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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) (HRP-1(CLP))

 GLYAT_HUMAN             Reviewed;         296 AA.
Q6IB77; H1AE11; O14833; Q96QK7;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
25-OCT-2017, entry version 113.
RecName: Full=Glycine N-acyltransferase {ECO:0000303|PubMed:10630424};
EC=2.3.1.13 {ECO:0000303|PubMed:22475485, ECO:0000303|PubMed:7802672};
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:0000303|PubMed:22475485, ECO:0000303|PubMed:7802672};
AltName: Full=HRP-1(CLP);
Name=GLYAT; Synonyms=ACGNAT, CAT, GAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-156.
PubMed=10630424;
DOI=10.1002/(SICI)1099-0461(2000)14:2<102::AID-JBT6>3.0.CO;2-H;
van der Westhuizen F.H., Pretorius P.J., Erasmus E.;
"The utilization of alanine, glutamic acid, and serine as amino acid
substrates for glycine N-acyltransferase.";
J. Biochem. Mol. Toxicol. 14:102-109(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT SER-156.
PubMed=22475485; DOI=10.1016/j.bbrc.2012.03.099;
Matsuo M., Terai K., Kameda N., Matsumoto A., Kurokawa Y., Funase Y.,
Nishikawa K., Sugaya N., Hiruta N., Kishimoto T.;
"Designation of enzyme activity of glycine-N-acyltransferase family
genes and depression of glycine-N-acyltransferase in human
hepatocellular carcinoma.";
Biochem. Biophys. Res. Commun. 420:901-906(2012).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-156.
Kishimoto T., Niwa S., Nishikawa K.;
"Human HRP-1(CLP).";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
THR-17 AND SER-156.
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-163, AND VARIANT SER-156.
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7802672; DOI=10.1006/bbrc.1994.2817;
Mawal Y.R., Qureshi I.A.;
"Purification to homogeneity of mitochondrial acyl CoA:glycine N-
acyltransferase from human liver.";
Biochem. Biophys. Res. Commun. 205:1373-1379(1994).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Mitochondrial acyltransferase which transfers an acyl
group to the N-terminus of glycine and glutamine, although much
less efficiently. Can conjugate numerous substrates to form a
variety of N-acylglycines, with a preference for benzoyl-CoA over
phenylacetyl-CoA as acyl donors. Thereby detoxify xenobiotics,
such as benzoic acid or salicylic acid, and endogenous organic
acids, such as isovaleric acid. {ECO:0000269|PubMed:22475485,
ECO:0000269|PubMed:7802672}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + glycine = CoA + N-acylglycine.
{ECO:0000303|PubMed:22475485, ECO:0000303|PubMed:7802672}.
-!- CATALYTIC ACTIVITY: Benzoyl-CoA + glycine = CoA + hippurate.
{ECO:0000303|PubMed:22475485, ECO:0000303|PubMed:7802672}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=57.9 mM for benzoyl-CoA {ECO:0000269|PubMed:7802672};
KM=83.7 mM for salicyl-CoA {ECO:0000269|PubMed:7802672};
KM=124 mM for isovaleryl-CoA {ECO:0000269|PubMed:7802672};
KM=198 mM for octanoyl-CoA {ECO:0000269|PubMed:7802672};
Vmax=17.1 umol/min/mg enzyme with benzoyl-CoA as substrate
{ECO:0000269|PubMed:7802672};
Vmax=10.1 umol/min/mg enzyme with salicyl-CoA as substrate
{ECO:0000269|PubMed:7802672};
Vmax=7.64 umol/min/mg enzyme with isovaleryl-CoA as substrate
{ECO:0000269|PubMed:7802672};
Vmax=3.3 umol/min/mg enzyme with octanoyl-CoA as substrate
{ECO:0000269|PubMed:7802672};
-!- INTERACTION:
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-715463, EBI-10171774;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-715463, EBI-945833;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22475485}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6IB77-1; Sequence=Displayed;
Name=2;
IsoId=Q6IB77-2; Sequence=VSP_024073, VSP_024074;
-!- TISSUE SPECIFICITY: Predominantly expressed in liver (at protein
level) and kidney. Down-regulated in hepatocellular carcinoma and
other liver cancers. {ECO:0000269|PubMed:22475485}.
-!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB81453.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAL43174.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF023466; AAB81453.1; ALT_INIT; mRNA.
EMBL; AB665285; BAL43174.1; ALT_INIT; mRNA.
