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Glycine N-acyltransferase (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase) (AAc) (Aralkyl acyl-CoA N-acyltransferase) (Aralkyl acyl-CoA:amino acid N-acyltransferase) (Benzoyl-coenzyme A:glycine N-acyltransferase) (Glycine N-benzoyltransferase) (EC 2.3.1.71)

 GLYAT_MOUSE             Reviewed;         296 AA.
Q91XE0; Q05DG2;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
12-SEP-2018, entry version 125.
RecName: Full=Glycine N-acyltransferase;
EC=2.3.1.13 {ECO:0000250|UniProtKB:Q6IB77};
AltName: Full=Acyl-CoA:glycine N-acyltransferase;
Short=AAc;
AltName: Full=Aralkyl acyl-CoA N-acyltransferase;
AltName: Full=Aralkyl acyl-CoA:amino acid N-acyltransferase;
AltName: Full=Benzoyl-coenzyme A:glycine N-acyltransferase;
AltName: Full=Glycine N-benzoyltransferase;
EC=2.3.1.71 {ECO:0000250|UniProtKB:Q6IB77};
Name=Glyat;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney, Spinal cord, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-16; LYS-127; LYS-141;
LYS-142; LYS-169; LYS-183; LYS-256 AND LYS-267, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16; LYS-113; LYS-127;
LYS-141; LYS-142; LYS-159; LYS-167; LYS-183 AND LYS-256, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- FUNCTION: Mitochondrial acyltransferase which transfers an acyl
group to the N-terminus of glycine and glutamine, although much
less efficiently. Can conjugate a multitude of substrates to form
a variety of N-acylglycines, thereby detoxify xenobiotics, such as
benzoic acid or salicylic acid, and endogenous organic acids, such
as isovaleric acid. {ECO:0000250|UniProtKB:Q6IB77}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + glycine = CoA + N-acylglycine.
{ECO:0000250|UniProtKB:Q6IB77}.
-!- CATALYTIC ACTIVITY: Benzoyl-CoA + glycine = CoA + hippurate.
{ECO:0000250|UniProtKB:Q6IB77}.
-!- SUBCELLULAR LOCATION: Mitochondrion
{ECO:0000250|UniProtKB:Q6IB77}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q91XE0-1; Sequence=Displayed;
Name=2;
IsoId=Q91XE0-2; Sequence=VSP_024075;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK039262; BAC30297.1; -; mRNA.
EMBL; AK143901; BAE25590.1; -; mRNA.
EMBL; AK143803; BAE25544.1; -; mRNA.
EMBL; BC010799; AAH10799.1; -; mRNA.
EMBL; BC015294; AAH15294.1; -; mRNA.
EMBL; BC024434; AAH24434.1; -; mRNA.
CCDS; CCDS29633.1; -. [Q91XE0-1]
RefSeq; NP_666047.1; NM_145935.3. [Q91XE0-1]
UniGene; Mm.39974; -.
ProteinModelPortal; Q91XE0; -.
IntAct; Q91XE0; 2.
MINT; Q91XE0; -.
STRING; 10090.ENSMUSP00000043308; -.
iPTMnet; Q91XE0; -.
PhosphoSitePlus; Q91XE0; -.
PaxDb; Q91XE0; -.
PeptideAtlas; Q91XE0; -.
PRIDE; Q91XE0; -.
Ensembl; ENSMUST00000044976; ENSMUSP00000043308; ENSMUSG00000063683. [Q91XE0-1]
Ensembl; ENSMUST00000119960; ENSMUSP00000114002; ENSMUSG00000063683. [Q91XE0-2]
GeneID; 107146; -.
KEGG; mmu:107146; -.
UCSC; uc008guh.1; mouse. [Q91XE0-1]
CTD; 10249; -.
MGI; MGI:2147502; Glyat.
eggNOG; ENOG410IJUM; Eukaryota.
eggNOG; ENOG4111428; LUCA.
GeneTree; ENSGT00390000004997; -.
HOGENOM; HOG000263599; -.
HOVERGEN; HBG107953; -.
InParanoid; Q91XE0; -.
KO; K00628; -.
OMA; HVDKSNI; -.
OrthoDB; EOG091G0ESR; -.
PhylomeDB; Q91XE0; -.
TreeFam; TF353258; -.
Reactome; R-MMU-177128; Conjugation of salicylate with glycine.
Reactome; R-MMU-177135; Conjugation of benzoate with glycine.
ChiTaRS; Glyat; mouse.
PRO; PR:Q91XE0; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000063683; Expressed in 146 organ(s), highest expression level in proximal tubule.
CleanEx; MM_GLYAT; -.
Genevisible; Q91XE0; MM.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0047961; F:glycine N-acyltransferase activity; ISO:MGI.
GO; GO:0047962; F:glycine N-benzoyltransferase activity; ISS:UniProtKB.
GO; GO:1901787; P:benzoyl-CoA metabolic process; ISO:MGI.
GO; GO:0006544; P:glycine metabolic process; ISS:UniProtKB.
GO; GO:0032787; P:monocarboxylic acid metabolic process; ISS:UniProtKB.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR010313; Glycine_N-acyltransferase.
InterPro; IPR013652; Glycine_N-acyltransferase_C.
InterPro; IPR015938; Glycine_N-acyltransferase_N.
PANTHER; PTHR15298; PTHR15298; 1.
Pfam; PF08444; Gly_acyl_tr_C; 1.
Pfam; PF06021; Gly_acyl_tr_N; 1.
SUPFAM; SSF55729; SSF55729; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Alternative splicing; Complete proteome;
Detoxification; Mitochondrion; Reference proteome; Transferase.
CHAIN 1 296 Glycine N-acyltransferase.
/FTId=PRO_0000281870.
MOD_RES 16 16 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 16 16 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 113 113 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 127 127 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 127 127 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 141 141 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 141 141 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 142 142 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 142 142 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 159 159 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 167 167 N6-acetyllysine.
{ECO:0000244|PubMed:23576753}.
MOD_RES 169 169 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 183 183 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 183 183 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 256 256 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23576753}.
MOD_RES 256 256 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 267 267 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
VAR_SEQ 1 34 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024075.
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


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