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Database: UniProt/SWISS-PROT
Entry: SDHB_MOUSE
LinkDB: SDHB_MOUSE
Original site: SDHB_MOUSE 
ID   SDHB_MOUSE              Reviewed;         282 AA.
AC   Q9CQA3; Q3TF82; Q9DC91;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JAN-2019, entry version 146.
DE   RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;
DE            EC=1.3.5.1;
DE   AltName: Full=Iron-sulfur subunit of complex II;
DE            Short=Ip;
DE   Flags: Precursor;
GN   Name=Sdhb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Brain, and Tongue;
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=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
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 49-92; 118-153; 170-179; 208-232 AND 245-257, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-57, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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: Iron-sulfur protein (IP) subunit of succinate
CC       dehydrogenase (SDH) that is involved in complex II of the
CC       mitochondrial electron transport chain and is responsible for
CC       transferring electrons from succinate to ubiquinone (coenzyme Q).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Matrix side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate
CC       reductase iron-sulfur protein family. {ECO:0000305}.
DR   EMBL; AK003052; BAB22534.1; -; mRNA.
DR   EMBL; AK003533; BAB22842.1; -; mRNA.
DR   EMBL; AK009660; BAB26422.1; -; mRNA.
DR   EMBL; AK153045; BAE31674.1; -; mRNA.
DR   EMBL; AK169252; BAE41016.1; -; mRNA.
DR   EMBL; BC013509; AAH13509.1; -; mRNA.
DR   EMBL; BC051934; AAH51934.1; -; mRNA.
DR   CCDS; CCDS18858.1; -.
DR   PIR; PT0094; PT0094.
DR   RefSeq; NP_075863.2; NM_023374.3.
DR   UniGene; Mm.246965; -.
DR   ProteinModelPortal; Q9CQA3; -.
DR   SMR; Q9CQA3; -.
DR   BioGrid; 212362; 4.
DR   ComplexPortal; CPX-562; Mitochondrial respiratory chain complex II.
DR   CORUM; Q9CQA3; -.
DR   IntAct; Q9CQA3; 9.
DR   MINT; Q9CQA3; -.
DR   STRING; 10090.ENSMUSP00000010007; -.
DR   iPTMnet; Q9CQA3; -.
DR   PhosphoSitePlus; Q9CQA3; -.
DR   SwissPalm; Q9CQA3; -.
DR   REPRODUCTION-2DPAGE; Q9CQA3; -.
DR   EPD; Q9CQA3; -.
DR   jPOST; Q9CQA3; -.
DR   MaxQB; Q9CQA3; -.
DR   PaxDb; Q9CQA3; -.
DR   PeptideAtlas; Q9CQA3; -.
DR   PRIDE; Q9CQA3; -.
DR   Ensembl; ENSMUST00000010007; ENSMUSP00000010007; ENSMUSG00000009863.
DR   GeneID; 67680; -.
DR   KEGG; mmu:67680; -.
DR   UCSC; uc008vnl.1; mouse.
DR   CTD; 6390; -.
DR   MGI; MGI:1914930; Sdhb.
DR   eggNOG; KOG3049; Eukaryota.
DR   eggNOG; COG0479; LUCA.
DR   GeneTree; ENSGT00390000013558; -.
DR   HOGENOM; HOG000160590; -.
DR   HOVERGEN; HBG005483; -.
DR   InParanoid; Q9CQA3; -.
DR   KO; K00235; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; 1264157at2759; -.
DR   PhylomeDB; Q9CQA3; -.
DR   TreeFam; TF300754; -.
DR   Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   ChiTaRS; Sdhb; mouse.
DR   PRO; PR:Q9CQA3; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   Bgee; ENSMUSG00000009863; Expressed in 314 organ(s), highest expression level in cardiac ventricle.
DR   Genevisible; Q9CQA3; MM.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0045273; C:respiratory chain complex II; IDA:MGI.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISO:MGI.
DR   GO; GO:0048039; F:ubiquinone binding; ISS:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR   GO; GO:0022904; P:respiratory electron transport chain; ISO:MGI.
DR   GO; GO:0006105; P:succinate metabolic process; ISO:MGI.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S.
DR   InterPro; IPR025192; Succ_DH/fum_Rdtase_N.
DR   Pfam; PF13085; Fer2_3; 1.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   TIGRFAMs; TIGR00384; dhsB; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Acetylation; Complete proteome;
KW   Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Oxidoreductase; Reference proteome; Transit peptide; Transport;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     30       Mitochondrion. {ECO:0000250}.
FT   CHAIN        31    282       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit, mitochondrial.
FT                                /FTId=PRO_0000010356.
FT   DOMAIN       42    135       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      178    208       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        95     95       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       100    100       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       103    103       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       115    115       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       188    188       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       191    191       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       194    194       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       198    198       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       245    245       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       251    251       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       255    255       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   BINDING     203    203       Ubiquinone; shared with DHSD.
FT                                {ECO:0000250}.
FT   MOD_RES      53     53       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES      57     57       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   CONFLICT     40     40       R -> K (in Ref. 1; BAB22534).
FT                                {ECO:0000305}.
SQ   SEQUENCE   282 AA;  31814 MW;  A8616A911427AF8E CRC64;
     MAATVGVSLK RGFPAAVLGR VGLQFQACRG AQTAAAAAPR IKKFAIYRWD PDKTGDKPRM
     QTYEVDLNKC GPMVLDALIK IKNEVDSTLT FRRSCREGIC GSCAMNINGG NTLACTRRID
     TDLSKVSKIY PLPHMYVIKD LVPDLSNFYA QYKSIEPYLK KKDESQEGKQ QYLQSIEDRE
     KLDGLYECIL CACCSTSCPS YWWNGDKYLG PAVLMQAYRW MIDSRDDFTE ERLAKLQDPF
     SVYRCHTIMN CTQTCPKGLN PGKAIAEIKK MMATYKEKRA LA
//
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