SDH32_ARATH
ID SDH32_ARATH Reviewed; 213 AA.
AC P0DKI1; O49369; Q9LXC4;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Succinate dehydrogenase subunit 3-2, mitochondrial {ECO:0000305};
DE Flags: Precursor;
GN Name=SDH3-2 {ECO:0000305};
GN OrderedLocusNames=At4g32210 {ECO:0000312|Araport:AT4G32210};
GN ORFNames=F10M6.150 {ECO:0000312|EMBL:CAA16969.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 [6]
RP PROTEIN SEQUENCE OF 106-119, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12970493; DOI=10.1104/pp.103.024620;
RA Eubel H., Jansch L., Braun H.P.;
RT "New insights into the respiratory chain of plant mitochondria.
RT Supercomplexes and a unique composition of complex II.";
RL Plant Physiol. 133:274-286(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16969.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79939.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BK000035; DAA00015.1; -; Genomic_DNA.
DR EMBL; AL021811; CAA16969.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161580; CAB79939.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86020.1; -; Genomic_DNA.
DR EMBL; AY070732; AAL50073.1; -; mRNA.
DR PIR; T05407; T05407.
DR RefSeq; NP_001190268.1; NM_001203339.2.
DR RefSeq; NP_194948.2; NM_119373.3.
DR RefSeq; NP_196522.1; NM_120997.4.
DR AlphaFoldDB; P0DKI1; -.
DR SMR; P0DKI1; -.
DR EnsemblPlants; AT4G32210.1; AT4G32210.1; AT4G32210.
DR EnsemblPlants; AT5G09600.1; AT5G09600.1; AT5G09600.
DR EnsemblPlants; AT5G09600.3; AT5G09600.3; AT5G09600.
DR GeneID; 3770570; -.
DR GeneID; 830819; -.
DR Gramene; AT4G32210.1; AT4G32210.1; AT4G32210.
DR Gramene; AT5G09600.1; AT5G09600.1; AT5G09600.
DR Gramene; AT5G09600.3; AT5G09600.3; AT5G09600.
DR KEGG; ath:AT4G32210; -.
DR KEGG; ath:AT5G09600; -.
DR Araport; AT4G32210; -.
DR HOGENOM; CLU_112617_0_0_1; -.
DR OMA; ICFTHYN; -.
DR OrthoDB; 1375683at2759; -.
DR PhylomeDB; P0DKI1; -.
DR UniPathway; UPA00223; -.
DR PRO; PR:P0DKI1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P0DKI1; baseline and differential.
DR Genevisible; P0DKI1; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045273; C:respiratory chain complex II; IDA:UniProtKB.
DR GO; GO:0045281; C:succinate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR PANTHER; PTHR10978; PTHR10978; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport; Tricarboxylic acid cycle.
FT TRANSIT 1..105
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:12970493"
FT CHAIN 106..213
FT /note="Succinate dehydrogenase subunit 3-2, mitochondrial"
FT /evidence="ECO:0000269|PubMed:12970493"
FT /id="PRO_0000431746"
FT TRANSMEM 148..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 130
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:P69054"
SQ SEQUENCE 213 AA; 23454 MW; 16C229DEE106E0A1 CRC64;
MAATALFRSI RRRDVVSAPL SVYKSLAGNA QPSWGSSYIG QNYASFSRAF GSKPVVNDIL
GTGLGTNNAI REEREKSKST EAAIVGAQLT RSFRALDVGT SKRLFSTISG DIKTTQEEPK
IKSFRPLSPH LSVYQPQMNS MLSIFNRISG VYLTGVTFAG YLLYLKMGMI CLTYPSFYQV
LYHTQQQLPV ITSVTALAAI YHTIKSTHSL LTH
