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TACO1_MOUSE
ID   TACO1_MOUSE             Reviewed;         294 AA.
AC   Q8K0Z7; B1AR86; Q3TI86; Q3USS8; Q9CV09;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Translational activator of cytochrome c oxidase 1;
DE   AltName: Full=Coiled-coil domain-containing protein 44;
DE   AltName: Full=Translational activator of mitochondrially-encoded cytochrome c oxidase 1;
GN   Name=Taco1; Synonyms=Ccdc44;
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].
RC   STRAIN=C57BL/6J, and DBA/2J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, and Tongue;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-162, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: Acts as a translational activator of mitochondrially-encoded
CC       cytochrome c oxidase 1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TACO1 family. {ECO:0000305}.
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DR   EMBL; AK010072; BAB26682.1; -; mRNA.
DR   EMBL; AK047078; BAC32953.1; -; mRNA.
DR   EMBL; AK140143; BAE24253.1; -; mRNA.
DR   EMBL; AK167963; BAE39960.1; -; mRNA.
DR   EMBL; AL596331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC029182; AAH29182.1; -; mRNA.
DR   CCDS; CCDS25547.1; -.
DR   RefSeq; NP_081622.1; NM_027346.1.
DR   PDB; 5EKZ; X-ray; 2.00 A; A=1-294.
DR   PDBsum; 5EKZ; -.
DR   AlphaFoldDB; Q8K0Z7; -.
DR   SMR; Q8K0Z7; -.
DR   BioGRID; 213915; 5.
DR   STRING; 10090.ENSMUSP00000002048; -.
DR   iPTMnet; Q8K0Z7; -.
DR   PhosphoSitePlus; Q8K0Z7; -.
DR   SwissPalm; Q8K0Z7; -.
DR   EPD; Q8K0Z7; -.
DR   jPOST; Q8K0Z7; -.
DR   MaxQB; Q8K0Z7; -.
DR   PaxDb; Q8K0Z7; -.
DR   PeptideAtlas; Q8K0Z7; -.
DR   PRIDE; Q8K0Z7; -.
DR   ProteomicsDB; 254643; -.
DR   Antibodypedia; 18674; 180 antibodies from 26 providers.
DR   DNASU; 70207; -.
DR   Ensembl; ENSMUST00000002048; ENSMUSP00000002048; ENSMUSG00000001983.
DR   GeneID; 70207; -.
DR   KEGG; mmu:70207; -.
DR   UCSC; uc007lyb.1; mouse.
DR   CTD; 51204; -.
DR   MGI; MGI:1917457; Taco1.
DR   VEuPathDB; HostDB:ENSMUSG00000001983; -.
DR   eggNOG; KOG2972; Eukaryota.
DR   GeneTree; ENSGT00390000012820; -.
DR   HOGENOM; CLU_062974_3_0_1; -.
DR   InParanoid; Q8K0Z7; -.
DR   OMA; ETIMYEG; -.
DR   OrthoDB; 1199273at2759; -.
DR   PhylomeDB; Q8K0Z7; -.
DR   TreeFam; TF300070; -.
DR   Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-MMU-611105; Respiratory electron transport.
DR   Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR   BioGRID-ORCS; 70207; 5 hits in 71 CRISPR screens.
DR   PRO; PR:Q8K0Z7; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8K0Z7; protein.
DR   Bgee; ENSMUSG00000001983; Expressed in quadriceps femoris and 96 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0097177; F:mitochondrial ribosome binding; IDA:MGI.
DR   GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR   GO; GO:0019843; F:rRNA binding; IDA:MGI.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:MGI.
DR   GO; GO:0061743; P:motor learning; IMP:MGI.
DR   GO; GO:1904959; P:regulation of cytochrome-c oxidase activity; IMP:MGI.
DR   GO; GO:0070129; P:regulation of mitochondrial translation; IMP:MGI.
DR   Gene3D; 1.10.10.200; -; 1.
DR   Gene3D; 3.30.70.980; -; 2.
DR   InterPro; IPR017856; Integrase-like_N.
DR   InterPro; IPR002876; Transcrip_reg_TACO1-like.
DR   InterPro; IPR026564; Transcrip_reg_TACO1-like_dom3.
DR   InterPro; IPR029072; YebC-like.
DR   PANTHER; PTHR12532; PTHR12532; 1.
DR   Pfam; PF01709; Transcrip_reg; 1.
DR   SUPFAM; SSF75625; SSF75625; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Coiled coil; Mitochondrion;
KW   Reference proteome; Translation regulation.
FT   CHAIN           1..294
FT                   /note="Translational activator of cytochrome c oxidase 1"
FT                   /id="PRO_0000175943"
FT   COILED          190..224
FT                   /evidence="ECO:0000255"
FT   MOD_RES         162
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   CONFLICT        86
FT                   /note="R -> G (in Ref. 1; BAE39960)"
FT                   /evidence="ECO:0000305"
FT   HELIX           75..92
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   HELIX           100..111
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   HELIX           116..123
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   STRAND          129..138
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   STRAND          144..152
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   HELIX           154..167
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   STRAND          180..191
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   HELIX           200..210
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   STRAND          213..219
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   STRAND          225..232
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   HELIX           236..245
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   STRAND          250..261
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   HELIX           267..282
FT                   /evidence="ECO:0007829|PDB:5EKZ"
FT   STRAND          286..291
FT                   /evidence="ECO:0007829|PDB:5EKZ"
SQ   SEQUENCE   294 AA;  32314 MW;  8285D9FE52E7AA1B CRC64;
     MMSWAAASLR MTAVPCFRVR CLGFRVGPWG ASQHANPGCG AAPHRTLHVS ATASAGHNKW
     SKVRHIKGPK DMERSRIFSK LTLSIRLAVK EGGPNPENNS SLANILELCR SKNMPKSTIE
     SALKTEKNKG IYLLYEGRGP GGSSLLIEAL SNSGPKCHLD IKYILNKNGG MMAEGARHFF
     DKKGVVVVGV EDREKKAVNL ERALELAIEA GAEDVKEAED EEEKNLFKFI CDASSLHQVR
     KKLDSLGLCP VSCSMEFIPH SKVQLAEPEL EQAAHLIQAL NNYEDVIHVY DNIE
 
 
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