位置:首页 > 蛋白库 > SDHB_RAT
SDHB_RAT
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   03-AUG-2022, entry version 173.
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; 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   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
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 {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
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   iPTMnet; P21913; -.
DR   PhosphoSitePlus; P21913; -.
DR   SwissPalm; P21913; -.
DR   jPOST; P21913; -.
DR   PaxDb; P21913; -.
DR   PRIDE; P21913; -.
DR   Ensembl; ENSRNOT00000105563; ENSRNOP00000088032; 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   GeneTree; ENSGT00390000013558; -.
DR   HOGENOM; CLU_044838_0_2_1; -.
DR   InParanoid; P21913; -.
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   Proteomes; UP000234681; Chromosome 5.
DR   Bgee; ENSRNOG00000007967; Expressed in heart and 20 other 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:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0045273; C:respiratory chain complex II; 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: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; IC:ComplexPortal.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC: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; IC:ComplexPortal.
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; 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; 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"
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"
FT   BINDING         100
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         198
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /ligand_note="ligand shared with DHSD"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         251
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024