MYG1_MOUSE
ID MYG1_MOUSE Reviewed; 380 AA.
AC Q9JK81; Q9CYX0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=MYG1 exonuclease {ECO:0000305};
DE EC=3.1.-.- {ECO:0000303|PubMed:31081026};
DE AltName: Full=Protein Gamm1;
DE Flags: Precursor;
GN Name=Myg1 {ECO:0000312|MGI:MGI:1929864};
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 [MRNA].
RC TISSUE=Brain;
RA Inazu T.;
RT "Gamm1: cloning and characterization.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Smicun Y., Chang E., Halaban R.;
RT "MYG1, a highly conserved novel gene from autonomously proliferating mouse
RT melanocytes.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=19014353; DOI=10.1042/bc20080086;
RA Philips M.-A., Vikesaa J., Luuk H., Joenson L., Lillevaeli K.,
RA Rehfeld J.F., Vasar E., Koks S., Nielsen F.C.;
RT "Characterization of MYG1 gene and protein: subcellular distribution and
RT function.";
RL Biol. Cell 101:361-373(2009).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=19818808; DOI=10.1016/j.bbr.2009.10.005;
RA Philips M.A., Abramov U., Lillevaeli K., Luuk H., Kurrikoff K., Raud S.,
RA Plaas M., Innos J., Puussaar T., Koks S., Vasar E.;
RT "Myg1-deficient mice display alterations in stress-induced responses and
RT reduction of sex-dependent behavioral differences.";
RL Behav. Brain Res. 207:182-195(2010).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31081026; DOI=10.1093/nar/gkz371;
RA Grover R., Burse S.A., Shankrit S., Aggarwal A., Kirty K., Narta K.,
RA Srivastav R., Ray A.K., Malik G., Vats A., Motiani R.K., Thukral L.,
RA Roy S.S., Bhattacharya S., Sharma R., Natarajan K., Mukerji M., Pandey R.,
RA Gokhale R.S., Natarajan V.T.;
RT "Myg1 exonuclease couples the nuclear and mitochondrial translational
RT programs through RNA processing.";
RL Nucleic Acids Res. 47:5852-5866(2019).
CC -!- FUNCTION: 3'-5' RNA exonuclease which cleaves in situ on specific
CC transcripts in both nucleus and mitochondrion. Involved in regulating
CC spatially segregated organellar RNA processing, acts as a coordinator
CC of nucleo-mitochondrial crosstalk (PubMed:31081026). In nucleolus,
CC processes pre-ribosomal RNA involved in ribosome assembly and alters
CC cytoplasmic translation. In mitochondrial matrix, processes 3'-termini
CC of the mito-ribosomal and messenger RNAs and controls translation of
CC mitochondrial proteins (PubMed:31081026).
CC {ECO:0000269|PubMed:31081026}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:19014353, ECO:0000269|PubMed:31081026}.
CC Mitochondrion matrix {ECO:0000269|PubMed:19014353,
CC ECO:0000269|PubMed:31081026}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:31081026}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC testis. {ECO:0000269|PubMed:19014353}.
CC -!- DEVELOPMENTAL STAGE: Strongly up-regulated from 7 dpc to 11 dpc. Widely
CC expressed at 8.5 dpc. At 11.75 dpc, expression is strongest in
CC developing neuroepithelium and eye. {ECO:0000269|PubMed:19014353}.
CC -!- DISRUPTION PHENOTYPE: Mutants are vital, fertile and display no gross
CC abnormalities. They show an inconsistent pattern of altered anxiety-
CC like behavior. Mutant males are significantly less anxious than their
CC wild-type littermates, females show increased anxiety in the locomotor
CC activity arena. {ECO:0000269|PubMed:19818808}.
CC -!- SIMILARITY: Belongs to the MYG1 family. {ECO:0000305}.
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DR EMBL; AF252871; AAF64518.1; -; mRNA.
DR EMBL; AF289484; AAG17846.1; -; mRNA.
DR EMBL; AK004104; BAB23171.1; -; mRNA.
DR EMBL; AK013232; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS27879.1; -.
DR RefSeq; NP_068359.1; NM_021713.2.
DR AlphaFoldDB; Q9JK81; -.
DR BioGRID; 208549; 5.
DR STRING; 10090.ENSMUSP00000109312; -.
DR iPTMnet; Q9JK81; -.
DR PhosphoSitePlus; Q9JK81; -.
DR EPD; Q9JK81; -.
DR jPOST; Q9JK81; -.
DR MaxQB; Q9JK81; -.
DR PaxDb; Q9JK81; -.
DR PeptideAtlas; Q9JK81; -.
DR PRIDE; Q9JK81; -.
DR ProteomicsDB; 293594; -.
DR Antibodypedia; 48361; 35 antibodies from 12 providers.
DR DNASU; 60315; -.
DR Ensembl; ENSMUST00000113682; ENSMUSP00000109312; ENSMUSG00000001285.
DR GeneID; 60315; -.
DR KEGG; mmu:60315; -.
DR UCSC; uc007xvi.1; mouse.
DR CTD; 60314; -.
DR MGI; MGI:1929864; Myg1.
DR VEuPathDB; HostDB:ENSMUSG00000001285; -.
DR eggNOG; KOG2948; Eukaryota.
DR GeneTree; ENSGT00390000010265; -.
DR InParanoid; Q9JK81; -.
DR OMA; FHCDEVV; -.
DR OrthoDB; 1174497at2759; -.
DR PhylomeDB; Q9JK81; -.
DR TreeFam; TF313313; -.
DR BioGRID-ORCS; 60315; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Myg1; mouse.
DR PRO; PR:Q9JK81; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9JK81; protein.
DR Bgee; ENSMUSG00000001285; Expressed in saccule of membranous labyrinth and 247 other tissues.
DR ExpressionAtlas; Q9JK81; baseline and differential.
DR Genevisible; Q9JK81; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0035641; P:locomotory exploration behavior; IMP:MGI.
DR InterPro; IPR003226; Met-dep_prot_hydro.
DR PANTHER; PTHR11215; PTHR11215; 1.
DR Pfam; PF03690; UPF0160; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Mitochondrion; Nuclease; Nucleus;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..380
FT /note="MYG1 exonuclease"
FT /id="PRO_0000213484"
FT MOD_RES 266
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB07"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 380 AA; 42723 MW; 9FD3E1908A2B51B2 CRC64;
MGRRFLRGIL TLPLRSVLQA QHRMLGSEQD PPAKRPRNNL MAPPRIGTHN GTFHCDEALA
CALLRLLPEY ANAEIVRTRD PEKLASCDIV VDVGGEYNPQ SHRYDHHQRT FTETMSSLCP
GKPWQTKLSS AGLVYLHFGR KLLAQLLGTS EEDSVVDTIY DKMYENFVEE VDAVDNGISQ
WAEGEPRYAM TTTLSARVAR LNPTWNQPNQ DTEAGFRRAM DLVQEEFLQR LNFYQHSWLP
ARALVEEALA QRFKVDSSGE IVELAKGGCP WKEHLYHLES ELSPKVAITF VIYTDQAGQW
RVQCVPKEPH SFQSRLPLPE PWRGLRDKAL DQVSGIPGCI FVHASGFIGG HHTREGALNM
ARATLAQRPA PVPLANAVVQ
