ID   COQ9A_XENLA             Reviewed;         317 AA.
AC   Q3B8B2; A3KMU0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Ubiquinone biosynthesis protein COQ9-A, mitochondrial;
DE   Flags: Precursor;
GN   Name=coq9-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lipid-binding protein involved in the biosynthesis of
CC       coenzyme Q, also named ubiquinone, an essential lipid-soluble electron
CC       transporter for aerobic cellular respiration. Binds a phospholipid of
CC       at least 10 carbons in each acyl group. {ECO:0000250|UniProtKB:O75208}.
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000250|UniProtKB:Q8K1Z0}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O75208}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q8K1Z0}.
CC   -!- DOMAIN: Structurally similar to the bacterial FadR protein (fatty acid
CC       metabolism regulator protein). {ECO:0000250|UniProtKB:O75208}.
CC   -!- SIMILARITY: Belongs to the COQ9 family. {ECO:0000305}.
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DR   EMBL; BC106647; AAI06648.1; -; mRNA.
DR   EMBL; BC133229; AAI33230.1; -; mRNA.
DR   RefSeq; NP_001089120.1; NM_001095651.1.
DR   AlphaFoldDB; Q3B8B2; -.
DR   SMR; Q3B8B2; -.
DR   GeneID; 733404; -.
DR   KEGG; xla:733404; -.
DR   CTD; 733404; -.
DR   Xenbase; XB-GENE-948685; coq9.L.
DR   OrthoDB; 1304924at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 733404; Expressed in heart and 20 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR013718; COQ9.
DR   InterPro; IPR012762; Ubiq_biosynth_COQ9.
DR   PANTHER; PTHR21427; PTHR21427; 1.
DR   Pfam; PF08511; COQ9; 1.
DR   TIGRFAMs; TIGR02396; diverge_rpsU; 1.
PE   2: Evidence at transcript level;
KW   Lipid-binding; Mitochondrion; Reference proteome; Transit peptide;
KW   Ubiquinone biosynthesis.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..317
FT                   /note="Ubiquinone biosynthesis protein COQ9-A,
FT                   mitochondrial"
FT                   /id="PRO_0000228640"
FT   REGION          50..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         240..243
FT                   /ligand="1,2-diacylglycero-3-phosphoethanolamine"
FT                   /ligand_id="ChEBI:CHEBI:57613"
FT                   /evidence="ECO:0000250|UniProtKB:O75208"
SQ   SEQUENCE   317 AA;  35387 MW;  8141C0998509AA4D CRC64;
     MAASVTRVLK GAGGRQLLLM VARRRPVLMQ PFLLMPRKFW VSSALRSEDQ RQPPFSASST
     HAETQGHAEE QYQQKQPPPR YTDQAGEESE GYESEEQLQQ QILSAALQFV PDFGWSADAI
     AEGAKSLDMS AAAAGMFEDG GSELILHFVT QCNLQLTELL EKEQKLVQLG TSEKKPTAQF
     LRDAVEARLR MHIPYIEHWP QALGMLLLPR NIPSSLKLLT AMVDDIWHYA GDQSTDVSWY
     TRRAVLTGIY NTTELVMLQD SSPDFEDTWK FLENRISEAM TMGDSVKQVA STGEAVIQGL
     MGAAVTLKNL TGLNQRR