SDF2B_DROME
ID SDF2B_DROME Reviewed; 156 AA.
AC A1Z897; Q8SYX8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Succinate dehydrogenase assembly factor 2-B, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDH assembly factor 2-B {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDHAF2-B {ECO:0000255|HAMAP-Rule:MF_03057};
DE Flags: Precursor;
GN ORFNames=CG12895;
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).
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. Required for flavinylation (covalent
CC attachment of FAD) of the flavoprotein subunit of the SDH catalytic
CC dimer. {ECO:0000255|HAMAP-Rule:MF_03057}.
CC -!- SUBUNIT: Interacts with the flavoprotein subunit within the SDH
CC catalytic dimer. {ECO:0000255|HAMAP-Rule:MF_03057}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03057}.
CC -!- SIMILARITY: Belongs to the SDHAF2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03057}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48877.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF58794.2; -; Genomic_DNA.
DR EMBL; AY071255; AAL48877.2; ALT_INIT; mRNA.
DR RefSeq; NP_001260868.1; NM_001273939.2.
DR RefSeq; NP_610586.3; NM_136742.5.
DR AlphaFoldDB; A1Z897; -.
DR SMR; A1Z897; -.
DR BioGRID; 61921; 1.
DR IntAct; A1Z897; 1.
DR STRING; 7227.FBpp0303465; -.
DR PaxDb; A1Z897; -.
DR DNASU; 36103; -.
DR EnsemblMetazoa; FBtr0088314; FBpp0087405; FBgn0033523.
DR EnsemblMetazoa; FBtr0330615; FBpp0303465; FBgn0033523.
DR GeneID; 36103; -.
DR KEGG; dme:Dmel_CG12895; -.
DR UCSC; CG12895-RA; d. melanogaster.
DR FlyBase; FBgn0033523; CG12895.
DR VEuPathDB; VectorBase:FBgn0033523; -.
DR eggNOG; KOG3326; Eukaryota.
DR GeneTree; ENSGT00390000001149; -.
DR HOGENOM; CLU_103054_0_3_1; -.
DR InParanoid; A1Z897; -.
DR OMA; HVKNHEK; -.
DR OrthoDB; 1492851at2759; -.
DR PhylomeDB; A1Z897; -.
DR BioGRID-ORCS; 36103; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36103; -.
DR PRO; PR:A1Z897; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033523; Expressed in mouthpart and 30 other tissues.
DR ExpressionAtlas; A1Z897; baseline and differential.
DR Genevisible; A1Z897; DM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0006121; P:mitochondrial electron transport, succinate to ubiquinone; ISS:UniProtKB.
DR GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR GO; GO:0018293; P:protein-FAD linkage; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 1.10.150.250; -; 1.
DR HAMAP; MF_03057; SDHAF2; 1.
DR InterPro; IPR005631; SDH.
DR InterPro; IPR036714; SDH_sf.
DR InterPro; IPR028882; SDHAF2.
DR Pfam; PF03937; Sdh5; 1.
DR SUPFAM; SSF109910; SSF109910; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 25..156
FT /note="Succinate dehydrogenase assembly factor 2-B,
FT mitochondrial"
FT /id="PRO_0000383168"
FT CONFLICT 50
FT /note="V -> F (in Ref. 3; AAL48877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 18380 MW; 631B7CF4B9EB8128 CRC64;
MLRQFIVSTV GRRLQLPMMA QSRLASNLDK TEYTTPGEIV DYDDPPHLPV PEYPVRPDEP
LETRKQRLLY QSRKRGMLEN DLLLSTFVAK HLKDFNAEQT AEYDQLINGV SNDWDIFYWA
TDTKPTPPQF DTEIMRLLKE HVKNHEKVQR IRQPDL
