GLYL3_MOUSE
ID GLYL3_MOUSE Reviewed; 290 AA.
AC E9Q5L8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Glycine-N-acyltransferase-like protein 3 {ECO:0000303|PubMed:27016726};
DE EC=2.3.1.13 {ECO:0000269|PubMed:27016726};
DE AltName: Full=Acyl-CoA:glycine-N-acyltransferase-like protein 3 {ECO:0000305|PubMed:27016726};
GN Name=Glyatl3 {ECO:0000303|PubMed:27016726, ECO:0000312|MGI:MGI:3647683};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RA McPherson J.D., Waterston R.H.;
RT "Genome Sequencing Center, 4444 Forest Park Parkway, St. Louis, MO 63108,
RT USA.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27016726; DOI=10.1194/jlr.m062042;
RA Jeffries K.A., Dempsey D.R., Farrell E.K., Anderson R.L., Garbade G.J.,
RA Gurina T.S., Gruhonjic I., Gunderson C.A., Merkler D.J.;
RT "Glycine N-acyltransferase-like 3 is responsible for long-chain N-
RT acylglycine formation in N18TG2 cells.";
RL J. Lipid Res. 57:781-790(2016).
CC -!- FUNCTION: Catalyzes the conjugation of long-chain fatty acyl-CoA
CC thioester and glycine to produce long-chain N-(fatty acyl)glycine, an
CC intermediate in the primary fatty acid amide biosynthetic pathway.
CC {ECO:0000269|PubMed:27016726}.
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:0000269|PubMed:27016726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + glycine = CoA + H(+) + N-(9Z-
CC octadecenoyl)glycine; Xref=Rhea:RHEA:51272, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:133992; Evidence={ECO:0000269|PubMed:27016726};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51273;
CC Evidence={ECO:0000269|PubMed:27016726};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + hexadecanoyl-CoA = CoA + H(+) + N-
CC hexadecanoylglycine; Xref=Rhea:RHEA:58536, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:142655; Evidence={ECO:0000269|PubMed:27016726};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58537;
CC Evidence={ECO:0000269|PubMed:27016726};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000269|PubMed:27016726}.
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DR EMBL; AC121932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50111.1; -.
DR RefSeq; NP_001138532.1; NM_001145060.1.
DR RefSeq; XP_006524650.1; XM_006524587.2.
DR AlphaFoldDB; E9Q5L8; -.
DR SMR; E9Q5L8; -.
DR STRING; 10090.ENSMUSP00000125916; -.
DR PhosphoSitePlus; E9Q5L8; -.
DR PaxDb; E9Q5L8; -.
DR PRIDE; E9Q5L8; -.
DR ProteomicsDB; 355057; -.
DR Antibodypedia; 30820; 51 antibodies from 11 providers.
DR Ensembl; ENSMUST00000166343; ENSMUSP00000125916; ENSMUSG00000091043.
DR GeneID; 435528; -.
DR KEGG; mmu:435528; -.
DR UCSC; uc012atm.1; mouse.
DR CTD; 389396; -.
DR MGI; MGI:3647683; Glyatl3.
DR VEuPathDB; HostDB:ENSMUSG00000091043; -.
DR eggNOG; ENOG502RFRQ; Eukaryota.
DR GeneTree; ENSGT00950000183133; -.
DR HOGENOM; CLU_060336_0_0_1; -.
DR InParanoid; E9Q5L8; -.
DR OMA; GTKFFKY; -.
DR OrthoDB; 1221333at2759; -.
DR PhylomeDB; E9Q5L8; -.
DR TreeFam; TF353258; -.
DR BRENDA; 2.3.1.13; 3474.
DR Reactome; R-MMU-177128; Conjugation of salicylate with glycine.
DR Reactome; R-MMU-177135; Conjugation of benzoate with glycine.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR BioGRID-ORCS; 435528; 3 hits in 72 CRISPR screens.
DR PRO; PR:E9Q5L8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; E9Q5L8; protein.
DR Bgee; ENSMUSG00000091043; Expressed in epiblast (generic) and 5 other tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:InterPro.
DR GO; GO:0047961; F:glycine N-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; 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 1: Evidence at protein level;
KW Acyltransferase; Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..290
FT /note="Glycine-N-acyltransferase-like protein 3"
FT /id="PRO_0000446855"
SQ SEQUENCE 290 AA; 32963 MW; 0139D0AA50B02DB1 CRC64;
MLVLKCSTKL FILENMLKSH FPESLKVYGA VMNINRGNPF QKEVVLDSWP NFKVIITRRE
REAETDNLDH YTNAYAVFYK DIRAYQQLLE EHDVINWDQV FQIQGLQSEL YAASKAVAKA
RLLDLDINLA SFKAVHFSPV SSVPDHSFLT GPTPRLTYLS VSDADLLNRT WSRGGNQQCL
RYLANLIACF PSVCVRDEKG NPVSWGITDQ FATMCHGYTL PDHRRKGYSR LVALTLARKL
QSRGFPSQGN VLDDNLASIN LLKSVQAEFL PCRFHRLILT PAAFSRQAHL
