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 24-JAN-2024, entry version 180. DE RecName: Full=Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial; DE EC=1.3.5.1 {ECO:0000250|UniProtKB:P21912}; 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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 project: RT 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 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: isolation RT of partial cDNA or genomic clones encoding the iron-sulfur protein of RT succinate dehydrogenase from several species."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1934-1938(1989). RN [5] RP ERRATUM OF PUBMED:2494655. 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 the succinate CC dehydrogenase complex (mitochondrial respiratory chain complex II), CC responsible for transferring electrons from succinate to ubiquinone CC (coenzyme Q). {ECO:0000250|UniProtKB:P21912}. 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:P21912}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Evidence={ECO:0000250|UniProtKB:Q007T0}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:Q007T0}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000250|UniProtKB:Q007T0}; CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:Q007T0}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:Q007T0}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q007T0}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate CC 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 cytochrome CC b560 composed of SDHC and SDHD (By similarity). Interacts with SDHAF1; CC the interaction is required for iron-sulfur cluster incorporation into CC SDHB (By similarity). {ECO:0000250|UniProtKB:P21912, CC ECO:0000250|UniProtKB:Q007T0}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:Q9YHT2}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q9YHT2}; Matrix side CC {ECO:0000250|UniProtKB:Q9YHT2}. CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase CC iron-sulfur protein family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P21913; -. DR SMR; P21913; -. DR BioGRID; 255955; 2. DR ComplexPortal; CPX-564; Mitochondrial respiratory chain complex II. DR CORUM; P21913; -. DR IntAct; P21913; 2. DR MINT; P21913; -. DR STRING; 10116.ENSRNOP00000010593; -. DR CarbonylDB; P21913; -. DR GlyGen; P21913; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P21913; -. DR PhosphoSitePlus; P21913; -. DR SwissPalm; P21913; -. DR jPOST; P21913; -. DR PaxDb; 10116-ENSRNOP00000010593; -. DR Ensembl; ENSRNOT00000105563.1; ENSRNOP00000088032.1; ENSRNOG00000007967.8. DR Ensembl; ENSRNOT00060041764; ENSRNOP00060034624; ENSRNOG00060024101. DR GeneID; 298596; -. DR KEGG; rno:298596; -. DR UCSC; RGD:1308598; rat. DR AGR; RGD:1308598; -. DR CTD; 6390; -. DR RGD; 1308598; Sdhb. DR eggNOG; KOG3049; Eukaryota. DR GeneTree; ENSGT00390000013558; -. DR HOGENOM; CLU_044838_0_2_1; -. DR InParanoid; P21913; -. DR OrthoDB; 119960at2759; -. 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 Proteomes; UP000234681; Chromosome 5. DR Bgee; ENSRNOG00000007967; Expressed in heart and 20 other cell types or tissues. 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:0005739; C:mitochondrion; ISO:RGD. DR GO; GO:0045273; C:respiratory chain complex II; ISO:RGD. DR GO; GO:0045257; C:succinate dehydrogenase complex (ubiquinone); ISO:RGD. 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:0102040; F:fumarate reductase (menaquinone); IEA:UniProtKB-EC. 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:0006121; P:mitochondrial electron transport, succinate to ubiquinone; NAS:ComplexPortal. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal. 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; NAS:ComplexPortal. DR CDD; cd00207; fer2; 1. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 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 NCBIfam; TIGR00384; dhsB; 1. DR PANTHER; PTHR11921:SF29; SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT, MITOCHONDRIAL; 1. DR PANTHER; PTHR11921; SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN; 1. DR Pfam; PF13085; Fer2_3; 1. DR Pfam; PF13534; Fer4_17; 1. DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1. DR SUPFAM; SSF46548; alpha-helical ferredoxin; 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. DR Genevisible; P21913; RN. PE 2: Evidence at transcript level; KW 2Fe-2S; 3Fe-4S; 4Fe-4S; Acetylation; 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 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:P21912" FT CHAIN 31..282 FT /note="Succinate dehydrogenase [ubiquinone] iron-sulfur FT subunit, mitochondrial" FT /id="PRO_0000158693" FT DOMAIN 56..135 FT /note="2Fe-2S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465" FT DOMAIN 178..208 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT REGION 148..220 FT /note="Interaction with SDHAF1" FT /evidence="ECO:0000250|UniProtKB:P21912" FT BINDING 95 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 100 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 103 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 115 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 188 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 191 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 194 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 198 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 203 FT /ligand="a ubiquinone" FT /ligand_id="ChEBI:CHEBI:16389" FT /ligand_note="ligand shared with DHSD" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 245 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 251 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT BINDING 255 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:Q007T0" FT MOD_RES 53 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CQA3" FT MOD_RES 57 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9CQA3" FT CONFLICT 122..124 FT /note="DLG -> NLN (in Ref. 4; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 153 FT /note="K -> R (in Ref. 4; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="D -> E (in Ref. 4; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 227 FT /note="E -> D (in Ref. 4; no nucleotide entry)" FT /evidence="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 //