GLYL3_HUMAN
ID GLYL3_HUMAN Reviewed; 288 AA.
AC Q5SZD4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glycine N-acyltransferase-like protein 3 {ECO:0000250|UniProtKB:E9Q5L8};
DE EC=2.3.1.13 {ECO:0000250|UniProtKB:E9Q5L8};
DE AltName: Full=Acyl-CoA:glycine-N-acyltransferase-like protein 3 {ECO:0000250|UniProtKB:E9Q5L8};
GN Name=GLYATL3 {ECO:0000312|HGNC:HGNC:21349}; Synonyms=C6orf140;
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 [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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:0000250|UniProtKB:E9Q5L8}.
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:E9Q5L8};
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:0000250|UniProtKB:E9Q5L8};
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:0000250|UniProtKB:E9Q5L8};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000250|UniProtKB:E9Q5L8}.
CC -!- SIMILARITY: Belongs to the glycine N-acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK126371; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL590244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47440.1; -.
DR RefSeq; NP_001010904.1; NM_001010904.1.
DR AlphaFoldDB; Q5SZD4; -.
DR SMR; Q5SZD4; -.
DR BioGRID; 133128; 1.
DR IntAct; Q5SZD4; 1.
DR STRING; 9606.ENSP00000360240; -.
DR iPTMnet; Q5SZD4; -.
DR PhosphoSitePlus; Q5SZD4; -.
DR BioMuta; GLYATL3; -.
DR DMDM; 269849680; -.
DR EPD; Q5SZD4; -.
DR MassIVE; Q5SZD4; -.
DR PaxDb; Q5SZD4; -.
DR PeptideAtlas; Q5SZD4; -.
DR PRIDE; Q5SZD4; -.
DR ProteomicsDB; 64055; -.
DR Antibodypedia; 30820; 51 antibodies from 11 providers.
DR DNASU; 389396; -.
DR Ensembl; ENST00000371197.9; ENSP00000360240.4; ENSG00000203972.10.
DR GeneID; 389396; -.
DR KEGG; hsa:389396; -.
DR MANE-Select; ENST00000371197.9; ENSP00000360240.4; NM_001010904.2; NP_001010904.1.
DR UCSC; uc003ozi.4; human.
DR CTD; 389396; -.
DR GeneCards; GLYATL3; -.
DR HGNC; HGNC:21349; GLYATL3.
DR HPA; ENSG00000203972; Tissue enhanced (liver).
DR MIM; 614763; gene.
DR neXtProt; NX_Q5SZD4; -.
DR OpenTargets; ENSG00000203972; -.
DR PharmGKB; PA165617919; -.
DR VEuPathDB; HostDB:ENSG00000203972; -.
DR eggNOG; ENOG502RFRQ; Eukaryota.
DR GeneTree; ENSGT00950000183133; -.
DR HOGENOM; CLU_060336_0_0_1; -.
DR InParanoid; Q5SZD4; -.
DR OMA; GTKFFKY; -.
DR OrthoDB; 1221333at2759; -.
DR PhylomeDB; Q5SZD4; -.
DR TreeFam; TF353258; -.
DR PathwayCommons; Q5SZD4; -.
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 SignaLink; Q5SZD4; -.
DR BioGRID-ORCS; 389396; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; GLYATL3; human.
DR GenomeRNAi; 389396; -.
DR Pharos; Q5SZD4; Tdark.
DR PRO; PR:Q5SZD4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5SZD4; protein.
DR Bgee; ENSG00000203972; Expressed in rectum and 6 other tissues.
DR ExpressionAtlas; Q5SZD4; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IEA:InterPro.
DR GO; GO:0047961; F:glycine N-acyltransferase activity; ISS: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 2: Evidence at transcript level;
KW Acyltransferase; Lipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..288
FT /note="Glycine N-acyltransferase-like protein 3"
FT /id="PRO_0000336055"
FT CONFLICT 104
FT /note="Q -> K (in Ref. 1; AK126371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 32704 MW; E83D9766EFB7F1B8 CRC64;
MLVLNCSTKL LILEKMLKSC FPESLKVYGA VMNINRGNPF QKEVVLDSWP DFKAVITRRQ
REAETDNLDH YTNAYAVFYK DVRAYRQLLE ECDVFNWDQV FQIQGLQSEL YDVSKAVANS
KQLNIKLTSF KAVHFSPVSS LPDTSFLKGP SPRLTYLSVA NADLLNRTWS RGGNEQCLRY
IANLISCFPS VCVRDEKGNP VSWSITDQFA TMCHGYTLPE HRRKGYSRLV ALTLARKLQS
RGFPSQGNVL DDNTASISLL KSLHAEFLPC RFHRLILTPA TFSGLPHL
