SDF2A_DROAN
ID SDF2A_DROAN Reviewed; 156 AA.
AC B3MI37;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Succinate dehydrogenase assembly factor 2-A, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDH assembly factor 2-A {ECO:0000255|HAMAP-Rule:MF_03057};
DE Short=SDHAF2-A {ECO:0000255|HAMAP-Rule:MF_03057};
DE Flags: Precursor;
GN ORFNames=GF11110;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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}.
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DR EMBL; CH902619; EDV38047.1; -; Genomic_DNA.
DR RefSeq; XP_001961225.1; XM_001961189.2.
DR AlphaFoldDB; B3MI37; -.
DR SMR; B3MI37; -.
DR STRING; 7217.FBpp0114302; -.
DR EnsemblMetazoa; FBtr0115810; FBpp0114302; FBgn0088150.
DR GeneID; 6493975; -.
DR KEGG; dan:6493975; -.
DR eggNOG; KOG3326; Eukaryota.
DR HOGENOM; CLU_103054_0_3_1; -.
DR InParanoid; B3MI37; -.
DR OMA; HVKNHEK; -.
DR OrthoDB; 1492851at2759; -.
DR PhylomeDB; B3MI37; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
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:0018293; P:protein-FAD linkage; ISS:UniProtKB.
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 3: Inferred from homology;
KW Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03057"
FT CHAIN 25..156
FT /note="Succinate dehydrogenase assembly factor 2-A,
FT mitochondrial"
FT /id="PRO_0000383162"
FT REGION 35..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 156 AA; 18177 MW; 98DA70555AC2B5AA CRC64;
MLRQFLVSTA VRRVVVPSMA QTRCASNLDK SEYTTPGEIV DYDDPPHIPV PEYPSRPDEP
LETRKQRLLY QSRKRGMLEN DLLLSTFVAK YLKSFTADQT AQYDDLINGV SNDWDIFYWA
TETKPTPPEF DTEIMRLLKE HVKNAEKVQR IRQPDL
