CQ10B_MOUSE
ID CQ10B_MOUSE Reviewed; 240 AA.
AC Q3THF9; Q6P6N0; Q9D9R6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Coenzyme Q-binding protein COQ10 homolog B, mitochondrial;
DE Flags: Precursor;
GN Name=Coq10b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Heart, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Limb;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for the function of coenzyme Q in the respiratory
CC chain. May serve as a chaperone or may be involved in the transport of
CC Q6 from its site of synthesis to the catalytic sites of the respiratory
CC complexes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with coenzyme Q. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3THF9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3THF9-2; Sequence=VSP_017686;
CC -!- SIMILARITY: Belongs to the COQ10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH62129.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB24648.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE22900.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE40661.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK006551; BAB24648.1; ALT_INIT; mRNA.
DR EMBL; AK136258; BAE22900.1; ALT_INIT; mRNA.
DR EMBL; AK146260; BAE27020.1; -; mRNA.
DR EMBL; AK168293; BAE40237.1; -; mRNA.
DR EMBL; AK168837; BAE40661.1; ALT_INIT; mRNA.
DR EMBL; BC062129; AAH62129.1; ALT_INIT; mRNA.
DR RefSeq; NP_001034799.1; NM_001039710.1.
DR RefSeq; NP_080700.3; NM_026424.3.
DR AlphaFoldDB; Q3THF9; -.
DR SMR; Q3THF9; -.
DR STRING; 10090.ENSMUSP00000027125; -.
DR iPTMnet; Q3THF9; -.
DR PhosphoSitePlus; Q3THF9; -.
DR MaxQB; Q3THF9; -.
DR PaxDb; Q3THF9; -.
DR PRIDE; Q3THF9; -.
DR ProteomicsDB; 283819; -. [Q3THF9-1]
DR ProteomicsDB; 283820; -. [Q3THF9-2]
DR GeneID; 67876; -.
DR KEGG; mmu:67876; -.
DR UCSC; uc007azz.1; mouse. [Q3THF9-1]
DR CTD; 80219; -.
DR MGI; MGI:1915126; Coq10b.
DR eggNOG; KOG3177; Eukaryota.
DR InParanoid; Q3THF9; -.
DR OrthoDB; 1517528at2759; -.
DR PhylomeDB; Q3THF9; -.
DR TreeFam; TF314447; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR BioGRID-ORCS; 67876; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Coq10b; mouse.
DR PRO; PR:Q3THF9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3THF9; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0048039; F:ubiquinone binding; IBA:GO_Central.
DR GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR CDD; cd07813; COQ10p_like; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR044996; COQ10-like.
DR InterPro; IPR005031; COQ10_START.
DR InterPro; IPR023393; START-like_dom_sf.
DR PANTHER; PTHR12901; PTHR12901; 1.
DR Pfam; PF03364; Polyketide_cyc; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..240
FT /note="Coenzyme Q-binding protein COQ10 homolog B,
FT mitochondrial"
FT /id="PRO_0000228648"
FT VAR_SEQ 38..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017686"
FT CONFLICT 28
FT /note="T -> P (in Ref. 1; BAE40237/BAE27020/BAB24648)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 27269 MW; E31CF3DB36836A27 CRC64;
MAARTSQRAL ARVASGCHPK STTVTEATAR GSARDVRHLA ACGVLINRTL PPCAAVLPKE
ICARTFFRIS APLVNKRKEY SERRILGYSM QEMYDVVSGM EDYQHFVPWC KKSDIISRRS
GYCKTRLEVG FPPVLERYTS IVTLVKPHLV KASCTDGKLF NHLETIWRFS PGLPGYPRTC
TLDFSISFEF RSLLHSQLAT LFFDEVVKQM VAAFERRACK LYGPETNIPR ELMLHEIHHT
