SDF2A_DROER
ID SDF2A_DROER Reviewed; 162 AA.
AC B3N8S9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 55.
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=GG10665;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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; CH954177; EDV59556.1; -; Genomic_DNA.
DR RefSeq; XP_001970497.1; XM_001970461.2.
DR AlphaFoldDB; B3N8S9; -.
DR SMR; B3N8S9; -.
DR STRING; 7220.FBpp0129211; -.
DR EnsemblMetazoa; FBtr0130719; FBpp0129211; FBgn0102972.
DR GeneID; 6542472; -.
DR KEGG; der:6542472; -.
DR eggNOG; KOG3326; Eukaryota.
DR HOGENOM; CLU_103054_0_3_1; -.
DR OMA; YGKPQNP; -.
DR OrthoDB; 1492851at2759; -.
DR PhylomeDB; B3N8S9; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0055070; P:copper ion homeostasis; IEA:EnsemblMetazoa.
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; Transit peptide.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03057"
FT CHAIN 24..162
FT /note="Succinate dehydrogenase assembly factor 2-A,
FT mitochondrial"
FT /id="PRO_0000383164"
SQ SEQUENCE 162 AA; 19058 MW; 362C12347E38919F CRC64;
MLRQLRLTMD ISGWIFLPWR RSMSNMKESP PPPPLASTFD DVIVDYEDPD YLPLPEYPLR
PNEPLQTRKQ RLLYQSRKRG MLENDLLLST FAAKHLQSFS AEQTAQYDQL INGVSNDWDI
YYWATDVKPT PKEYDTEIMG LLKEHVKNAE RVSRLRQPDL NT
