ID GLYAT_RAT Reviewed; 296 AA. AC Q5PQT3; Q7TP56; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 24-JAN-2024, entry version 118. 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}; DE AltName: Full=Liver regeneration-related protein LRRG067; GN Name=Glyat; ORFNames=Ab2-132; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RA Xu C.S., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J., RA Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M., Shi J.B., RA Rahman S., Wang Q.N., Zhang J.B.; RT "Liver regeneration after PH."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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). 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 -!- SIMILARITY: Belongs to the glycine N-acyltransferase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAP92593.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY325192; AAP92593.1; ALT_SEQ; mRNA. DR EMBL; BC087043; AAH87043.1; -; mRNA. DR RefSeq; NP_001009648.1; NM_001009648.2. DR RefSeq; XP_006231183.1; XM_006231121.3. DR RefSeq; XP_006231184.1; XM_006231122.3. DR RefSeq; XP_006231185.1; XM_006231123.3. DR RefSeq; XP_008758479.1; XM_008760257.1. DR RefSeq; XP_017444517.1; XM_017589028.1. DR AlphaFoldDB; Q5PQT3; -. DR SMR; Q5PQT3; -. DR STRING; 10116.ENSRNOP00000069894; -. DR iPTMnet; Q5PQT3; -. DR PhosphoSitePlus; Q5PQT3; -. DR PaxDb; 10116-ENSRNOP00000016454; -. DR Ensembl; ENSRNOT00000016454.6; ENSRNOP00000016454.3; ENSRNOG00000012142.7. DR Ensembl; ENSRNOT00055017488; ENSRNOP00055014085; ENSRNOG00055010338. DR Ensembl; ENSRNOT00060050773; ENSRNOP00060042232; ENSRNOG00060029234. DR Ensembl; ENSRNOT00065039053; ENSRNOP00065031709; ENSRNOG00065022841. DR GeneID; 293779; -. DR KEGG; rno:293779; -. DR UCSC; RGD:1307163; rat. DR AGR; RGD:1307163; -. DR CTD; 10249; -. DR RGD; 1307163; Glyat. DR eggNOG; ENOG502SDQB; Eukaryota. DR GeneTree; ENSGT00950000183133; -. DR HOGENOM; CLU_060336_0_0_1; -. DR InParanoid; Q5PQT3; -. DR OrthoDB; 3415109at2759; -. DR PhylomeDB; Q5PQT3; -. DR TreeFam; TF353258; -. DR Reactome; R-RNO-177128; Conjugation of salicylate with glycine. DR Reactome; R-RNO-177135; Conjugation of benzoate with glycine. DR Reactome; R-RNO-9749641; Aspirin ADME. DR PRO; PR:Q5PQT3; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000012142; Expressed in adult mammalian kidney and 12 other cell types or tissues. DR ExpressionAtlas; Q5PQT3; baseline and differential. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0047961; F:glycine N-acyltransferase activity; ISO:RGD. DR GO; GO:0047962; F:glycine N-benzoyltransferase activity; ISS:UniProtKB. DR GO; GO:1901787; P:benzoyl-CoA metabolic process; ISO:RGD. 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 Gene3D; 3.40.630.30; -; 1. 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:SF9; GLYCINE N-ACYLTRANSFERASE; 1. DR PANTHER; PTHR15298; L-COA N-ACYLTRANSFERASE-RELATED; 1. DR Pfam; PF08444; Gly_acyl_tr_C; 1. DR Pfam; PF06021; Gly_acyl_tr_N; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. PE 2: Evidence at transcript level; KW Acetylation; Acyltransferase; Detoxification; Mitochondrion; KW Reference proteome; Transferase. FT CHAIN 1..296 FT /note="Glycine N-acyltransferase" FT /id="PRO_0000281872" FT MOD_RES 16 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 16 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 113 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 127 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 127 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 142 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 142 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 159 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 169 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 183 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 183 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 256 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 256 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 267 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" SQ SEQUENCE 296 AA; 33899 MW; A559056779671ABB CRC64; MIVPLQGAQM LQMLEKSLKK YLPESLKVYG TIYHVNHGNP FNLKALVDKW PDFNTVVVRP QEQEMKDDLD FYTNTYQIYS KDPENCQEFL GSSEVINWKQ HLQIQSSQSH LNKAIQNLAS IHSLQVKHSE NILYVVSETV RKLFPSLLDT KNLSPGSGKP KAINQEMFKL SSLDVTHAAL VNKFWLFGGN ERSQRFIERC IKNFPSSCVL GPEGTPASWT LMDQTGEMRM GGTVPQYRAQ GLVSFVIYSQ DQIMKKRGFP VYSHTDKSNT VMQKMSYSLQ HLPMPCAWNQ WICVPM //