SDF2A_DROYA
ID SDF2A_DROYA Reviewed; 162 AA.
AC B4P2P8;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
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};
GN ORFNames=GE23226;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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 -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {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; CM000157; EDW89309.1; -; Genomic_DNA.
DR RefSeq; XP_002089597.1; XM_002089561.2.
DR AlphaFoldDB; B4P2P8; -.
DR SMR; B4P2P8; -.
DR STRING; 7245.FBpp0268236; -.
DR EnsemblMetazoa; FBtr0269744; FBpp0268236; FBgn0240425.
DR GeneID; 6528553; -.
DR KEGG; dya:Dyak_GE23226; -.
DR eggNOG; KOG3326; Eukaryota.
DR HOGENOM; CLU_103054_0_3_1; -.
DR OMA; YGKPQNP; -.
DR OrthoDB; 1492851at2759; -.
DR PhylomeDB; B4P2P8; -.
DR Proteomes; UP000002282; Chromosome 2L.
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.
FT CHAIN 1..162
FT /note="Succinate dehydrogenase assembly factor 2-A,
FT mitochondrial"
FT /id="PRO_0000383182"
SQ SEQUENCE 162 AA; 19061 MW; 165F940D5644AF36 CRC64;
MLRQLRLTMD ILGWIFLPWR RSISNIKDSP PPPPLASTFD DVIVDYEDPD YLPLPEYPVR
PNEPLETRKQ RLLYQSRKRG MLENDLLLST FAAKHLQNFS AEQTAQYDQL INGVSNDWDI
YYWATDVKPT PKEYDTEIMR LLKKHVKNAE GVTRLRQPDL NT
