GLYL2_HUMAN
ID GLYL2_HUMAN Reviewed; 294 AA.
AC Q8WU03; A5LGC7; Q86WC3; Q96AT2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Glycine N-acyltransferase-like protein 2 {ECO:0000305};
DE EC=2.3.1.13 {ECO:0000269|PubMed:20305126, ECO:0000269|PubMed:22475485};
DE AltName: Full=Acyl-CoA:glycine N-acyltransferase-like protein 2;
GN Name=GLYATL2 {ECO:0000312|HGNC:HGNC:24178};
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], AND VARIANT LYS-160.
RA Nakayama Y., Weissman S.M., Bothwell A.L.;
RT "Isolation of a novel BXMAS2-10 gene from IgM cross-linking induced human B
RT cell.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-82 AND ILE-168.
RC TISSUE=Bone marrow;
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 [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND CATALYTIC ACTIVITY.
RX PubMed=20305126; DOI=10.1096/fj.09-148551;
RA Waluk D.P., Schultz N., Hunt M.C.;
RT "Identification of glycine N-acyltransferase-like 2 (GLYATL2) as a
RT transferase that produces N-acyl glycines in humans.";
RL FASEB J. 24:2795-2803(2010).
RN [6]
RP ACETYLATION AT LYS-19.
RX PubMed=22408254; DOI=10.1074/jbc.m112.347260;
RA Waluk D.P., Sucharski F., Sipos L., Silberring J., Hunt M.C.;
RT "Reversible lysine acetylation regulates activity of human glycine N-
RT acyltransferase-like 2 (hGLYATL2): implications for production of glycine-
RT conjugated signaling molecules.";
RL J. Biol. Chem. 287:16158-16167(2012).
CC -!- FUNCTION: Mitochondrial acyltransferase which transfers the acyl group
CC to the N-terminus of glycine (PubMed:22475485, PubMed:20305126).
CC Conjugates numerous substrates, such as arachidonoyl-CoA and saturated
CC medium and long-chain acyl-CoAs ranging from chain-length C8:0-CoA to
CC C18:0-CoA, to form a variety of N-acylglycines. Shows a preference for
CC monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor.
CC Does not exhibit any activity toward C22:6-CoA and chenodeoxycholoyl-
CC CoA, nor toward serine or alanine (PubMed:20305126).
CC {ECO:0000269|PubMed:20305126, ECO:0000269|PubMed:22475485}.
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:20305126, ECO:0000269|PubMed:22475485};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19870;
CC Evidence={ECO:0000305|PubMed:22475485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + glycine = CoA + H(+) + N-(9Z-
CC hexadecenoyl)-glycine; Xref=Rhea:RHEA:51372, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:61540,
CC ChEBI:CHEBI:134042; Evidence={ECO:0000269|PubMed:20305126};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51373;
CC Evidence={ECO:0000305|PubMed:20305126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + octadecanoyl-CoA = CoA + H(+) + N-
CC octadecanoylglycine; Xref=Rhea:RHEA:51368, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:134041; Evidence={ECO:0000269|PubMed:20305126};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51369;
CC Evidence={ECO:0000305|PubMed:20305126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + glycine = CoA + H(+) +
CC N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine; Xref=Rhea:RHEA:51364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:59002;
CC Evidence={ECO:0000269|PubMed:20305126};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51365;
CC Evidence={ECO:0000305|PubMed:20305126};
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:20305126};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51273;
CC Evidence={ECO:0000305|PubMed:20305126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + octanoyl-CoA = CoA + H(+) + N-octanoylglycine;
CC Xref=Rhea:RHEA:64240, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57386, ChEBI:CHEBI:142681;
CC Evidence={ECO:0000269|PubMed:20305126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + glycine = CoA + H(+) + N-decanoylglycine;
CC Xref=Rhea:RHEA:64248, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61430, ChEBI:CHEBI:142680;
CC Evidence={ECO:0000269|PubMed:20305126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + tetradecanoyl-CoA = CoA + H(+) + N-
CC tetradecanoylglycine; Xref=Rhea:RHEA:64252, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57305, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:86500; Evidence={ECO:0000269|PubMed:20305126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + glycine = CoA + H(+) + N-dodecanoylglycine;
CC Xref=Rhea:RHEA:64256, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57375, ChEBI:CHEBI:142678;
CC Evidence={ECO:0000269|PubMed:20305126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + glycine = CoA + H(+) + N-
CC (9Z,12Z-octadecadienoyl)-glycine; Xref=Rhea:RHEA:64260,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:150011;
CC Evidence={ECO:0000269|PubMed:20305126};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + glycine = an N-(fatty acyl)-glycine + CoA +
CC H(+); Xref=Rhea:RHEA:64244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:77636, ChEBI:CHEBI:149742;
CC Evidence={ECO:0000269|PubMed:20305126};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20305126};
CC Vmax=933 nmol/min/mg enzyme with (9Z)-octadecenoyl-CoA as substrate
CC {ECO:0000269|PubMed:20305126};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:20305126}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in salivary gland and
CC trachea. Also detected in thyroid gland, spinal cord, prostate, lung
CC and fetal brain. {ECO:0000269|PubMed:20305126}.
