2.A.50.2.6 MBOAT4, GOAT, or OACT4 of 435 aas and 7 - 9 TMSs in a 4 - 6 + 3 TMS arrangement. It mediates the octanoylation of ghrelin at 'Ser-3',but can use a variety of fatty acids as substrates including octanoic acid,
decanoic acid and tetradecanoic acid (Gutierrez et al. 2008). Campaña et al. 2019 reported a structural model of a eukaryotic membrane-bound O-acyltransferase (MBOAT), ghrelin O-acyltransferase (GOAT), which modifies the metabolism-regulating hormone, ghrelin. The proposed structure revealed a strategy for transmembrane protein acylation with catalysis occurring in an internal channel connecting the endoplasmic reticulum (ER) lumen and the cytoplasm (Campaña et al. 2019).
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Accession Number: | Q96T53 |
Protein Name: | Ghrelin O-acyltransferase |
Length: | 435 |
Molecular Weight: | 49716.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 7 |
Location1 / Topology2 / Orientation3: |
Endoplasmic reticulum membrane1 / Multi-pass membrane protein2 |
Substrate |
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1: MEWLWLFFLH PISFYQGAAF PFALLFNYLC IMDSFSTRAR YLFLLTGGGA LAVAAMGSYA
61: VLVFTPAVCA VALLCSLAPQ QVHRWTFCFQ MSWQTLCHLG LHYTEYYLHE PPSVRFCITL
121: SSLMLLTQRV TSLSLDICEG KVKAASGGFR SRSSLSEHVC KALPYFSYLL FFPALLGGSL
181: CSFQRFQARV QGSSALHPRH SFWALSWRGL QILGLECLNV AVSRVVDAGA GLTDCQQFEC
241: IYVVWTTAGL FKLTYYSHWI LDDSLLHAAG FGPELGQSPG EEGYVPDADI WTLERTHRIS
301: VFSRKWNQST ARWLRRLVFQ HSRAWPLLQT FAFSAWWHGL HPGQVFGFVC WAVMVEADYL
361: IHSFANEFIR SWPMRLFYRT LTWAHTQLII AYIMLAVEVR SLSSLWLLCN SYNSVFPMVY
421: CILLLLLAKR KHKCN