ID   SDHF3_NEMVE             Reviewed;         115 AA.
AC   A7S1H9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Succinate dehydrogenase assembly factor 3, mitochondrial {ECO:0000250|UniProtKB:Q04401};
DE            Short=SDH assembly factor 3 {ECO:0000250|UniProtKB:Q04401};
DE            Short=SDHAF3 {ECO:0000250|UniProtKB:Q04401};
DE   Flags: Precursor;
GN   Name=acn9; ORFNames=v1g100698;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(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. Promotes maturation of the iron-sulfur
CC       protein subunit of the SDH catalytic dimer, protecting it from the
CC       deleterious effects of oxidants. May act together with SDHAF1.
CC       {ECO:0000250|UniProtKB:Q04401, ECO:0000250|UniProtKB:Q8SZ16}.
CC   -!- SUBUNIT: Interacts with the iron-sulfur protein subunit within the SDH
CC       catalytic dimer. {ECO:0000250|UniProtKB:Q04401}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q04401}.
CC   -!- SIMILARITY: Belongs to the complex I LYR family. SDHAF3 subfamily.
CC       {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; DS469564; EDO42461.1; -; Genomic_DNA.
DR   RefSeq; XP_001634524.1; XM_001634474.1.
DR   AlphaFoldDB; A7S1H9; -.
DR   SMR; A7S1H9; -.
DR   STRING; 45351.EDO42461; -.
DR   PRIDE; A7S1H9; -.
DR   EnsemblMetazoa; EDO42461; EDO42461; NEMVEDRAFT_v1g100698.
DR   GeneID; 5514341; -.
DR   KEGG; nve:5514341; -.
DR   eggNOG; KOG4100; Eukaryota.
DR   HOGENOM; CLU_102310_2_0_1; -.
DR   InParanoid; A7S1H9; -.
DR   OMA; LTEWQMY; -.
DR   OrthoDB; 1613308at2759; -.
DR   PhylomeDB; A7S1H9; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0034553; P:mitochondrial respiratory chain complex II assembly; IBA:GO_Central.
DR   GO; GO:0006105; P:succinate metabolic process; IBA:GO_Central.
DR   InterPro; IPR008381; SDHAF3/Sdh7.
DR   PANTHER; PTHR13137; PTHR13137; 1.
PE   3: Inferred from homology;
KW   Chaperone; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..115
FT                   /note="Succinate dehydrogenase assembly factor 3,
FT                   mitochondrial"
FT                   /id="PRO_0000328457"
SQ   SEQUENCE   115 AA;  13483 MW;  BC382224DD5B769A CRC64;
     MSLPRHTLAI QALYRRVLKL HRKLPLEIKA LGDQYAKDEF RRHKKASQEQ AVRFMQEWKI
     YADTIEQQVN SQQLNVLGKD LKDEHIESLT EEQLGQLYSL QEAALKPDSS EPRDI