MBOAT4
entrez
619373
canonical
uniprot
Q96T53
canonical
ensembl
ENSG00000177669
resolver
ensp
ENSP00000314196
resolver
genesymbol
MBOAT4
resolver
genesymbol_syn
GOAT
resolver
genesymbol_syn
OACT4
resolver
hgnc
HGNC:32311
resolver
uniprot
B1Q003
resolver
uniprot_entry
MBOA4_HUMAN
resolver
uniprot_sec
B1Q003
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by c8-acylated ghrelin mimetic peptide with an IC(50) of 22 nM (PubMed:25562443). Inhibited by 1-[2-cyano-3,12-dioxooleana-1,9(11)- dien-28-oyl] (CDDO) derivatives such as CDDO-imidazole (CDDO-Im), CDDO-methyl ester (CDDO-Me), CDDO-ethylamide (CDDO-EA), CDDO-trifluoroethylamide (CDDO-TFEA) with an IC(50) of 38 uM, 6uM, 8 uM and 44 uM respectively (PubMed:28134508). Inhibited by cyclohexenone derivatives such as 2-cyano-2-cyclohexanone and 2-bromo-2-cyclohexanone (PubMed:28134508). Inhibited by steroid derivatives such as alpha-cyanoenone steroid (PubMed:28134508). {ECO:0000269|PubMed:25562443, ECO:0000269|PubMed:28134508}.
uniprot
proteins
amino_acid_sequence
MEWLWLFFLHPISFYQGAAFPFALLFNYLCIMDSFSTRARYLFLLTGGGALAVAAMGSYAVLVFTPAVCAVALLCSLAPQQVHRWTFCFQMSWQTLCHLGLHYTEYYLHEPPSVRFCITLSSLMLLTQRVTSLSLDICEGKVKAASGGFRSRSSLSEHVCKALPYFSYLLFFPALLGGSLCSFQRFQARVQGSSALHPRHSFWALSWRGLQILGLECLNVAVSRVVDAGAGLTDCQQFECIYVVWTTAGLFKLTYYSHWILDDSLLHAAGFGPELGQSPGEEGYVPDADIWTLERTHRISVFSRKWNQSTARWLRRLVFQHSRAWPLLQTFAFSAWWHGLHPGQVFGFVCWAVMVEADYLIHSFANEFIRSWPMRLFYRTLTWAHTQLIIAYIMLAVEVRSLSSLWLLCNSYNSVFPMVYCILLLLLAKRKHKCN
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
function
FUNCTION: Catalyzes ghrelin acylation at 'Ser-3' using preferentially octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading to ghrelin activity (PubMed:18443287, PubMed:24045953, PubMed:25562443, PubMed:28134508). In vitro also uses acyl-CoA donors of different lengths from short-chain (C2) to long-chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16) that are not efficient (PubMed:18443287). {ECO:0000269|PubMed:18443287, ECO:0000269|PubMed:24045953, ECO:0000269|PubMed:25562443, ECO:0000269|PubMed:28134508}.
uniprot
proteins
mass_dalton
49716
uniprot
proteins
mutagenesis
MUTAGEN 338; /note="H->A: Abolishes ability to acylate ghrelin."; /evidence="ECO:0000269|PubMed:18443287
uniprot
proteins
post_translational_modification
PTM: Not glycosylated. {ECO:0000250|UniProtKB:P0C7A3}.
uniprot
proteins
protein_family
Membrane-bound acyltransferase family
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
18443287
uniprot
proteins
pubmed
24045953
uniprot
proteins
pubmed
25562443
uniprot
proteins
pubmed
28134508
uniprot
proteins
sequence_length
435
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P0C7A3}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P0C7A3}.
uniprot
proteins
transmembrane_region
TRANSMEM 6..26; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P0C7A3, ECO:0000255"; TRANSMEM 41..56; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P0C7A3, ECO:0000255"; TRANSMEM 60..76; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P0C7A3"; TRANSMEM 83..101; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P0C7A3"; TRANSMEM 121..136; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P0C7A3"; TRANSMEM 207..227; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P0C7A3"; TRANSMEM 241..261; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P0C7A3, ECO:0000255"; TRANSMEM 325..338; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P0C7A3"; TRANSMEM 341..357; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P0C7A3"; TRANSMEM 377..397; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 408..428; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins