SDHF3_DROME
ID SDHF3_DROME Reviewed; 120 AA.
AC Q8SZ16; Q9VEU3;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Succinate dehydrogenase assembly factor 3, mitochondrial {ECO:0000303|PubMed:24954417};
DE Short=SDH assembly factor 3;
DE Short=SDHAF3 {ECO:0000303|PubMed:24954417};
DE Flags: Precursor;
GN Name=Sdhaf3 {ECO:0000303|PubMed:24954417};
GN ORFNames=CG14898 {ECO:0000312|FlyBase:FBgn0038437};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24954417; DOI=10.1016/j.cmet.2014.05.014;
RA Na U., Yu W., Cox J., Bricker D.K., Brockmann K., Rutter J., Thummel C.S.,
RA Winge D.R.;
RT "The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur
RT subunit of succinate dehydrogenase.";
RL Cell Metab. 20:253-266(2014).
CC -!- FUNCTION: Plays an essential role in the assembly of succinate
CC dehydrogenase (SDH), an enzyme complex (also referred to as respiratory
CC complex II) that is a component of both the tricarboxylic acid (TCA)
CC cycle and the mitochondrial electron transport chain, and which couples
CC the oxidation of succinate to fumarate with the reduction of ubiquinone
CC (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur
CC protein subunit SdhB of the SDH catalytic dimer, protecting it from the
CC deleterious effects of oxidants. {ECO:0000269|PubMed:24954417}.
CC -!- SUBUNIT: Interacts with SdhB within an SdhA-SdhB subcomplex.
CC {ECO:0000250|UniProtKB:Q04401}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q04401}.
CC -!- DISRUPTION PHENOTYPE: Reduces the SdhB protein level resulting in an
CC approximate 50% reduction in SDH enzymatic activity.
CC {ECO:0000269|PubMed:24954417}.
CC -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014297; AAF55325.2; -; Genomic_DNA.
DR EMBL; AY071188; AAL48810.1; -; mRNA.
DR RefSeq; NP_650552.3; NM_142295.4.
DR AlphaFoldDB; Q8SZ16; -.
DR SMR; Q8SZ16; -.
DR BioGRID; 67049; 2.
DR IntAct; Q8SZ16; 2.
DR STRING; 7227.FBpp0082759; -.
DR PaxDb; Q8SZ16; -.
DR PRIDE; Q8SZ16; -.
DR DNASU; 42004; -.
DR EnsemblMetazoa; FBtr0083308; FBpp0082759; FBgn0038437.
DR GeneID; 42004; -.
DR KEGG; dme:Dmel_CG14898; -.
DR UCSC; CG14898-RA; d. melanogaster.
DR CTD; 57001; -.
DR FlyBase; FBgn0038437; Sdhaf3.
DR VEuPathDB; VectorBase:FBgn0038437; -.
DR eggNOG; KOG4100; Eukaryota.
DR GeneTree; ENSGT00390000010029; -.
DR HOGENOM; CLU_102310_2_0_1; -.
DR InParanoid; Q8SZ16; -.
DR OMA; INQLTHP; -.
DR OrthoDB; 1613308at2759; -.
DR PhylomeDB; Q8SZ16; -.
DR BioGRID-ORCS; 42004; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42004; -.
DR PRO; PR:Q8SZ16; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038437; Expressed in adult abdomen and 29 other tissues.
DR ExpressionAtlas; Q8SZ16; baseline and differential.
DR Genevisible; Q8SZ16; DM.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR GO; GO:0050881; P:musculoskeletal movement; IMP:FlyBase.
DR GO; GO:0055093; P:response to hyperoxia; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
DR GO; GO:0006105; P:succinate metabolic process; IMP:FlyBase.
DR InterPro; IPR008381; SDHAF3/Sdh7.
DR PANTHER; PTHR13137; PTHR13137; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 37..120
FT /note="Succinate dehydrogenase assembly factor 3,
FT mitochondrial"
FT /id="PRO_0000431383"
SQ SEQUENCE 120 AA; 13894 MW; C9FA0563E1668682 CRC64;
MSRILMSQLT HPQRVRLLYK TILRLHRGLP AELRALGDNY VRDEFRRHLK CNPMEAQLFM
TEWARYASTI TQQLGIRGKP KGELGEEIDP KTVEMLKDDQ VVQLYELMLA AKGVEDAQGK
