ID GLYAT_HUMAN Reviewed; 296 AA. AC Q6IB77; H1AE11; O14833; Q96QK7; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 3. DT 02-SEP-2026, entry version 160. DE RecName: Full=Glycine N-acyltransferase {ECO:0000303|PubMed:10630424}; DE EC=2.3.1.13 {ECO:0000303|PubMed:22475485, ECO:0000303|PubMed:7802672}; 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:0000303|PubMed:22475485, ECO:0000303|PubMed:7802672}; DE AltName: Full=HRP-1(CLP); GN Name=GLYAT; Synonyms=ACGNAT, CAT, GAT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-156. RX PubMed=10630424; RX DOI=10.1002/(sici)1099-0461(2000)14:2<102::aid-jbt6>3.0.co;2-h; RA van der Westhuizen F.H., Pretorius P.J., Erasmus E.; RT "The utilization of alanine, glutamic acid, and serine as amino acid RT substrates for glycine N-acyltransferase."; RL J. Biochem. Mol. Toxicol. 14:102-109(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT SER-156. RX PubMed=22475485; DOI=10.1016/j.bbrc.2012.03.099; RA Matsuo M., Terai K., Kameda N., Matsumoto A., Kurokawa Y., Funase Y., RA Nishikawa K., Sugaya N., Hiruta N., Kishimoto T.; RT "Designation of enzyme activity of glycine-N-acyltransferase family genes RT and depression of glycine-N-acyltransferase in human hepatocellular RT carcinoma."; RL Biochem. Biophys. Res. Commun. 420:901-906(2012). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-156. RA Kishimoto T., Niwa S., Nishikawa K.; RT "Human HRP-1(CLP)."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS THR-17 AND RP SER-156. 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). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-163, AND VARIANT SER-156. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=7802672; DOI=10.1006/bbrc.1994.2817; RA Mawal Y.R., Qureshi I.A.; RT "Purification to homogeneity of mitochondrial acyl CoA:glycine N- RT acyltransferase from human liver."; RL Biochem. Biophys. Res. Commun. 205:1373-1379(1994). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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 numerous substrates to form a variety of N- CC acylglycines, with a preference for benzoyl-CoA over phenylacetyl-CoA CC as acyl donors. Thereby detoxify xenobiotics, such as benzoic acid or CC salicylic acid, and endogenous organic acids, such as isovaleric acid. CC {ECO:0000269|PubMed:22475485, ECO:0000269|PubMed:7802672}. 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:0000303|PubMed:22475485, ECO:0000303|PubMed:7802672}; CC -!- CATALYTIC ACTIVITY: CC Reaction=benzoyl-CoA + glycine = N-benzoylglycine + CoA + H(+); 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:0000303|PubMed:22475485, CC ECO:0000303|PubMed:7802672}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=57.9 mM for benzoyl-CoA {ECO:0000269|PubMed:7802672}; CC KM=83.7 mM for salicyl-CoA {ECO:0000269|PubMed:7802672}; CC KM=124 mM for isovaleryl-CoA {ECO:0000269|PubMed:7802672}; CC KM=198 mM for octanoyl-CoA {ECO:0000269|PubMed:7802672}; CC Vmax=17.1 umol/min/mg enzyme with benzoyl-CoA as substrate CC {ECO:0000269|PubMed:7802672}; CC Vmax=10.1 umol/min/mg enzyme with salicyl-CoA as substrate CC {ECO:0000269|PubMed:7802672}; CC Vmax=7.64 umol/min/mg enzyme with isovaleryl-CoA as substrate CC {ECO:0000269|PubMed:7802672}; CC Vmax=3.3 umol/min/mg enzyme with octanoyl-CoA as substrate CC {ECO:0000269|PubMed:7802672}; CC -!- INTERACTION: CC Q6IB77; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-715463, EBI-10171774; CC Q6IB77; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-715463, EBI-945833; CC Q6IB77-2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12142423, EBI-22310682; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22475485}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6IB77-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6IB77-2; Sequence=VSP_024073, VSP_024074; CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver (at protein level) CC and kidney. Down-regulated in hepatocellular carcinoma and other liver CC cancers. {ECO:0000269|PubMed:22475485}. CC -!- SIMILARITY: Belongs to the glycine N-acyltransferase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB81453.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAL43174.