GLYAT_HUMAN
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 03-AUG-2022, entry version 141.
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 = 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: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};
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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_005838.3. [Q6IB77-2]
DR RefSeq; NP_964011.2; NM_201648.2. [Q6IB77-1]
DR AlphaFoldDB; Q6IB77; -.
DR SMR; Q6IB77; -.
DR BioGRID; 115543; 6.
DR IntAct; Q6IB77; 7.
DR STRING; 9606.ENSP00000484592; -.
DR DrugBank; DB00145; Glycine.
DR iPTMnet; Q6IB77; -.
DR PhosphoSitePlus; Q6IB77; -.
DR BioMuta; GLYAT; -.
DR DMDM; 311033446; -.
DR EPD; Q6IB77; -.
DR MassIVE; Q6IB77; -.
DR PaxDb; Q6IB77; -.
DR PeptideAtlas; Q6IB77; -.
DR PRIDE; Q6IB77; -.
DR ProteomicsDB; 66367; -. [Q6IB77-1]
DR ProteomicsDB; 66368; -. [Q6IB77-2]
DR Antibodypedia; 27684; 195 antibodies from 25 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 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 neXtProt; NX_Q6IB77; -.
DR OpenTargets; ENSG00000149124; -.
DR PharmGKB; PA28748; -.
DR VEuPathDB; HostDB:ENSG00000149124; -.
DR eggNOG; ENOG502SDQB; Eukaryota.
DR GeneTree; ENSGT00950000183133; -.
DR HOGENOM; CLU_060336_0_0_1; -.
DR InParanoid; Q6IB77; -.
DR OMA; IDDFDHY; -.
DR OrthoDB; 1221333at2759; -.
DR PhylomeDB; Q6IB77; -.
DR TreeFam; TF353258; -.
DR BRENDA; 2.3.1.13; 2681.
DR BRENDA; 2.3.1.71; 2681.
DR PathwayCommons; Q6IB77; -.
DR Reactome; R-HSA-177128; Conjugation of salicylate with glycine.
DR Reactome; R-HSA-177135; Conjugation of benzoate with glycine.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SABIO-RK; Q6IB77; -.
DR SignaLink; Q6IB77; -.
DR BioGRID-ORCS; 10249; 7 hits in 1074 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 tissues.
DR ExpressionAtlas; Q6IB77; baseline and differential.
DR Genevisible; Q6IB77; HS.
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:0016410; F:N-acyltransferase activity; IBA:GO_Central.
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 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_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
