Search Results

Overview

Uniprot IDQ14032
Protein NameBile acid-CoA:amino acid N-acyltransferase
Gene NameBAAT
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
123 NKVASAPKASLTLER
334 GDKTINSKAHAEQAI
345 EQAIGQLKRHGKNNW
408 EIQRFLRKHLIPDVT

Function

Catalyzes the amidation of bile acids (BAs) with the amino acids taurine and glycine (PubMed:12239217, PubMed:12810727, PubMed:2037576, PubMed:8034703). More than 95% of the BAs are N-acyl amidates with glycine and taurine (PubMed:8034703). Amidation of BAs in the liver with glycine or taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (PubMed:12810727). This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption (PubMed:12810727). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (PubMed:12239217, PubMed:12810727, PubMed:8034703). In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs (PubMed:12810727)

Protein Sequence

10 MIQLTATPVS 20 ALVDEPVHIR 30 ATGLIPFQMV 40 SFQASLEDEN 50 GDMFYSQAHY 60 RANEFGEVDL 70 NHASSLGGDY 80 MGVHPMGLFW 90 SLKPEKLLTR 100 LLKRDVMNRP 110 FQVQVKLYDL 120 ELIVNNKVAS 130 APKASLTLER 140 WYVAPGVTRI 150 KVREGRLRGA 160 LFLPPGEGLF 170 PGVIDLFGGL 180 GGLLEFRASL 190 LASRGFASLA 200 LAYHNYEDLP 210 RKPEVTDLEY 220 FEEAANFLLR 230 HPKVFGSGVG 240 VVSVCQGVQI 250 GLSMAIYLKQ 260 VTATVLINGT 270 NFPFGIPQVY 280 HGQIHQPLPH 290 SAQLISTNAL 300 GLLELYRTFE 310 TTQVGASQYL 320 FPIEEAQGQF 330 LFIVGEGDKT 340 INSKAHAEQA 350 IGQLKRHGKN 360 NWTLLSYPGA 370 GHLIEPPYSP 380 LCCASTTHDL 390 RLHWGGEVIP 400 HAAAQEHAWK 410 EIQRFLRKHL IPDVTSQL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005782 peroxisomal matrix
Cellular Component GO:0005777 peroxisome
Molecular Function GO:0016746 acyltransferase activity
Molecular Function GO:0052689 carboxylic ester hydrolase activity
Molecular Function GO:0033882 choloyl-CoA hydrolase activity
Molecular Function GO:0047617 fatty acyl-CoA hydrolase activity
Molecular Function GO:0047963 glycine N-choloyltransferase activity
Molecular Function GO:0052816 long-chain fatty acyl-CoA hydrolase activity
Molecular Function GO:0052815 medium-chain fatty acyl-CoA hydrolase activity
Molecular Function GO:0016410 N-acyltransferase activity
Molecular Function GO:0052817 very long-chain fatty acyl-CoA hydrolase activity
Biological Process GO:0006637 acyl-CoA metabolic process
Biological Process GO:0031100 animal organ regeneration
Biological Process GO:0006699 bile acid biosynthetic process
Biological Process GO:0002152 bile acid conjugation
Biological Process GO:0008206 bile acid metabolic process
Biological Process GO:0006631 fatty acid metabolic process
Biological Process GO:0006544 glycine metabolic process
Biological Process GO:0001889 liver development
Biological Process GO:0019530 taurine metabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.