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Database: UniProt
Entry: Q8K2B3
LinkDB: Q8K2B3
Original site: Q8K2B3 
ID   SDHA_MOUSE              Reviewed;         664 AA.
AC   Q8K2B3; Q0QF19; Q3UH25; Q3UKP7; Q3V4B1; Q921P5; Q9Z1Z4;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   09-JUL-2014, entry version 110.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial;
DE            EC=1.3.5.1;
DE   AltName: Full=Flavoprotein subunit of complex II;
DE            Short=Fp;
DE   Flags: Precursor;
GN   Name=Sdha;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Egg, Heart, Pancreas, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-14; 47-92; 121-128; 196-207; 233-246; 251-282;
RP   313-325; 362-418; 452-480; 486-498; 528-547; 601-615; 624-633 AND
RP   637-647.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 59-609.
RC   TISSUE=Liver;
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
RT   relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 74-605.
RC   TISSUE=Heart;
RA   Weinreich D.M.;
RT   "OXPHOS genes in mammals and the molecular clock.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   ACETYLATION AT LYS-179; LYS-182; LYS-250; LYS-335; LYS-480; LYS-485;
RP   LYS-498; LYS-547; LYS-550; LYS-598; LYS-608; LYS-624 AND LYS-633,
RP   DEACETYLATION BY SIRT3, AND MUTAGENESIS OF LYS-.
RX   PubMed=21858060; DOI=10.1371/journal.pone.0023295;
RA   Finley L.W., Haas W., Desquiret-Dumas V., Wallace D.C., Procaccio V.,
RA   Gygi S.P., Haigis M.C.;
RT   "Succinate dehydrogenase is a direct target of sirtuin 3 deacetylase
RT   activity.";
RL   PLoS ONE 6:E23295-E23295(2011).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179 AND LYS-547,
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-179; LYS-250; LYS-335;
RP   LYS-485; LYS-498; LYS-538; LYS-547 AND LYS-615, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167; LYS-179; LYS-182;
RP   LYS-335; LYS-423; LYS-498; LYS-517; LYS-538; LYS-547; LYS-608; LYS-636
RP   AND LYS-647, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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) (By similarity). Can act as a
CC       tumor suppressor (By similarity).
CC   -!- CATALYTIC ACTIVITY: Succinate + a quinone = fumarate + a quinol.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       fumarate from succinate (eukaryal route): step 1/1.
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. Interacts with
CC       SDHAF2/SDH5; interaction is required for FAD attachment (By
CC       similarity). Interacts with TRAP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- PTM: Acetylation of Lys-498 and Lys-538 is observed in liver
CC       mitochondria from fasted mice but not from fed mice. Deacetylated
CC       by SIRT3.
CC   -!- PTM: Phosphorylation at Tyr-215 is important for efficient
CC       electron transfer in complex II and the prevention of ROS
CC       generation (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family.
CC       FRD/SDH subfamily.
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DR   EMBL; AK029520; BAC26491.1; -; mRNA.
DR   EMBL; AK034928; BAC28884.1; -; mRNA.
DR   EMBL; AK049590; BAC33831.1; -; mRNA.
DR   EMBL; AK050475; BAC34276.1; -; mRNA.
DR   EMBL; AK075990; BAC36101.1; -; mRNA.
DR   EMBL; AK145923; BAE26754.1; -; mRNA.
DR   EMBL; AK147286; BAE27822.1; -; mRNA.
DR   EMBL; AK147624; BAE28032.1; -; mRNA.
DR   EMBL; AK153085; BAE31710.1; -; mRNA.
DR   EMBL; AK162148; BAE36754.1; -; mRNA.
DR   EMBL; AK169254; BAE41018.1; -; mRNA.
DR   EMBL; AK004362; BAE43173.1; -; mRNA.
DR   EMBL; BC011301; AAH11301.1; -; mRNA.
DR   EMBL; BC031849; AAH31849.1; -; mRNA.
DR   EMBL; DQ402975; ABD77308.1; -; mRNA.
DR   EMBL; AF095938; AAC72373.1; -; mRNA.
DR   CCDS; CCDS26643.1; -.
DR   RefSeq; NP_075770.1; NM_023281.1.
DR   UniGene; Mm.158231; -.
DR   ProteinModelPortal; Q8K2B3; -.
DR   SMR; Q8K2B3; 52-664.
DR   IntAct; Q8K2B3; 7.
DR   MINT; MINT-4122544; -.
DR   PhosphoSite; Q8K2B3; -.
DR   REPRODUCTION-2DPAGE; Q8K2B3; -.
DR   MaxQB; Q8K2B3; -.
DR   PaxDb; Q8K2B3; -.
DR   PRIDE; Q8K2B3; -.
DR   Ensembl; ENSMUST00000022062; ENSMUSP00000022062; ENSMUSG00000021577.
DR   GeneID; 66945; -.
DR   KEGG; mmu:66945; -.
DR   UCSC; uc007rfa.1; mouse.
DR   CTD; 6389; -.
DR   MGI; MGI:1914195; Sdha.
DR   eggNOG; COG1053; -.
DR   GeneTree; ENSGT00390000010046; -.
DR   HOVERGEN; HBG001461; -.
DR   InParanoid; Q8K2B3; -.
DR   KO; K00234; -.
DR   OMA; RTEQGRI; -.
DR   OrthoDB; EOG7MH0XJ; -.
DR   PhylomeDB; Q8K2B3; -.
DR   TreeFam; TF300763; -.
DR   UniPathway; UPA00223; UER01006.
DR   ChiTaRS; SdhA; mouse.
DR   NextBio; 323092; -.
DR   PRO; PR:Q8K2B3; -.
DR   ArrayExpress; Q8K2B3; -.
