GATA_MOUSE
ID GATA_MOUSE Reviewed; 525 AA.
AC Q9CZN8; Q3TDF6; Q6NS53;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03150};
DE Short=Glu-AdT subunit A {ECO:0000255|HAMAP-Rule:MF_03150};
DE EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_03150};
DE AltName: Full=Glutaminyl-tRNA synthase-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03150};
GN Name=Qrsl1;
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 NOD; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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=Brain, and Heart;
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: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in the
CC mitochondria. The reaction takes place in the presence of glutamine and
CC ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03150};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03150}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03150}.
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DR EMBL; AK012351; BAB28181.1; -; mRNA.
DR EMBL; AK170225; BAE41646.1; -; mRNA.
DR EMBL; BC070459; AAH70459.1; -; mRNA.
DR CCDS; CCDS35894.1; -.
DR RefSeq; NP_001074523.1; NM_001081054.2.
DR AlphaFoldDB; Q9CZN8; -.
DR SMR; Q9CZN8; -.
DR BioGRID; 218178; 4.
DR STRING; 10090.ENSMUSP00000020012; -.
DR ChEMBL; CHEMBL3259494; -.
DR PhosphoSitePlus; Q9CZN8; -.
DR EPD; Q9CZN8; -.
DR MaxQB; Q9CZN8; -.
DR PaxDb; Q9CZN8; -.
DR PeptideAtlas; Q9CZN8; -.
DR PRIDE; Q9CZN8; -.
DR ProteomicsDB; 265728; -.
DR Antibodypedia; 32156; 157 antibodies from 23 providers.
DR Ensembl; ENSMUST00000020012; ENSMUSP00000020012; ENSMUSG00000019863.
DR GeneID; 76563; -.
DR KEGG; mmu:76563; -.
DR UCSC; uc007ezn.1; mouse.
DR CTD; 55278; -.
DR MGI; MGI:1923813; Qrsl1.
DR VEuPathDB; HostDB:ENSMUSG00000019863; -.
DR eggNOG; KOG1211; Eukaryota.
DR GeneTree; ENSGT00550000074866; -.
DR HOGENOM; CLU_009600_7_6_1; -.
DR InParanoid; Q9CZN8; -.
DR OMA; EVSCPHF; -.
DR OrthoDB; 1195292at2759; -.
DR PhylomeDB; Q9CZN8; -.
DR TreeFam; TF313766; -.
DR BRENDA; 6.3.5.7; 3474.
DR BioGRID-ORCS; 76563; 30 hits in 74 CRISPR screens.
DR ChiTaRS; Qrsl1; mouse.
DR PRO; PR:Q9CZN8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CZN8; protein.
DR Bgee; ENSMUSG00000019863; Expressed in metanephric renal vesicle and 245 other tissues.
DR Genevisible; Q9CZN8; MM.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; ISO:MGI.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; ISO:MGI.
DR GO; GO:0032543; P:mitochondrial translation; IMP:MGI.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR Gene3D; 3.90.1300.10; -; 1.
DR HAMAP; MF_00120; GatA; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR004412; GatA.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR00132; gatA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..525
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A,
FT mitochondrial"
FT /id="PRO_0000316769"
FT ACT_SITE 76
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 168
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT ACT_SITE 192
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03150"
FT CONFLICT 367
FT /note="D -> G (in Ref. 1; BAE41646)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="A -> S (in Ref. 2; AAH70459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 56783 MW; AC75BB4D470F9AD2 CRC64;
MLGRTLREVS AALKQGQVTP TELCKNCLSL IKKTKYLNAY ITVSEEVALK QAEESEKRYK
QGQSLGDLDG IPVAVKDNFS TTGIETTCAS NMLKGYVPPY NATVVQKLLD QGALLMGKTN
LDEFAMGSGS TDGVFGPVRN PWTYSKQYRE RSRQDAGDDS HWLITGGSSG GSAAAVAAFT
CFAALGSDTG GSTRNPAAHC GIVGFKPSYG LVSRHGLIPL VNSMDVPGIL TRCVDDTAIV
LGTLAGHDPK DSTTVRNPAQ PASVPGGMDV SRLCIGIPKE YLVPELSSEV RSLWSQAADL
FESEGAKVIE VSLPHTCYSI VCYHVLCTSE VASNMARFDG LQYGHRSGVD VSTEAMYAAT
RQEGFNDVVR GRILSGNFFL LKENYENYFV KAQKVRRLIV KDFVDVFESG VDVLLTPTTL
TEAVPYLEFI KEDNRTRSAQ DDIFTQAVNM AGLPAVSVPV ALSNQGLPIG LQLIGRAFCD
QQLLTVAKWF EKQVQFPVIQ LQGLMDDGSL VLENGKLTSA SLTQR
