}.
FT   BINDING     451    451       Substrate.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   MOD_RES      99     99       Tele-8alpha-FAD histidine.
FT                                {ECO:0000250|UniProtKB:Q0QF01}.
FT   MOD_RES     167    167       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     179    179       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     179    179       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     182    182       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     215    215       Phosphotyrosine; by SRC.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     250    250       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     250    250       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     335    335       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     335    335       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     480    480       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     485    485       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     485    485       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     498    498       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     498    498       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     517    517       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     538    538       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     538    538       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     541    541       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     547    547       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     547    547       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     550    550       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     598    598       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     608    608       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P31040}.
FT   MOD_RES     615    615       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     624    624       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     636    636       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
FT   MOD_RES     647    647       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q8K2B3}.
SQ   SEQUENCE   664 AA;  72692 MW;  705C3B8852ADFE21 CRC64;
     MSGVRGLSRL LSARRLALAK AWPTVLQTGA RGFHFTVDGN KRASAKVSDS ISAQYPVVDH
     EFDAVVVGAG GAGLRAAFGL SEAGFNTACV TKLFPTRSHT VAAQGGINAA LGNMEEDNWR
     WHFYDTVKGS DWLGDQDAIH YMTEQAPAAV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF
     GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE
     DGSIHRIRAK NTVVATGGYG RTYFSCTSAH TSTGDGTAMI TRAGLPCQDL EFVQFHPTGI
     YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE
     KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ
     VLRHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IEESCRPGDK
     VPPIKPNAGE ESVMNLDKLR FADGSIRTSE LRLSMQKSMQ NHAAVFRVGS VLQEGCGKIS
     KLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR
     IDEYDYSKPI QGQQKKPFEE HWRKHTLSYV DVSTGKVTLE YRPVIDKTLN EADCATVPPA
     IRSY
//
DBGET integrated database retrieval system