CC -!- PTM: Acetylation at Lys-19 drastically decreases the production of N-
CC oleoyl and N-arachidonoyl glycines. {ECO:0000269|PubMed:22408254}.
CC -!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF426250; AAO73139.1; -; mRNA.
DR EMBL; AB207211; BAF63415.1; -; mRNA.
DR EMBL; CH471076; EAW73826.1; -; Genomic_DNA.
DR EMBL; BC016789; AAH16789.1; -; mRNA.
DR EMBL; BC021682; AAH21682.1; -; mRNA.
DR CCDS; CCDS41649.1; -.
DR RefSeq; NP_659453.3; NM_145016.3.
DR RefSeq; XP_016872826.1; XM_017017337.1.
DR RefSeq; XP_016872827.1; XM_017017338.1.
DR AlphaFoldDB; Q8WU03; -.
DR SMR; Q8WU03; -.
DR STRING; 9606.ENSP00000287275; -.
DR DrugBank; DB00145; Glycine.
DR SwissLipids; SLP:000001661; -.
DR iPTMnet; Q8WU03; -.
DR PhosphoSitePlus; Q8WU03; -.
DR BioMuta; GLYATL2; -.
DR DMDM; 74730653; -.
DR MassIVE; Q8WU03; -.
DR PaxDb; Q8WU03; -.
DR PeptideAtlas; Q8WU03; -.
DR PRIDE; Q8WU03; -.
DR ProteomicsDB; 74617; -.
DR Antibodypedia; 27688; 73 antibodies from 20 providers.
DR DNASU; 219970; -.
DR Ensembl; ENST00000287275.6; ENSP00000287275.1; ENSG00000156689.7.
DR Ensembl; ENST00000532258.1; ENSP00000434277.1; ENSG00000156689.7.
DR GeneID; 219970; -.
DR KEGG; hsa:219970; -.
DR MANE-Select; ENST00000287275.6; ENSP00000287275.1; NM_145016.4; NP_659453.3.
DR UCSC; uc001nnd.6; human.
DR CTD; 219970; -.
DR GeneCards; GLYATL2; -.
DR HGNC; HGNC:24178; GLYATL2.
DR HPA; ENSG00000156689; Tissue enhanced (breast, cervix, salivary gland).
DR MIM; 614762; gene.
DR neXtProt; NX_Q8WU03; -.
DR OpenTargets; ENSG00000156689; -.
DR PharmGKB; PA142671728; -.
DR VEuPathDB; HostDB:ENSG00000156689; -.
DR eggNOG; ENOG502QVT5; Eukaryota.
DR GeneTree; ENSGT00950000183133; -.
DR HOGENOM; CLU_060336_0_0_1; -.
DR InParanoid; Q8WU03; -.
DR OMA; VLHEPQK; -.
DR OrthoDB; 1221333at2759; -.
DR PhylomeDB; Q8WU03; -.
DR TreeFam; TF353258; -.
DR BRENDA; 2.3.1.13; 2681.
DR PathwayCommons; Q8WU03; -.
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; Q8WU03; -.
DR BioGRID-ORCS; 219970; 7 hits in 1037 CRISPR screens.
DR ChiTaRS; GLYATL2; human.
DR GenomeRNAi; 219970; -.
DR Pharos; Q8WU03; Tbio.
DR PRO; PR:Q8WU03; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8WU03; protein.
DR Bgee; ENSG00000156689; Expressed in minor salivary gland and 97 other tissues.
DR ExpressionAtlas; Q8WU03; baseline and differential.
DR Genevisible; Q8WU03; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0042758; P:long-chain fatty acid catabolic process; IDA:UniProtKB.
DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IDA:UniProtKB.
DR GO; GO:1903965; P:monounsaturated fatty acid catabolic process; IDA:UniProtKB.
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; Endoplasmic reticulum; Lipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..294
FT /note="Glycine N-acyltransferase-like protein 2"
FT /id="PRO_0000281875"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22408254"
FT VARIANT 82
FT /note="P -> S (in dbSNP:rs17856514)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031296"
FT VARIANT 160
FT /note="E -> K (in dbSNP:rs11229651)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_031297"
FT VARIANT 168
FT /note="L -> I (in dbSNP:rs17851433)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031298"
FT CONFLICT 219
FT /note="Q -> R (in Ref. 1; AAO73139)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="Y -> C (in Ref. 1; AAO73139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 34277 MW; A1F5C3EC989D90D1 CRC64;
MLVLHNSQKL QILYKSLEKS IPESIKVYGA IFNIKDKNPF NMEVLVDAWP DYQIVITRPQ
KQEMKDDQDH YTNTYHIFTK APDKLEEVLS YSNVISWEQT LQIQGCQEGL DEAIRKVATS
KSVQVDYMKT ILFIPELPKK HKTSSNDKME LFEVDDDNKE GNFSNMFLDA SHAGLVNEHW
AFGKNERSLK YIERCLQDFL GFGVLGPEGQ LVSWIVMEQS CELRMGYTVP KYRHQGNMLQ
IGYHLEKYLS QKEIPFYFHV ADNNEKSLQA LNNLGFKICP CGWHQWKCTP KKYC