EMBL; AB013093; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AP000445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009785; AAH09785.1; -; mRNA.
EMBL; CR456927; CAG33208.1; -; mRNA.
CCDS; CCDS7970.1; -. [Q6IB77-1]
CCDS; CCDS7971.1; -. [Q6IB77-2]
RefSeq; NP_005829.3; NM_005838.3. [Q6IB77-2]
RefSeq; NP_964011.2; NM_201648.2. [Q6IB77-1]
UniGene; Hs.145384; -.
ProteinModelPortal; Q6IB77; -.
BioGrid; 115543; 5.
IntAct; Q6IB77; 6.
MINT; MINT-1412441; -.
STRING; 9606.ENSP00000340200; -.
DrugBank; DB00145; Glycine.
iPTMnet; Q6IB77; -.
PhosphoSitePlus; Q6IB77; -.
BioMuta; GLYAT; -.
DMDM; 311033446; -.
EPD; Q6IB77; -.
PaxDb; Q6IB77; -.
PeptideAtlas; Q6IB77; -.
PRIDE; Q6IB77; -.
DNASU; 10249; -.
Ensembl; ENST00000278400; ENSP00000278400; ENSG00000149124. [Q6IB77-2]
Ensembl; ENST00000344743; ENSP00000340200; ENSG00000149124. [Q6IB77-1]
Ensembl; ENST00000529732; ENSP00000431688; ENSG00000149124. [Q6IB77-1]
Ensembl; ENST00000611865; ENSP00000484592; ENSG00000149124. [Q6IB77-1]
GeneID; 10249; -.
KEGG; hsa:10249; -.
UCSC; uc001nnb.4; human. [Q6IB77-1]
CTD; 10249; -.
DisGeNET; 10249; -.
EuPathDB; HostDB:ENSG00000149124.10; -.
GeneCards; GLYAT; -.
HGNC; HGNC:13734; GLYAT.
HPA; HPA040251; -.
HPA; HPA044094; -.
MIM; 607424; gene.
neXtProt; NX_Q6IB77; -.
OpenTargets; ENSG00000149124; -.
PharmGKB; PA28748; -.
eggNOG; ENOG410IJUM; Eukaryota.
eggNOG; ENOG4111428; LUCA.
GeneTree; ENSGT00390000004997; -.
HOGENOM; HOG000263599; -.
HOVERGEN; HBG107953; -.
InParanoid; Q6IB77; -.
KO; K00628; -.
OMA; IPRSWNQ; -.
OrthoDB; EOG091G0ESR; -.
PhylomeDB; Q6IB77; -.
TreeFam; TF353258; -.
BRENDA; 2.3.1.13; 2681.
BRENDA; 2.3.1.71; 2681.
Reactome; R-HSA-177128; Conjugation of salicylate with glycine.
Reactome; R-HSA-177135; Conjugation of benzoate with glycine.
SABIO-RK; Q6IB77; -.
GeneWiki; GLYAT; -.
GenomeRNAi; 10249; -.
PRO; PR:Q6IB77; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149124; -.
CleanEx; HS_CAT; -.
CleanEx; HS_GLYAT; -.
ExpressionAtlas; Q6IB77; baseline and differential.
Genevisible; Q6IB77; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0047961; F:glycine N-acyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0047962; F:glycine N-benzoyltransferase activity; ISS:UniProtKB.
GO; GO:0016746; F:transferase activity, transferring acyl groups; TAS:ProtInc.
GO; GO:0006637; P:acyl-CoA metabolic process; TAS:ProtInc.
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; TAS:ProtInc.
GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
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; Polymorphism; Reference proteome;
Transferase.
CHAIN 1 296 Glycine N-acyltransferase.
/FTId=PRO_0000281869.
MOD_RES 16 16 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 16 16 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 127 127 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 127 127 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 141 141 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 141 141 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 159 159 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 169 169 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 183 183 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 183 183 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 256 256 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
MOD_RES 256 256 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91XE0}.
VAR_SEQ 163 163 I -> M (in isoform 2).
{ECO:0000303|PubMed:10630424,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_024073.
VAR_SEQ 164 296 Missing (in isoform 2).
{ECO:0000303|PubMed:10630424,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_024074.
VARIANT 17 17 S -> T (in dbSNP:rs10896818).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_031294.
VARIANT 156 156 N -> S (in dbSNP:rs675815).
{ECO:0000269|PubMed:10630424,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3, ECO:0000269|Ref.6}.
/FTId=VAR_031295.
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


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