MBOA4_HUMAN
ID MBOA4_HUMAN Reviewed; 435 AA.
AC Q96T53; B1Q003;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ghrelin O-acyltransferase {ECO:0000303|PubMed:18443287};
DE EC=2.3.1.- {ECO:0000269|PubMed:18443287, ECO:0000269|PubMed:24045953, ECO:0000269|PubMed:25562443, ECO:0000269|PubMed:28134508};
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 4;
DE Short=O-acyltransferase domain-containing protein 4;
GN Name=MBOAT4 {ECO:0000312|HGNC:HGNC:32311}; Synonyms=GOAT, OACT4;
GN ORFNames=FKSG89;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF HIS-338, VARIANT ALA-46, AND CATALYTIC ACTIVITY.
RC TISSUE=Thyroid carcinoma;
RX PubMed=18443287; DOI=10.1073/pnas.0800708105;
RA Gutierrez J.A., Solenberg P.J., Perkins D.R., Willency J.A., Knierman M.D.,
RA Jin Z., Witcher D.R., Luo S., Onyia J.E., Hale J.E.;
RT "Ghrelin octanoylation mediated by an orphan lipid transferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6320-6325(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Wang Y.-G., Gong L.;
RT "Identification of FKSG89, a novel gene located on human chromosome 8.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP TOPOLOGY, FUNCTION, CATALYTIC ACTIVITY, VARIANT ALA-46, AND
RP CHARACTERIZATION OF VARIANT ALA-46.
RX PubMed=24045953; DOI=10.1074/jbc.m113.510313;
RA Taylor M.S., Ruch T.R., Hsiao P.Y., Hwang Y., Zhang P., Dai L.,
RA Huang C.R.L., Berndsen C.E., Kim M.S., Pandey A., Wolberger C.,
RA Marmorstein R., Machamer C., Boeke J.D., Cole P.A.;
RT "Architectural organization of the metabolic regulatory enzyme ghrelin O-
RT acyltransferase.";
RL J. Biol. Chem. 288:32211-32228(2013).
RN [5]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=25562443; DOI=10.1021/bi5010359;
RA Darling J.E., Zhao F., Loftus R.J., Patton L.M., Gibbs R.A., Hougland J.L.;
RT "Structure-activity analysis of human ghrelin O-acyltransferase reveals
RT chemical determinants of ghrelin selectivity and acyl group recognition.";
RL Biochemistry 54:1100-1110(2015).
RN [6]
RP CATALYTIC ACTIVITY, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=28134508; DOI=10.1021/acs.biochem.6b01008;
RA McGovern-Gooch K.R., Mahajani N.S., Garagozzo A., Schramm A.J.,
RA Hannah L.G., Sieburg M.A., Chisholm J.D., Hougland J.L.;
RT "Synthetic Triterpenoid Inhibition of Human Ghrelin O-Acyltransferase: The
RT Involvement of a Functionally Required Cysteine Provides Mechanistic
RT Insight into Ghrelin Acylation.";
RL Biochemistry 56:919-931(2017).
CC -!- FUNCTION: Catalyzes ghrelin acylation at 'Ser-3' using preferentially
CC octanoyl-CoA, hexanoyl-CoA and decanoyl-CoA as acyl-CoA donors leading
CC to ghrelin activity (PubMed:24045953, PubMed:18443287, PubMed:25562443,
CC PubMed:28134508). In vitro uses also acyl-CoA donors of different
CC lengths from short-chain (C2) to long-chain fatty acids (C16) knowing
CC that acyl-CoA donors from butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are
CC more efficient compared to longer acyl-CoA donors, such as myristoyl-
CC CoA (C14) and palmitoyl-CoA (C16) that are not efficient
CC (PubMed:18443287). {ECO:0000269|PubMed:18443287,
CC ECO:0000269|PubMed:24045953, ECO:0000269|PubMed:25562443,
CC ECO:0000269|PubMed:28134508}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + octanoyl-CoA = CoA + O-octanoyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:59964, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:15484, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:143548; Evidence={ECO:0000269|PubMed:18443287,
CC ECO:0000269|PubMed:24045953, ECO:0000269|PubMed:25562443,
CC ECO:0000269|PubMed:28134508};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59965;
CC Evidence={ECO:0000269|PubMed:24045953, ECO:0000269|PubMed:25562443};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + L-seryl-[protein] = CoA + O-decanoyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:59972, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:15486, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:143549; Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59973;
CC Evidence={ECO:0000269|PubMed:18443287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-seryl-[protein] = CoA + O-acetyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:59392, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:15352, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:141128; Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393;
CC Evidence={ECO:0000305|PubMed:18443287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + L-seryl-[protein] = CoA + O-butanoyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:68276, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:17461, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:177287; Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68277;
