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Database: UniProt/SWISS-PROT
Entry: SDHB_BOVIN
LinkDB: SDHB_BOVIN
Original site: SDHB_BOVIN 
ID   SDHB_BOVIN              Reviewed;         280 AA.
AC   Q3T189;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   13-FEB-2019, entry version 109.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BC102067; AAI02068.1; -; mRNA.
DR   RefSeq; NP_001035573.1; NM_001040483.1.
DR   UniGene; Bt.13128; -.
DR   ProteinModelPortal; Q3T189; -.
DR   SMR; Q3T189; -.
DR   CORUM; Q3T189; -.
DR   IntAct; Q3T189; 2.
DR   STRING; 9913.ENSBTAP00000010949; -.
DR   PaxDb; Q3T189; -.
DR   PeptideAtlas; Q3T189; -.
DR   PRIDE; Q3T189; -.
DR   Ensembl; ENSBTAT00000010949; ENSBTAP00000010949; ENSBTAG00000008314.
DR   GeneID; 286840; -.
DR   KEGG; bta:286840; -.
DR   CTD; 6390; -.
DR   VGNC; VGNC:34391; SDHB.
DR   eggNOG; KOG3049; Eukaryota.
DR   eggNOG; COG0479; LUCA.
DR   GeneTree; ENSGT00390000013558; -.
DR   HOGENOM; HOG000160590; -.
DR   HOVERGEN; HBG005483; -.
DR   InParanoid; Q3T189; -.
DR   KO; K00235; -.
DR   OMA; DGQYFGP; -.
DR   OrthoDB; 1264157at2759; -.
DR   TreeFam; TF300754; -.
DR   Reactome; R-BTA-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; UER01006.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000008314; Expressed in 10 organ(s), highest expression level in heart.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
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: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; IEA:UniProtKB-EC.
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; IBA:GO_Central.
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     28       Mitochondrion. {ECO:0000250}.
FT   CHAIN        29    280       Succinate dehydrogenase [ubiquinone]
FT                                iron-sulfur subunit, mitochondrial.
FT                                /FTId=PRO_0000247594.
FT   DOMAIN       40    133       2Fe-2S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00465}.
FT   DOMAIN      176    206       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   REGION      146    218       Interaction with SDHAF1.
FT                                {ECO:0000250|UniProtKB:P21912}.
FT   METAL        93     93       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL        98     98       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       101    101       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       113    113       Iron-sulfur 1 (2Fe-2S). {ECO:0000250}.
FT   METAL       186    186       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       189    189       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       192    192       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       196    196       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       243    243       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       249    249       Iron-sulfur 3 (3Fe-4S). {ECO:0000250}.
FT   METAL       253    253       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   BINDING     201    201       Ubiquinone; shared with DHSD.
FT                                {ECO:0000250}.
FT   MOD_RES      51     51       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9CQA3}.
FT   MOD_RES      55     55       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q9CQA3}.
SQ   SEQUENCE   280 AA;  31518 MW;  BE51FF2193F8B6C5 CRC64;
     MAAVVALSLR RRFPAAALGG ARLQACRGAQ TAAAAAPRIK KFAIYRWDPD KTGDKPHMQT
     YEIDLNNCGP MVLDALIKIK NEIDSTLTFR RSCREGICGS CAMNINGGNT LACTRRIDTN
     LSKVSKIYPL PHMYVIKDLV PDLSNFYAQY KSIEPYLKKK DESQGGKEQY LQSIEDREKL
     DGLYECILCA CCSTSCPSYW WNGDKYLGPA VLMQAYRWMI DSRDDFTEER LAKLQDPFSL
     YRCHTIMNCT QTCPKGLNPG KAIAEIKKMM ATYKEKQASA
//
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