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Database: UniProt
Entry: P21913
LinkDB: P21913
Original site: P21913 
ID   SDHB_RAT                Reviewed;         282 AA.
AC   P21913; B0BMZ2; Q0QEZ3;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   13-FEB-2019, entry version 161.
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; Synonyms=Sdh1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 26-257.
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 109-251.
RC   TISSUE=Brain cortex;
RX   PubMed=2494655; DOI=10.1073/pnas.86.6.1934;
RA   Gould S.J., Subramani S., Scheffler I.E.;
RT   "Use of the DNA polymerase chain reaction for homology probing:
RT   isolation of partial cDNA or genomic clones encoding the iron-sulfur
RT   protein of succinate dehydrogenase from several species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989).
RN   [5]
RP   ERRATUM.
RA   Gould S.J., Subramani S., Scheffler I.E.;
RL   Proc. Natl. Acad. Sci. U.S.A. 90:2556-2556(1993).
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 (By similarity).
CC       Interacts with SDHAF1; the interaction is required for iron-sulfur
CC       cluster incorporation into SDHB (By similarity).
CC       {ECO:0000250|UniProtKB:P21912, ECO:0000250|UniProtKB:Q007T0}.
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; CH473968; EDL80954.1; -; Genomic_DNA.
DR   EMBL; BC158620; AAI58621.1; -; mRNA.
DR   EMBL; DQ403001; ABD77134.1; -; mRNA.
DR   PIR; B32394; B32394.
DR   RefSeq; NP_001094009.1; NM_001100539.1.
DR   UniGene; Rn.3902; -.
DR   ProteinModelPortal; P21913; -.
DR   SMR; P21913; -.
DR   BioGrid; 255955; 2.
DR   ComplexPortal; CPX-564; Mitochondrial respiratory chain complex II.
DR   CORUM; P21913; -.
DR   IntAct; P21913; 1.
DR   MINT; P21913; -.
DR   STRING; 10116.ENSRNOP00000010593; -.
DR   CarbonylDB; P21913; -.
DR   iPTMnet; P21913; -.
DR   PhosphoSitePlus; P21913; -.
DR   SwissPalm; P21913; -.
DR   jPOST; P21913; -.
DR   PaxDb; P21913; -.
DR   PRIDE; P21913; -.
DR   Ensembl; ENSRNOT00000010593; ENSRNOP00000010593; ENSRNOG00000007967.
DR   GeneID; 298596; -.
DR   KEGG; rno:298596; -.
DR   UCSC; RGD:1308598; rat.
DR   CTD; 6390; -.
DR   RGD; 1308598; Sdhb.
DR   eggNOG; KOG3049; Eukaryota.
DR   eggNOG; COG0479; LUCA.
DR   GeneTree; ENSGT00390000013558; -.
DR   HOGENOM; HOG000160590; -.
DR   HOVERGEN; HBG005483; -.
DR   InParanoid; P21913; -.
DR   KO; K00235; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; 1264157at2759; -.
DR   PhylomeDB; P21913; -.
DR   TreeFam; TF300754; -.
DR   Reactome; R-RNO-71403; Citric acid cycle (TCA cycle).
DR   SABIO-RK; P21913; -.
DR   UniPathway; UPA00223; UER01006.
DR   PRO; PR:P21913; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000007967; Expressed in 10 organ(s), highest expression level in heart.
DR   Genevisible; P21913; RN.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR   GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR   GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IMP:RGD.
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; IMP:RGD.
DR   GO; GO:0006105; P:succinate metabolic process; IMP:RGD.
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   2: Evidence at transcript level;
KW   2Fe-2S; 3Fe-4S; 4Fe-4S; Acetylation; Complete proteome;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   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_0000158693.
FT   DOMAIN       56    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   REGION      148    220       Interaction with SDHAF1.
FT                                {ECO:0000250|UniProtKB:P21912}.
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:0000250|UniProtKB:Q9CQA3}.
FT   MOD_RES      57     57       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9CQA3}.
FT   CONFLICT    122    124       DLG -> NLN (in Ref. 4; no nucleotide
FT                                entry). {ECO:0000305}.
FT   CONFLICT    153    153       K -> R (in Ref. 4; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    178    178       D -> E (in Ref. 4; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    227    227       E -> D (in Ref. 4; no nucleotide entry).
FT                                {ECO:0000305}.
SQ   SEQUENCE   282 AA;  31830 MW;  6600EBC8201529A9 CRC64;
     MAAVVGVSLK RGFSATALGR VGLQFQACRE AQTAAAAAPR IKTFAIYRWD PDKAGDKPRM
     QTYKVDLNKC GPMVLDALIK IKNEIDSTLT FRRSCREGIC GSCAMNINGG NTLACTRRID
     TDLGKVSKIY PLPHMYVIKD LVPDLSNFYA QYKSIEPYLK KKDESQEGKQ QYLQSIEDRE
     KLDGLYECIL CACCSTSCPS YWWNGDKYLG PAVLMQAYRW MIDSRDEFTE ERLAKLQDPF
     SLYRCHTIMN CTQTCPKGLN PGKAIAEIKK MMATYKEKRA LA
//
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