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AF023466; AAB81453.1; ALT_INIT; mRNA. DR EMBL; AB665285; BAL43174.1; ALT_INIT; mRNA. DR EMBL; AB013093; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AP000445; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009785; AAH09785.1; -; mRNA. DR EMBL; CR456927; CAG33208.1; -; mRNA. DR CCDS; CCDS7970.1; -. [Q6IB77-1] DR CCDS; CCDS7971.1; -. [Q6IB77-2] DR RefSeq; NP_005829.3; NM_005838.4. [Q6IB77-2] DR RefSeq; NP_964011.2; NM_201648.3. [Q6IB77-1] DR AlphaFoldDB; Q6IB77; -. DR SMR; Q6IB77; -. DR BioGRID; 115543; 10. DR FunCoup; Q6IB77; 30. DR IntAct; Q6IB77; 7. DR NDEx; IQUERY-CP-GLYAT; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000340200; -. DR DrugBank; DB00145; Glycine. DR GlyGen; Q6IB77; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6IB77; -. DR PhosphoSitePlus; Q6IB77; -. DR BioMuta; GLYAT; -. DR DMDM; 311033446; -. DR jPOST; Q6IB77; -. DR MassIVE; Q6IB77; -. DR PaxDb; 9606-ENSP00000340200; -. DR PeptideAtlas; Q6IB77; -. DR ProteomicsDB; 66367; -. [Q6IB77-1] DR ProteomicsDB; 66368; -. [Q6IB77-2] DR Antibodypedia; 27684; 192 antibodies from 26 providers. DR DNASU; 10249; -. DR Ensembl; ENST00000278400.3; ENSP00000278400.3; ENSG00000149124.11. [Q6IB77-2] DR Ensembl; ENST00000344743.8; ENSP00000340200.3; ENSG00000149124.11. [Q6IB77-1] DR Ensembl; ENST00000529732.5; ENSP00000431688.1; ENSG00000149124.11. [Q6IB77-1] DR Ensembl; ENST00000611865.4; ENSP00000484592.1; ENSG00000149124.11. [Q6IB77-1] DR GeneID; 10249; -. DR KEGG; hsa:10249; -. DR MANE-Select; ENST00000344743.8; ENSP00000340200.3; NM_201648.3; NP_964011.2. DR UCSC; uc001nnb.4; human. [Q6IB77-1] DR AGR; HGNC:13734; -. DR ClinPGx; PA28748; -. DR CTD; 10249; -. DR DisGeNET; 10249; -. DR GeneCards; GLYAT; -. DR HGNC; HGNC:13734; GLYAT. DR HPA; ENSG00000149124; Group enriched (kidney, liver). DR MIM; 607424; gene. DR OpenTargets; ENSG00000149124; -. DR VEuPathDB; HostDB:ENSG00000149124; -. DR eggNOG; ENOG502SDQB; Eukaryota. DR GeneTree; ENSGT00950000183133; -. DR HOGENOM; CLU_060336_0_0_1; -. DR InParanoid; Q6IB77; -. DR OMA; ERCIQNF; -. DR OrthoDB; 61870at2759; -. DR PAN-GO; Q6IB77; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q6IB77; -. DR BRENDA; 2.3.1.13; 2681. DR BRENDA; 2.3.1.71; 2681. DR PathwayCommons; Q6IB77; -. DR Reactome; R-HSA-159424; Conjugation of carboxylic acids. DR Reactome; R-HSA-177128; Conjugation of salicylate with glycine. DR Reactome; R-HSA-177135; Conjugation of benzoate with glycine. DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism. DR Reactome; R-HSA-9749641; Aspirin ADME. DR SABIO-RK; Q6IB77; -. DR SignaLink; Q6IB77; -. DR Agora; ENSG00000149124; -. DR BioGRID-ORCS; 10249; 7 hits in 1153 CRISPR screens. DR ChiTaRS; GLYAT; human. DR GeneWiki; GLYAT; -. DR GenomeRNAi; 10249; -. DR Pharos; Q6IB77; Tbio. DR PRO; PR:Q6IB77; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q6IB77; protein. DR Bgee; ENSG00000149124; Expressed in right lobe of liver and 104 other cell types or tissues. DR ExpressionAtlas; Q6IB77; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0016746; F:acyltransferase activity; TAS:ProtInc. DR GO; GO:0047961; F:glycine N-acyltransferase activity; IDA:UniProtKB. DR GO; GO:0047962; F:glycine N-benzoyltransferase activity; IDA:UniProtKB. DR GO; GO:0006637; P:acyl-CoA metabolic process; TAS:ProtInc. DR GO; GO:1901787; P:benzoyl-CoA metabolic process; IDA:UniProtKB. DR GO; GO:0006544; P:glycine metabolic process; IDA:UniProtKB. DR GO; GO:0032787; P:monocarboxylic acid metabolic process; ISS:UniProtKB. DR GO; GO:0009636; P:response to toxic substance; TAS:ProtInc. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR FunFam; 3.40.630.30:FF:000075; Glycine N-acyltransferase; 1. 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 1: Evidence at protein level; KW Acetylation; Acyltransferase; Alternative splicing; Detoxification; KW Mitochondrion; Proteomics identification; Reference proteome; Transferase. FT CHAIN 1..296 FT /note="Glycine N-acyltransferase" FT /id="PRO_0000281869" 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 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 141 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q91XE0" FT MOD_RES 141 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 VAR_SEQ 163 FT /note="I -> M (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10630424, FT ECO:0000303|PubMed:15489334" FT /id="VSP_024073" FT VAR_SEQ 164..296 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10630424, FT ECO:0000303|PubMed:15489334" FT /id="VSP_024074" FT VARIANT 17 FT /note="S -> T (in dbSNP:rs10896818)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_031294" FT VARIANT 156 FT /note="N -> S (in dbSNP:rs675815)" FT /evidence="ECO:0000269|PubMed:10630424, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3, FT ECO:0000269|Ref.6" FT /id="VAR_031295" SQ SEQUENCE 296 AA; 33924 MW; CB9D63FA48C23FE3 CRC64; MMLPLQGAQM LQMLEKSLRK SLPASLKVYG TVFHINHGNP FNLKAVVDKW PDFNTVVVCP QEQDMTDDLD HYTNTYQIYS KDPQNCQEFL GSPELINWKQ HLQIQSSQPS LNEAIQNLAA IKSFKVKQTQ RILYMAAETA KELTPFLLKS KILSPNGGKP KAINQEMFKL SSMDVTHAHL VNKFWHFGGN ERSQRFIERC IQTFPTCCLL GPEGTPVCWD LMDQTGEMRM AGTLPEYRLH GLVTYVIYSH AQKLGKLGFP VYSHVDYSNE AMQKMSYTLQ HVPIPRSWNQ WNCVPL //