GLYAT_RAT
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 03-AUG-2022, entry version 112.
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};
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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.ENSRNOP00000016454; -.
DR iPTMnet; Q5PQT3; -.
DR PhosphoSitePlus; Q5PQT3; -.
DR PaxDb; Q5PQT3; -.
DR PRIDE; Q5PQT3; -.
DR Ensembl; ENSRNOT00000016454; ENSRNOP00000016454; ENSRNOG00000012142.
DR GeneID; 293779; -.
DR KEGG; rno:293779; -.
DR UCSC; RGD:1307163; rat.
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; 1221333at2759; -.
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 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:0016410; F:N-acyltransferase activity; IBA:GO_Central.
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 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 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
