BAAT
entrez
570
canonical
uniprot
Q14032
canonical
ensembl
ENSG00000136881
resolver
ensembl
ENSG00000276559
resolver
ensp
ENSP00000259407
resolver
ensp
ENSP00000378491
resolver
ensp
ENSP00000484063
resolver
ensp
ENSP00000501610
resolver
ensp
ENSP00000574229
resolver
ensp
ENSP00000574230
resolver
ensp
ENSP00000574232
resolver
ensp
ENSP00000574233
resolver
ensp
ENSP00000574238
resolver
ensp
ENSP00000574239
resolver
ensp
ENSP00000574240
resolver
ensp
ENSP00000574241
resolver
enst
ENST00000259407
resolver
enst
ENST00000395051
resolver
enst
ENST00000621712
resolver
enst
ENST00000674556
resolver
enst
ENST00000904170
resolver
enst
ENST00000904171
resolver
enst
ENST00000904173
resolver
enst
ENST00000904174
resolver
enst
ENST00000904179
resolver
enst
ENST00000904180
resolver
enst
ENST00000904181
resolver
enst
ENST00000904182
resolver
genesymbol
BAAT
resolver
hgnc
HGNC:932
resolver
uniprot
Q3B7W9
resolver
uniprot
Q96L31
resolver
uniprot_entry
BAAT_HUMAN
resolver
uniprot_sec
Q3B7W9
resolver
uniprot_sec
Q96L31
resolver
amino_acid_sequence
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDLNHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVASAPKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASLLASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQIGLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFETTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGAGHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
uniprot
proteins
disease_involvement
DISEASE: Hypercholanemia, familial 3 (FHCA3) [MIM:619232]: An autosomal recessive metabolic disorder characterized by reduced biliary secretion of conjugated bile acids, fat malabsorption, and fat-soluble vitamin deficiency. Clinical manifestations include rickets with variable growth failure due to vitamin D deficiency, and coagulopathy due to deficiency of vitamin K-dependent clotting factors. Additional variable features include pruritis, anemia, hepatomegaly, and bile duct proliferation on liver biopsy. Laboratory studies show abnormally increased levels of unconjugated bile acids. {ECO:0000269|PubMed:12704386, ECO:0000269|PubMed:23415802}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.1.65
uniprot
proteins
ec_number
3.1.2.2
uniprot
proteins
ec_number
3.1.2.27
uniprot
proteins
function
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). {ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:2037576, ECO:0000269|PubMed:8034703, ECO:0000303|PubMed:12810727, ECO:0000303|PubMed:8034703}.
uniprot
proteins
mass_dalton
46299
uniprot
proteins
mutagenesis
MUTAGEN 235; /note="C->A: Abolishes N-acyltransferase activity."; /evidence="ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727"; MUTAGEN 235; /note="C->S: Lowers N-acyltransferase activity; enhanced thioesterase activity presumably dependent on the formation of a bile acid-enzyme covalent intermediate via a thioester bond."; /evidence="ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727"; MUTAGEN 328; /note="D->A: Abolishes N-acyltransferase activity."; /evidence="ECO:0000269|PubMed:12239217, ECO:0000269|PubMed:12810727"; MUTAGEN 362; /note="H->A: Abolishes N-acyltransferase activity."; /evidence="ECO:0000269|PubMed:12239217"; MUTAGEN 362; /note="H->Q: Abolishes N-acyltransferase activity."; /evidence="ECO:0000269|PubMed:12810727"; MUTAGEN 372; /note="C->A: Retains N-acyltransferase activity."; /evidence="ECO:0000269|PubMed:12810727"; MUTAGEN 417; /note="Q->K: Translocation to peroxisomes."; /evidence="ECO:0000269|PubMed:12810727
uniprot
proteins
protein_family
C/M/P thioester hydrolase family
uniprot
proteins
pubmed
12239217
uniprot
proteins
pubmed
12704386
uniprot
proteins
pubmed
12810727
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
2037576
uniprot
proteins
pubmed
23415802
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
8034703
uniprot
proteins
sequence_length
418
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12810727, ECO:0000269|PubMed:23415802, ECO:0000269|PubMed:8034703}. Peroxisome {ECO:0000250|UniProtKB:Q63276}.
uniprot
proteins