CC Evidence={ECO:0000305|PubMed:18443287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + pentanoyl-CoA = CoA + O-pentanoyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:68280, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:17462, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389,
CC ChEBI:CHEBI:177288; Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68281;
CC Evidence={ECO:0000305|PubMed:18443287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexanoyl-CoA + L-seryl-[protein] = CoA + O-hexanoyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:68284, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:17463, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:177289; Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68285;
CC Evidence={ECO:0000269|PubMed:18443287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heptanoyl-CoA + L-seryl-[protein] = CoA + O-heptanoyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:68288, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:17464, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:78811,
CC ChEBI:CHEBI:177290; Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68289;
CC Evidence={ECO:0000305|PubMed:18443287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + nonanoyl-CoA = CoA + O-nonanoyl-L-seryl-
CC [protein]; Xref=Rhea:RHEA:68292, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:17465, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287, ChEBI:CHEBI:76291,
CC ChEBI:CHEBI:177291; Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68293;
CC Evidence={ECO:0000305|PubMed:18443287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + L-seryl-[protein] = CoA + O-dodecanoyl-L-
CC seryl-[protein]; Xref=Rhea:RHEA:68296, Rhea:RHEA-COMP:9863,
CC Rhea:RHEA-COMP:17466, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:177292;
CC Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68297;
CC Evidence={ECO:0000305|PubMed:18443287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + tetradecanoyl-CoA = CoA + O-tetradecanoyl-
CC L-seryl-[protein]; Xref=Rhea:RHEA:68300, Rhea:RHEA-COMP:9863,
CC Rhea:RHEA-COMP:17467, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:177293;
CC Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68301;
CC Evidence={ECO:0000305|PubMed:18443287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-CoA + L-seryl-[protein] = CoA + O-fatty acyl-L-
CC seryl-[protein]; Xref=Rhea:RHEA:68272, Rhea:RHEA-COMP:9863,
CC Rhea:RHEA-COMP:17460, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:77636, ChEBI:CHEBI:177286;
CC Evidence={ECO:0000269|PubMed:18443287};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68273;
CC Evidence={ECO:0000305|PubMed:18443287};
CC -!- ACTIVITY REGULATION: Inhibited by c8-acylated ghrelin mimetic peptide
CC with an IC(50) of 22 nM (PubMed:25562443). Inhibited by 1-[2-cyano-
CC 3,12-dioxooleana-1,9(11)- dien-28-oyl] (CDDO) derivatives such as CDDO-
CC imidazole (CDDO-Im), CDDO-methyl ester (CDDO-Me), CDDO-ethylamide
CC (CDDO-EA), CDDO-trifluoroethylamide (CDDO-TFEA) with an IC(50) of 38
CC uM, 6uM, 8 uM and 44 uM respectively (PubMed:28134508). Inhibited by
CC cyclohexenone derivatives such as 2-cyano-2-cyclohexanone and 2-bromo-
CC 2-cyclohexanone (PubMed:28134508). Inhibited by steroid derivatives
CC such as alpha-cyanoenone steroid (PubMed:28134508).
CC {ECO:0000269|PubMed:25562443, ECO:0000269|PubMed:28134508}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.5 uM for GSSFLC peptide {ECO:0000269|PubMed:25562443};
CC KM=1 uM for GFSFLC peptide {ECO:0000269|PubMed:25562443};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P0C7A3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P0C7A3}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0C7A3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96T53-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96T53-2; Sequence=VSP_032958, VSP_032959;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in stomach with moderate
CC levels in pancreas and relatively low levels in most other tissues.
CC {ECO:0000269|PubMed:18443287}.
CC -!- PTM: Not glycosylated. {ECO:0000250|UniProtKB:P0C7A3}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; EU518495; ACB05873.2; -; mRNA.
DR EMBL; AF359269; AAK43717.1; -; mRNA.
DR EMBL; AC026979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47835.1; -. [Q96T53-1]
DR RefSeq; NP_001094386.1; NM_001100916.1. [Q96T53-1]
DR RefSeq; XP_016869215.1; XM_017013726.1. [Q96T53-1]
DR AlphaFoldDB; Q96T53; -.
DR SMR; Q96T53; -.
DR STRING; 9606.ENSP00000314196; -.
DR BindingDB; Q96T53; -.
DR ChEMBL; CHEMBL3588729; -.
DR SwissLipids; SLP:000001956; -.
DR TCDB; 2.A.50.2.6; the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family.
DR PhosphoSitePlus; Q96T53; -.
DR BioMuta; MBOAT4; -.
