SDH4_ARATH
ID SDH4_ARATH Reviewed; 151 AA.
AC Q941A0;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Succinate dehydrogenase subunit 4, mitochondrial {ECO:0000305};
DE Flags: Precursor;
GN Name=SDH4 {ECO:0000305};
GN OrderedLocusNames=At2g46505 {ECO:0000312|Araport:AT2G46505};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11454775; DOI=10.1093/genetics/158.3.1289;
RA Adams K.L., Rosenblueth M., Qiu Y.L., Palmer J.D.;
RT "Multiple losses and transfers to the nucleus of two mitochondrial
RT succinate dehydrogenase genes during angiosperm evolution.";
RL Genetics 158:1289-1300(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12374303; DOI=10.1023/a:1019926301981;
RA Figueroa P., Leon G., Elorza A., Holuigue L., Araya A., Jordana X.;
RT "The four subunits of mitochondrial respiratory complex II are encoded by
RT multiple nuclear genes and targeted to mitochondria in Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 50:725-734(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=15604729; DOI=10.1007/s11103-004-2316-2;
RA Millar A.H., Eubel H., Jansch L., Kruft V., Heazlewood J.L., Braun H.P.;
RT "Mitochondrial cytochrome c oxidase and succinate dehydrogenase complexes
RT contain plant specific subunits.";
RL Plant Mol. Biol. 56:77-90(2004).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC {ECO:0000250|UniProtKB:P69054}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P69054};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000305}.
CC -!- SUBUNIT: Component of complex II composed of eight subunits in plants:
CC four classical SDH subunits SDH1, SDH2, SDH3 and SDH4 (a flavoprotein
CC (FP), an iron-sulfur protein (IP), and a cytochrome b composed of a
CC large and a small subunit.), as well as four subunits unknown in
CC mitochondria from bacteria and heterotrophic eukaryotes.
CC {ECO:0000269|PubMed:15604729}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, inflorescences and stems.
CC {ECO:0000269|PubMed:12374303}.
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DR EMBL; BK000036; DAA00016.1; -; Genomic_DNA.
DR EMBL; AC006418; AAM15243.1; -; Genomic_DNA.
DR EMBL; AC006526; AAM15261.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10711.1; -; Genomic_DNA.
DR EMBL; AY052323; AAK96516.1; -; mRNA.
DR EMBL; AY061903; AAL31230.1; -; mRNA.
DR EMBL; AY084510; AAM61078.1; -; mRNA.
DR RefSeq; NP_566077.1; NM_130215.3.
DR AlphaFoldDB; Q941A0; -.
DR STRING; 3702.AT2G46505.1; -.
DR PaxDb; Q941A0; -.
DR PRIDE; Q941A0; -.
DR ProteomicsDB; 234495; -.
DR EnsemblPlants; AT2G46505.1; AT2G46505.1; AT2G46505.
DR GeneID; 819261; -.
DR Gramene; AT2G46505.1; AT2G46505.1; AT2G46505.
DR KEGG; ath:AT2G46505; -.
DR Araport; AT2G46505; -.
DR TAIR; locus:505006320; AT2G46505.
DR eggNOG; ENOG502SAZF; Eukaryota.
DR HOGENOM; CLU_1847890_0_0_1; -.
DR InParanoid; Q941A0; -.
DR OMA; HIHEGME; -.
DR OrthoDB; 1466762at2759; -.
DR BioCyc; MetaCyc:AT2G46505-MON; -.
DR UniPathway; UPA00223; -.
DR PRO; PR:Q941A0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q941A0; baseline and differential.
DR Genevisible; Q941A0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005749; C:mitochondrial respiratory chain complex II, succinate dehydrogenase complex (ubiquinone); IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0045273; C:respiratory chain complex II; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; ISS:TAIR.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:TAIR.
DR InterPro; IPR044963; SDH4.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR36358; PTHR36358; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
PE 1: Evidence at protein level;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..78
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 79..151
FT /note="Succinate dehydrogenase subunit 4, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431749"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 109
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with second transmembrane
FT subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P0AC44"
FT BINDING 121
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250|UniProtKB:P0AC44"
SQ SEQUENCE 151 AA; 16842 MW; 0C7E03F8355E4ABB CRC64;
MSLRRTILDL HRQTQRATLS KSLPFSMSHI SSASATAAVR NPLGRDLSSI PFAQAQKLKP
DSTNLVTDRS ISSSIGQSEL NKAAKFSRQS SSRGYTNGSF LRKIPVVFHI HEGMEEILAD
YVHQEMTRNL IVMSLGLFQI IVLKDIILFL L