Glycine N-acyltransferase-like protein 2
Details
- Name
- Glycine N-acyltransferase-like protein 2
- Synonyms
- 2.3.1.13
- Acyl-CoA:glycine N-acyltransferase-like protein 2
- Gene Name
- GLYATL2
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0016748|Glycine N-acyltransferase-like protein 2 MLVLHNSQKLQILYKSLEKSIPESIKVYGAIFNIKDKNPFNMEVLVDAWPDYQIVITRPQ KQEMKDDQDHYTNTYHIFTKAPDKLEEVLSYSNVISWEQTLQIQGCQEGLDEAIRKVATS KSVQVDYMKTILFIPELPKKHKTSSNDKMELFEVDDDNKEGNFSNMFLDASHAGLVNEHW AFGKNERSLKYIERCLQDFLGFGVLGPEGQLVSWIVMEQSCELRMGYTVPKYRHQGNMLQ IGYHLEKYLSQKEIPFYFHVADNNEKSLQALNNLGFKICPCGWHQWKCTPKKYC
- Number of residues
- 294
- Molecular Weight
- 34277.055
- Theoretical pI
- 6.67
- GO Classification
- Functionsglycine N-acyltransferase activityComponentsendoplasmic reticulum / mitochondrion
- General Function
- Glycine n-acyltransferase activity
- Specific Function
- Mitochondrial acyltransferase which transfers the acyl group to the N-terminus of glycine. Conjugates numerous substrates, such as arachidonoyl-CoA and saturated medium and long-chain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. Shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor. Does not exhibit any activity toward C22:6-CoA and chenodeoxycholoyl-CoA, nor toward serine or alanine.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Endoplasmic reticulum
- Gene sequence
>lcl|BSEQ0016749|Glycine N-acyltransferase-like protein 2 (GLYATL2) ATGCTTGTGCTTCATAACTCTCAGAAGCTGCAGATTCTGTATAAATCCTTAGAAAAGAGC ATCCCTGAATCCATAAAGGTATATGGCGCCATTTTCAACATAAAAGATAAAAACCCTTTC AACATGGAGGTGCTGGTAGATGCCTGGCCAGATTACCAGATCGTCATTACCCGGCCTCAG AAACAGGAGATGAAAGATGACCAGGATCATTATACCAACACTTACCACATCTTCACCAAA GCTCCTGACAAATTAGAGGAAGTCCTGTCATACTCCAATGTAATCAGCTGGGAGCAAACT TTGCAGATCCAAGGTTGCCAAGAGGGCTTGGATGAAGCAATAAGAAAGGTTGCAACTTCA AAATCAGTGCAGGTAGATTACATGAAAACCATCCTCTTTATACCGGAATTACCAAAGAAA CACAAGACCTCAAGTAATGACAAGATGGAGTTATTTGAAGTGGATGATGATAACAAGGAA GGAAACTTTTCAAACATGTTCTTAGATGCTTCACATGCAGGTCTTGTGAATGAACACTGG GCCTTTGGGAAAAATGAGAGGAGCTTGAAATATATTGAACGCTGCCTCCAGGATTTTCTA GGATTTGGTGTGCTGGGTCCAGAGGGCCAGCTTGTCTCTTGGATTGTGATGGAACAGTCC TGTGAGTTGAGAATGGGTTATACTGTCCCCAAATACAGACACCAAGGCAACATGTTGCAA ATTGGTTATCATCTTGAAAAGTATCTTTCTCAGAAAGAAATCCCATTTTATTTCCATGTG GCAGATAATAATGAGAAAAGCCTACAGGCACTGAACAATTTGGGGTTTAAGATTTGTCCT TGTGGCTGGCATCAGTGGAAATGCACCCCCAAGAAATATTGTTGA
- Chromosome Location
- 11
- Locus
- 11q12.1
- External Identifiers
Resource Link UniProtKB ID Q8WU03 UniProtKB Entry Name GLYL2_HUMAN GenBank Protein ID 29243559 GenBank Gene ID AF426250 GenAtlas ID GLYATL2 HGNC ID HGNC:24178 - General References
- 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. 2012 Apr 20;420(4):901-6. doi: 10.1016/j.bbrc.2012.03.099. Epub 2012 Mar 27. [Article]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
- Waluk DP, Schultz N, Hunt MC: Identification of glycine N-acyltransferase-like 2 (GLYATL2) as a transferase that produces N-acyl glycines in humans. FASEB J. 2010 Aug;24(8):2795-803. doi: 10.1096/fj.09-148551. Epub 2010 Mar 19. [Article]
- Waluk DP, Sucharski F, Sipos L, Silberring J, Hunt MC: Reversible lysine acetylation regulates activity of human glycine N-acyltransferase-like 2 (hGLYATL2): implications for production of glycine-conjugated signaling molecules. J Biol Chem. 2012 May 11;287(20):16158-67. doi: 10.1074/jbc.M112.347260. Epub 2012 Mar 9. [Article]