DR DMDM; 182676418; -.
DR jPOST; Q96T53; -.
DR PaxDb; Q96T53; -.
DR PeptideAtlas; Q96T53; -.
DR PRIDE; Q96T53; -.
DR Antibodypedia; 54984; 213 antibodies from 23 providers.
DR DNASU; 619373; -.
DR Ensembl; ENST00000320542.4; ENSP00000314196.3; ENSG00000177669.4. [Q96T53-1]
DR GeneID; 619373; -.
DR KEGG; hsa:619373; -.
DR MANE-Select; ENST00000320542.4; ENSP00000314196.3; NM_001100916.2; NP_001094386.1.
DR UCSC; uc010lvg.4; human. [Q96T53-1]
DR CTD; 619373; -.
DR DisGeNET; 619373; -.
DR GeneCards; MBOAT4; -.
DR HGNC; HGNC:32311; MBOAT4.
DR HPA; ENSG00000177669; Group enriched (fallopian tube, gallbladder, pancreas, stomach).
DR MIM; 611940; gene.
DR neXtProt; NX_Q96T53; -.
DR OpenTargets; ENSG00000177669; -.
DR PharmGKB; PA142671233; -.
DR VEuPathDB; HostDB:ENSG00000177669; -.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_1_1; -.
DR InParanoid; Q96T53; -.
DR OMA; MDWLQLF; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q96T53; -.
DR TreeFam; TF314906; -.
DR PathwayCommons; Q96T53; -.
DR Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR BioGRID-ORCS; 619373; 14 hits in 1066 CRISPR screens.
DR ChiTaRS; MBOAT4; human.
DR GenomeRNAi; 619373; -.
DR Pharos; Q96T53; Tbio.
DR PRO; PR:Q96T53; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96T53; protein.
DR Bgee; ENSG00000177669; Expressed in islet of Langerhans and 64 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR GO; GO:0008374; F:O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0016412; F:serine O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0016486; P:peptide hormone processing; TAS:Reactome.
DR GO; GO:0018191; P:peptidyl-serine octanoylation; IDA:UniProtKB.
DR GO; GO:0051366; P:protein decanoylation; IEA:Ensembl.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Ghrelin O-acyltransferase"
FT /id="PRO_0000273024"
FT TOPO_DOM 1..5
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3, ECO:0000255"
FT TOPO_DOM 27..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 41..56
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3, ECO:0000255"
FT TOPO_DOM 57..59
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 60..76
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 77..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 102..120
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..136
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 137..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24045953"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 228..240
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3, ECO:0000255"
FT TOPO_DOM 262..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24045953"
FT TRANSMEM 325..338
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 339..340
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 341..357
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 358..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..407
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ACT_SITE 307
FT /evidence="ECO:0000250"
FT ACT_SITE 338
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_032958"
FT VAR_SEQ 107..114
FT /note="YLHEPPSV -> MFFKKLSC (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_032959"
FT VARIANT 46
FT /note="T -> A (does not affect octanoyltransferase
FT activity; dbSNP:rs7813902)"
FT /evidence="ECO:0000269|PubMed:18443287,
FT ECO:0000269|PubMed:24045953"
FT /id="VAR_059434"
FT VARIANT 231
FT /note="G -> E (in dbSNP:rs16876563)"
FT /id="VAR_030069"
FT MUTAGEN 338
FT /note="H->A: Abolishes ability to acylate ghrelin."
FT /evidence="ECO:0000269|PubMed:18443287"
SQ SEQUENCE 435 AA; 49716 MW; 0CF97AAE734F24A7 CRC64;
MEWLWLFFLH PISFYQGAAF PFALLFNYLC IMDSFSTRAR YLFLLTGGGA LAVAAMGSYA
VLVFTPAVCA VALLCSLAPQ QVHRWTFCFQ MSWQTLCHLG LHYTEYYLHE PPSVRFCITL
SSLMLLTQRV TSLSLDICEG KVKAASGGFR SRSSLSEHVC KALPYFSYLL FFPALLGGSL
CSFQRFQARV QGSSALHPRH SFWALSWRGL QILGLECLNV AVSRVVDAGA GLTDCQQFEC
IYVVWTTAGL FKLTYYSHWI LDDSLLHAAG FGPELGQSPG EEGYVPDADI WTLERTHRIS
VFSRKWNQST ARWLRRLVFQ HSRAWPLLQT FAFSAWWHGL HPGQVFGFVC WAVMVEADYL
IHSFANEFIR SWPMRLFYRT LTWAHTQLII AYIMLAVEVR SLSSLWLLCN SYNSVFPMVY
CILLLLLAKR KHKCN
