GLYAT_MOUSE
ID GLYAT_MOUSE Reviewed; 296 AA.
AC Q91XE0; Q05DG2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glycine N-acyltransferase;
DE EC=2.3.1.13 {ECO:0000250|UniProtKB:Q6IB77};
DE AltName: Full=Acyl-CoA:glycine N-acyltransferase;
DE Short=AAc;
DE AltName: Full=Aralkyl acyl-CoA N-acyltransferase;
DE AltName: Full=Aralkyl acyl-CoA:amino acid N-acyltransferase;
DE AltName: Full=Benzoyl-coenzyme A:glycine N-acyltransferase;
DE AltName: Full=Glycine N-benzoyltransferase;
DE EC=2.3.1.71 {ECO:0000250|UniProtKB:Q6IB77};
GN Name=Glyat;
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; TISSUE=Kidney, Spinal cord, and Spleen;
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] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Kidney;
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=Kidney, and Liver;
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 [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-16; LYS-127; LYS-141; LYS-142;
RP LYS-169; LYS-183; LYS-256 AND LYS-267, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16; LYS-113; LYS-127; LYS-141;
RP LYS-142; LYS-159; LYS-167; LYS-183 AND LYS-256, 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: Mitochondrial acyltransferase which transfers an acyl group
CC to the N-terminus of glycine and glutamine, although much less
CC efficiently. Can conjugate a multitude of substrates to form a variety
CC of N-acylglycines, thereby detoxify xenobiotics, such as benzoic acid
CC or salicylic acid, and endogenous organic acids, such as isovaleric
CC acid. {ECO:0000250|UniProtKB:Q6IB77}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + glycine = an N-acylglycine + CoA + H(+);
CC Xref=Rhea:RHEA:19869, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57670, ChEBI:CHEBI:58342; EC=2.3.1.13;
CC Evidence={ECO:0000250|UniProtKB:Q6IB77};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + glycine = CoA + H(+) + N-benzoylglycine;
CC Xref=Rhea:RHEA:18493, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57369, ChEBI:CHEBI:606565;
CC EC=2.3.1.71; Evidence={ECO:0000250|UniProtKB:Q6IB77};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q6IB77}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91XE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91XE0-2; Sequence=VSP_024075;
CC -!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK039262; BAC30297.1; -; mRNA.
DR EMBL; AK143901; BAE25590.1; -; mRNA.
DR EMBL; AK143803; BAE25544.1; -; mRNA.
DR EMBL; BC010799; AAH10799.1; -; mRNA.
DR EMBL; BC015294; AAH15294.1; -; mRNA.
DR EMBL; BC024434; AAH24434.1; -; mRNA.
DR CCDS; CCDS29633.1; -. [Q91XE0-1]
DR RefSeq; NP_666047.1; NM_145935.3. [Q91XE0-1]
DR AlphaFoldDB; Q91XE0; -.
DR SMR; Q91XE0; -.
DR IntAct; Q91XE0; 1.
DR MINT; Q91XE0; -.
DR STRING; 10090.ENSMUSP00000043308; -.
DR iPTMnet; Q91XE0; -.
DR PhosphoSitePlus; Q91XE0; -.
DR EPD; Q91XE0; -.
DR jPOST; Q91XE0; -.
DR MaxQB; Q91XE0; -.
DR PaxDb; Q91XE0; -.
DR PeptideAtlas; Q91XE0; -.
DR PRIDE; Q91XE0; -.
DR ProteomicsDB; 271237; -. [Q91XE0-1]
DR ProteomicsDB; 271238; -. [Q91XE0-2]
DR Antibodypedia; 27684; 195 antibodies from 25 providers.
DR DNASU; 107146; -.
DR Ensembl; ENSMUST00000044976; ENSMUSP00000043308; ENSMUSG00000063683. [Q91XE0-1]
DR Ensembl; ENSMUST00000119960; ENSMUSP00000114002; ENSMUSG00000063683. [Q91XE0-2]
DR GeneID; 107146; -.
DR KEGG; mmu:107146; -.
DR UCSC; uc008guh.1; mouse. [Q91XE0-1]
DR CTD; 10249; -.
DR MGI; MGI:2147502; Glyat.
DR VEuPathDB; HostDB:ENSMUSG00000063683; -.
DR eggNOG; ENOG502SDQB; Eukaryota.
DR GeneTree; ENSGT00950000183133; -.
DR HOGENOM; CLU_060336_0_0_1; -.
DR InParanoid; Q91XE0; -.
DR OMA; PISWLTM; -.
DR OrthoDB; 1221333at2759; -.
DR PhylomeDB; Q91XE0; -.
DR TreeFam; TF353258; -.
DR BRENDA; 2.3.1.13; 3474.
DR BRENDA; 2.3.1.71; 3474.
DR Reactome; R-MMU-177128; Conjugation of salicylate with glycine.
DR Reactome; R-MMU-177135; Conjugation of benzoate with glycine.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR BioGRID-ORCS; 107146; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Glyat; mouse.
DR PRO; PR:Q91XE0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91XE0; protein.
DR Bgee; ENSMUSG00000063683; Expressed in right kidney and 66 other tissues.
DR Genevisible; Q91XE0; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0047961; F:glycine N-acyltransferase activity; ISO:MGI.
DR GO; GO:0047962; F:glycine N-benzoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:1901787; P:benzoyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0006544; P:glycine metabolic process; ISS:UniProtKB.
DR GO; GO:0032787; P:monocarboxylic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR010313; Glycine_N-acyltransferase.
DR InterPro; IPR013652; Glycine_N-acyltransferase_C.
DR InterPro; IPR015938; Glycine_N-acyltransferase_N.
DR PANTHER; PTHR15298; PTHR15298; 1.
DR Pfam; PF08444; Gly_acyl_tr_C; 1.
DR Pfam; PF06021; Gly_acyl_tr_N; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Alternative splicing; Detoxification;
KW Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Glycine N-acyltransferase"
FT /id="PRO_0000281870"
FT MOD_RES 16
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 16
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 127
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 127
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 141
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 141
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 142
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 142
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 159
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 167
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 169
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 183
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 256
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 256
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 267
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024075"
SQ SEQUENCE 296 AA; 34098 MW; 2825F8C6F7BA2C96 CRC64;
MIVPLQGAQM LQMLEKSLRK YLPESLKVYG TVYHMIHGNP FNLKALVDKW PDFNTVVVRP
QEQEMTDDLD FYINTYQVYS KDPQNCQEFL ESSEVINWKQ HLQIQSSQSH LNKTIQNLAS
IQSFQIKHSE NILYVSSETI KKLFPSLLDT KNLSTGSGKP KAIDQDKFKL SSLDVVHAAL
VNKFWLFGGN ERSQRFIERC IKNFPSSCVL GPEGTPASWT LMDQTGEMRM GGTMPEYRLQ
GLVSFVVHSQ DQIMTKRGYP VYSHTEKSNI AMQKMSYTLQ HLPMPCAWNQ WKCMPM