DR   Bgee; Q8K2B3; -.
DR   Genevestigator; Q8K2B3; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0007399; P:nervous system development; IEA:Ensembl.
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; 1.20.58.100; -; 1.
DR   Gene3D; 3.90.700.10; -; 1.
DR   InterPro; IPR003953; FAD_bind_dom.
DR   InterPro; IPR003952; FRD_SDH_FAD_BS.
DR   InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat.
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; 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; Complete proteome; Direct protein sequencing;
KW   Electron transport; FAD; Flavoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle; Tumor suppressor.
FT   TRANSIT       1     43       Mitochondrion (By similarity).
FT   CHAIN        44    664       Succinate dehydrogenase [ubiquinone]
FT                                flavoprotein subunit, mitochondrial.
FT                                /FTId=PRO_0000010337.
FT   NP_BIND      68     73       FAD (By similarity).
FT   NP_BIND      91    106       FAD (By similarity).
FT   NP_BIND     456    457       FAD (By similarity).
FT   ACT_SITE    340    340       Proton acceptor (By similarity).
FT   BINDING     275    275       FAD (By similarity).
FT   BINDING     296    296       Substrate (By similarity).
FT   BINDING     308    308       Substrate (By similarity).
FT   BINDING     407    407       Substrate (By similarity).
FT   BINDING     440    440       FAD (By similarity).
FT   BINDING     451    451       Substrate (By similarity).
FT   MOD_RES      99     99       Tele-8alpha-FAD histidine (By
FT                                similarity).
FT   MOD_RES     167    167       N6-acetyllysine.
FT   MOD_RES     179    179       N6-acetyllysine; alternate.
FT   MOD_RES     179    179       N6-succinyllysine; alternate.
FT   MOD_RES     182    182       N6-acetyllysine.
FT   MOD_RES     215    215       Phosphotyrosine; by SRC (By similarity).
FT   MOD_RES     250    250       N6-acetyllysine; alternate.
FT   MOD_RES     250    250       N6-succinyllysine; alternate.
FT   MOD_RES     335    335       N6-acetyllysine; alternate.
FT   MOD_RES     335    335       N6-succinyllysine; alternate.
FT   MOD_RES     423    423       N6-acetyllysine.
FT   MOD_RES     480    480       N6-acetyllysine.
FT   MOD_RES     485    485       N6-acetyllysine; alternate.
FT   MOD_RES     485    485       N6-succinyllysine; alternate.
FT   MOD_RES     498    498       N6-acetyllysine; alternate.
FT   MOD_RES     498    498       N6-succinyllysine; alternate.
FT   MOD_RES     517    517       N6-acetyllysine.
FT   MOD_RES     538    538       N6-acetyllysine; alternate.
FT   MOD_RES     538    538       N6-succinyllysine; alternate.
FT   MOD_RES     547    547       N6-acetyllysine; alternate.
FT   MOD_RES     547    547       N6-succinyllysine; alternate.
FT   MOD_RES     550    550       N6-acetyllysine.
FT   MOD_RES     598    598       N6-acetyllysine.
FT   MOD_RES     608    608       N6-acetyllysine.
FT   MOD_RES     615    615       N6-succinyllysine.
FT   MOD_RES     624    624       N6-acetyllysine.
FT   MOD_RES     633    633       N6-acetyllysine.
FT   MOD_RES     636    636       N6-acetyllysine.
FT   MOD_RES     647    647       N6-acetyllysine.
FT   CONFLICT     69     69       A -> V (in Ref. 1; BAE26754).
FT   CONFLICT    246    246       R -> Q (in Ref. 1; BAE26754).
FT   CONFLICT    428    428       Q -> R (in Ref. 1; BAE26754).
FT   CONFLICT    501    501       F -> L (in Ref. 4; ABD77308).
FT   CONFLICT    517    517       K -> M (in Ref. 4; ABD77308).
FT   CONFLICT    571    571       L -> M (in Ref. 4; ABD77308).
SQ   SEQUENCE   664 AA;  72585 MW;  DDCE1535163C9449 CRC64;
     MAGVGAVSRL LRGRRLALTG AWPGTLQKQT CGFHFSVGEN KKASAKVSDA ISTQYPVVDH
     EFDAVVVGAG GAGLRAAFGL SEAGFNTACL TKLFPTRSHT VAAQGGINAA LGNMEEDNWR
     WHFYDTVKGS DWLGDQDAIH YMTEQAPASV VELENYGMPF SRTEDGKIYQ RAFGGQSLKF
     GKGGQAHRCC CVADRTGHSL LHTLYGRSLR YDTSYFVEYF ALDLLMENGE CRGVIALCIE
     DGSIHRIRAK NTVIATGGYG RTYFSCTSAH TSTGDGTAMV TRAGLPCQDL EFVQFHPTGI
     YGAGCLITEG CRGEGGILIN SQGERFMERY APVAKDLASR DVVSRSMTLE IREGRGCGPE
     KDHVYLQLHH LPPEQLATRL PGISETAMIF AGVDVTKEPI PVLPTVHYNM GGIPTNYKGQ
     VLKHVNGQDQ IVPGLYACGE AACASVHGAN RLGANSLLDL VVFGRACALS IAESCRPGDK
     VPSIKANAGE ESVMNLDKLR FADGSIRTSE LRLNMQKSMQ NHAAVFRVGS VLQEGCEKIS
     QLYGDLKHLK TFDRGMVWNT DLVETLELQN LMLCALQTIY GAEARKESRG AHAREDYKVR
     VDEYDYSKPI QGQQKKPFGE HWRKHTLSYV DIKTGKVTLE YRPVIDKTLN EADCATVPPA
     IRSY
//
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