COQ4_DANRE
ID COQ4_DANRE Reviewed; 271 AA.
AC A9JR86; A2BFR6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03111};
DE AltName: Full=Coenzyme Q biosynthesis protein 4 homolog {ECO:0000255|HAMAP-Rule:MF_03111};
GN Name=coq4; ORFNames=si:dkey-170o10.3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Component of the coenzyme Q biosynthetic pathway. May play a
CC role in organizing a multi-subunit COQ enzyme complex required for
CC coenzyme Q biosynthesis. Required for steady-state levels of other COQ
CC polypeptides. {ECO:0000255|HAMAP-Rule:MF_03111}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03111}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC at least coq3, coq4, coq5, coq6, coq7 and coq9. {ECO:0000255|HAMAP-
CC Rule:MF_03111}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03111}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03111}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03111}.
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_03111}.
CC -!- SIMILARITY: Belongs to the COQ4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03111}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM15135.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BC155557; AAI55558.1; -; mRNA.
DR EMBL; BX294186; CAM15135.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001108192.1; NM_001114720.1.
DR AlphaFoldDB; A9JR86; -.
DR SMR; A9JR86; -.
DR STRING; 7955.ENSDARP00000118229; -.
DR PaxDb; A9JR86; -.
DR PeptideAtlas; A9JR86; -.
DR GeneID; 100137123; -.
DR KEGG; dre:100137123; -.
DR CTD; 51117; -.
DR ZFIN; ZDB-GENE-060526-218; coq4.
DR eggNOG; KOG3244; Eukaryota.
DR InParanoid; A9JR86; -.
DR PhylomeDB; A9JR86; -.
DR TreeFam; TF314625; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:A9JR86; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03111; Coq4; 1.
DR InterPro; IPR007715; Coq4.
DR InterPro; IPR027540; Coq4_euk.
DR PANTHER; PTHR12922; PTHR12922; 1.
DR Pfam; PF05019; Coq4; 1.
PE 2: Evidence at transcript level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Ubiquinone biosynthesis.
FT CHAIN 1..271
FT /note="Ubiquinone biosynthesis protein COQ4 homolog,
FT mitochondrial"
FT /id="PRO_0000388053"
FT CONFLICT 271
FT /note="S -> SYYF (in Ref. 2; CAM15135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 30429 MW; 474C0C1A56B5AB8B CRC64;
MRGLPGAFLG SFKTSYGYLS QRLYGVLTEE KYDGRLYPSH IPTSTVQKAI LAVGSGVAAL
KNPYRHDMVA VLGETTGHQT LIKLRDRMRN DPEGSTILLE RPRIRLSTLD LSNMSALPDG
TLGREYLRFL EENRVTPDTR AEVKFVDNEE LAYVMQRYRE VHDLLHTLLG MPTNMLGEVA
VKWFEAAQTG LPMCILGAAL GPLRLSVSRL QLLGQSLGLW ALRNGGRARC VLSIYYERRW
EQTLDELRHE LNIEEPPVSL IASIKNSSSK S