Pter
entrez
19212
canonical
uniprot
Q60866
canonical
ensembl
ENSMUSG00000026730
resolver
ensp
ENSMUSP00000028063
resolver
ensp
ENSMUSP00000110444
resolver
ensp
ENSMUSP00000117009
resolver
genesymbol
Pter
resolver
uniprot
A2AUR4
resolver
uniprot
A2AUR6
resolver
uniprot
Q8BTA3
resolver
uniprot_entry
PTER_MOUSE
resolver
uniprot_sec
A2AUR4
resolver
uniprot_sec
A2AUR6
resolver
uniprot_sec
Q8BTA3
resolver
amino_acid_sequence
MSSLSGKVQTVLGLVEPSQLGRTLTHEHLTMTFDSFYCPPPPCHEVTSKEPIMMKNLFWIQKNPYSHRENLQLNQEVGAIREELLYFKAKGGGALVENTTTGLSRDVHTLKWLAEQTGVHIIAGAGFYVDATHSAATRAMSVEQLTDVLINEILHGADGTSIKCGVIGEIGCSWPLTDSERKILEATAHAQAQLGCPVIIHPGRNPGAPFQIIRILQEAGADISKTVMSHLDRTIFDKKELLEFAQLGCYLEYDLFGTELLNYQLSPDIDMPDDNKRIRRVHFLVDEGYEDRILMAHDIHTKHRLMKYGGHGYSHILTNIVPKMLLRGLTERVLDKILIENPKQWLTFK
uniprot
proteins
ec_number
3.1.-.-
uniprot
proteins
function
FUNCTION: N-acetyltaurine hydrolase that regulates feeding by catalyzing the hydrolysis of N-acetyltaurine into taurine and acetate (PubMed:39112712). N-acetyltaurine has anorexigenic and anti-obesity effects that are dependent on GFRAL receptor and GDF15 (PubMed:39112712). PTER also acts on other N-acetyl amino acids (Met, Ile, Leu, Val) and N-propionyltaurine, but at lower rates (PubMed:39112712). {ECO:0000269|PubMed:39112712}.
uniprot
proteins
mass_dalton
39218
uniprot
proteins
mutagenesis
MUTAGEN 26; /note="H->F: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 28; /note="H->F: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 65; /note="Y->F: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 169; /note="E->A: Decreased N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 201; /note="H->F: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 204; /note="R->A: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 230; /note="H->F: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 233; /note="R->A: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 255; /note="L->A: Increased N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 258; /note="T->G: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 260; /note="L->G: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 263; /note="Y->F: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 298; /note="D->A: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 300; /note="H->A: Abolished N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712"; MUTAGEN 304; /note="R->K: Slightly decreased N-acetyltaurine hydrolase activity."; /evidence="ECO:0000269|PubMed:39112712
uniprot
proteins
protein_family
Metallo-dependent hydrolases superfamily
uniprot
proteins
protein_family
Phosphotriesterase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
39112712
uniprot
proteins
pubmed
8654936
uniprot
proteins
sequence_length
349
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:39112712}.
uniprot
proteins