SDHF4_DROME
ID SDHF4_DROME Reviewed; 118 AA.
AC Q9VLU6;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Succinate dehydrogenase assembly factor 4, mitochondrial {ECO:0000303|PubMed:24954416};
DE Short=SDH assembly factor 4 {ECO:0000303|PubMed:24954416};
DE Short=SDHAF4 {ECO:0000303|PubMed:24954416};
DE AltName: Full=Starvation-upregulated protein {ECO:0000312|FlyBase:FBgn0031971};
DE Flags: Precursor;
GN Name=Sirup {ECO:0000312|FlyBase:FBgn0031971};
GN Synonyms=Sdhaf4 {ECO:0000303|PubMed:24954416};
GN ORFNames=CG7224 {ECO:0000312|FlyBase:FBgn0031971};
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].
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=24954416; DOI=10.1016/j.cmet.2014.05.012;
RA Van Vranken J.G., Bricker D.K., Dephoure N., Gygi S.P., Cox J.E.,
RA Thummel C.S., Rutter J.;
RT "SDHAF4 promotes mitochondrial succinate dehydrogenase activity and
RT prevents neurodegeneration.";
RL Cell Metab. 20:241-252(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 (PubMed:24954416). Binds to the flavoprotein
CC subunit SdhA in its FAD-bound form, blocking the generation of excess
CC reactive oxigen species (ROS) and facilitating its assembly with the
CC iron-sulfur protein subunit SdhB into the SDH catalytic dimer (By
CC similarity). {ECO:0000250|UniProtKB:P38345,
CC ECO:0000269|PubMed:24954416}.
CC -!- SUBUNIT: Interacts with SdhA in its FAD-bound form.
CC {ECO:0000250|UniProtKB:P38345}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:P38345}.
CC -!- SIMILARITY: Belongs to the SDHAF4 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; AE014296; AAF52586.2; -; Genomic_DNA.
DR EMBL; AE014134; AHN54248.1; -; Genomic_DNA.
DR EMBL; BT056317; ACL81239.1; -; mRNA.
DR RefSeq; NP_001285734.1; NM_001298805.1.
DR RefSeq; NP_609170.1; NM_135326.5.
DR AlphaFoldDB; Q9VLU6; -.
DR BioGRID; 60223; 5.
DR IntAct; Q9VLU6; 3.
DR STRING; 7227.FBpp0079154; -.
DR PaxDb; Q9VLU6; -.
DR PRIDE; Q9VLU6; -.
DR DNASU; 34089; -.
DR EnsemblMetazoa; FBtr0079532; FBpp0079154; FBgn0031971.
DR EnsemblMetazoa; FBtr0343382; FBpp0310037; FBgn0031971.
DR GeneID; 34089; -.
DR KEGG; dme:Dmel_CG7224; -.
DR UCSC; CG7224-RA; d. melanogaster.
DR CTD; 34089; -.
DR FlyBase; FBgn0031971; Sirup.
DR VEuPathDB; VectorBase:FBgn0031971; -.
DR eggNOG; KOG3245; Eukaryota.
DR GeneTree; ENSGT00390000009155; -.
DR HOGENOM; CLU_160299_0_2_1; -.
DR InParanoid; Q9VLU6; -.
DR OMA; MGKQVSY; -.
DR OrthoDB; 1530126at2759; -.
DR PhylomeDB; Q9VLU6; -.
DR SignaLink; Q9VLU6; -.
DR BioGRID-ORCS; 34089; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Sirup; fly.
DR GenomeRNAi; 34089; -.
DR PRO; PR:Q9VLU6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0031971; Expressed in capitellum (Drosophila) and 59 other tissues.
DR ExpressionAtlas; Q9VLU6; baseline and differential.
DR Genevisible; Q9VLU6; DM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; IMP:UniProtKB.
DR GO; GO:0045333; P:cellular respiration; IMP:UniProtKB.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IGI:UniProtKB.
DR GO; GO:1904231; P:positive regulation of succinate dehydrogenase activity; IMP:UniProtKB.
DR InterPro; IPR012875; SDHF4.
DR Pfam; PF07896; DUF1674; 1.
PE 3: Inferred from homology;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..118
FT /note="Succinate dehydrogenase assembly factor 4,
FT mitochondrial"
FT /id="PRO_0000431384"
FT REGION 65..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 118 AA; 13323 MW; DBEB82C99173C965 CRC64;
MQSVTRQTAR VLPQMGKQVS YLSTSGAWRA TASGGDMVVE IKEPKTRTEK LMAFQKKLRA
KTPLGKLDEF SRHPYQEKEP LKPWPNQTNP YTGEIGGPAG PEPTRYGDWE RKGRVSDF
