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COQ9_XENTR
ID   COQ9_XENTR              Reviewed;         317 AA.
AC   Q5RJV0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Ubiquinone biosynthesis protein COQ9, mitochondrial;
DE   Flags: Precursor;
GN   Name=coq9;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2004) 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; BC086494; AAH86494.1; -; mRNA.
DR   RefSeq; NP_001011181.1; NM_001011181.2.
DR   AlphaFoldDB; Q5RJV0; -.
DR   SMR; Q5RJV0; -.
DR   DNASU; 496601; -.
DR   Ensembl; ENSXETT00000062558; ENSXETP00000058937; ENSXETG00000025042.
DR   GeneID; 496601; -.
DR   KEGG; xtr:496601; -.
DR   CTD; 57017; -.
DR   Xenbase; XB-GENE-948680; coq9.
DR   HOGENOM; CLU_057411_0_2_1; -.
DR   InParanoid; Q5RJV0; -.
DR   OrthoDB; 1304924at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000025042; Expressed in skeletal muscle tissue and 14 other tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
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, mitochondrial"
FT                   /id="PRO_0000228642"
FT   REGION          45..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..82
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;  35305 MW;  D7F90244E105BC4E CRC64;
     MAASVARVLK AAGGRQLLLM VARRRPVLRQ PFLLMPRKFW GTSALRSEDQ KQPPFSSTSA
     HAGTPEHAEE QYQQQQPPPR YTDQAGEESE GYESEEQLQQ RILSAALQFV PDFGWSADAI
     AEGAKSLDMS AAAAGMFEDG GSELVLHFVT QCNSQLTELL EEEQKLVQLG TSEKKPTTQF
     LRDAVEARLR MHIPYIEQWP QALGMLLLPR NIPSSLKLLT AMVDDIWHYA GDQSTDVSWY
     TRRAVLTGIY NTTELVMLQD SSPDFEDTWK FLENRISEAM TMGTSVKQVA STGEAVIQGL
     MGAAVTLKNL TGLNQRR
 
 
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