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}.
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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 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: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.
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
//
