MBOA4_MOUSE
ID MBOA4_MOUSE Reviewed; 435 AA.
AC P0C7A3; B1Q004; B2RWL6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Ghrelin O-acyltransferase {ECO:0000303|PubMed:18443287};
DE EC=2.3.1.- {ECO:0000269|PubMed:18443287, ECO:0000269|PubMed:18669668, ECO:0000269|PubMed:19501572, ECO:0000269|PubMed:24045953, ECO:0000269|PubMed:28134508, ECO:0000305|PubMed:18267071};
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 4;
DE Short=O-acyltransferase domain-containing protein 4;
DE Contains:
DE RecName: Full=44,4 kDa frgament {ECO:0000305|PubMed:24045953};
GN Name=Mboat4 {ECO:0000312|MGI:MGI:2685017}; Synonyms=Gm171, Goat;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MUTAGENESIS OF CYS-181; ASN-307 AND HIS-338, AND CATALYTIC
RP ACTIVITY.
RX PubMed=18267071; DOI=10.1016/j.cell.2008.01.017;
RA Yang J., Brown M.S., Liang G., Grishin N.V., Goldstein J.L.;
RT "Identification of the acyltransferase that octanoylates ghrelin, an
RT appetite-stimulating peptide hormone.";
RL Cell 132:387-396(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-338, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18669668; DOI=10.1073/pnas.0805353105;
RA Yang J., Zhao T.J., Goldstein J.L., Brown M.S.;
RT "Inhibition of ghrelin O-acyltransferase (GOAT) by octanoylated
RT pentapeptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10750-10755(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=19501572; DOI=10.1016/j.bbrc.2009.06.001;
RA Ohgusu H., Shirouzu K., Nakamura Y., Nakashima Y., Ida T., Sato T.,
RA Kojima M.;
RT "Ghrelin O-acyltransferase (GOAT) has a preference for n-hexanoyl-CoA over
RT n-octanoyl-CoA as an acyl donor.";
RL Biochem. Biophys. Res. Commun. 386:153-158(2009).
RN [7]
RP SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
RP OF ASN-27; MET-56; ILE-149; GLN-191; LYS-219; LYS-252; ILE-290; LEU-293;
RP ARG-298; ASN-307; SER-309; LYS-321; HIS-338; LYS-356; ASN-366; CYS-368;
RP LYS-431 AND LYS-433, SUBUNIT, AND PROTEOLYTIC CLEAVAGE.
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 [8]
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:18267071, PubMed:24045953, PubMed:28134508,
CC PubMed:18669668, PubMed:18443287, PubMed:19501572). In vitro uses also
CC acyl-CoA donors of different lengths from short-chain (C2) to long-
CC chain fatty acids (C16) knowing that acyl-CoA donors from butanoyl-CoA
CC (C4) to dodecanoyl-CoA (C12) are more efficient compared to longer
CC acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-CoA (C16)
CC that are not efficient (PubMed:19501572). {ECO:0000269|PubMed:18267071,
CC ECO:0000269|PubMed:18443287, ECO:0000269|PubMed:18669668,
CC ECO:0000269|PubMed:19501572, ECO:0000269|PubMed:24045953,
CC ECO:0000269|PubMed:28134508}.
CC -!- FUNCTION: [44,4 kDa frgament]: Inactive octanoyltransferase activity.
CC {ECO:0000269|PubMed:24045953}.
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:18669668, ECO:0000269|PubMed:19501572,
CC ECO:0000269|PubMed:24045953, ECO:0000269|PubMed:28134508,
CC ECO:0000305|PubMed:18267071};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59965;
CC Evidence={ECO:0000269|PubMed:18443287, ECO:0000269|PubMed:19501572,
CC ECO:0000269|PubMed:24045953};
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:19501572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68285;
CC Evidence={ECO:0000305|PubMed:19501572};
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:19501572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59973;
CC Evidence={ECO:0000305|PubMed:19501572};
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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59393;
CC Evidence={ECO:0000250|UniProtKB:Q96T53};
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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68277;
CC Evidence={ECO:0000250|UniProtKB:Q96T53};
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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68281;
CC Evidence={ECO:0000250|UniProtKB:Q96T53};
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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68289;
CC Evidence={ECO:0000250|UniProtKB:Q96T53};
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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68293;
CC Evidence={ECO:0000250|UniProtKB:Q96T53};
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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68297;
CC Evidence={ECO:0000250|UniProtKB:Q96T53};
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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68301;
CC Evidence={ECO:0000250|UniProtKB:Q96T53};
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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68273;
CC Evidence={ECO:0000250|UniProtKB:Q96T53};
CC -!- ACTIVITY REGULATION: Inhibited by 1-[2-cyano-3,12-dioxooleana-
CC 1,9(11)- dien-28-oyl]ethylamide (CDDO-EA) with an IC(50) of 60 uM
CC (PubMed:28134508). Inhibited by Fe3+ and Cu2+ and the O-acyltransferase
CC activity is completely blocked over 5 mM Fe3+ and 0.5 mM Cu2+
CC (PubMed:19501572). {ECO:0000269|PubMed:19501572,
CC ECO:0000269|PubMed:28134508}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=294 uM for n-hexanoyl-CoA {ECO:0000269|PubMed:19501572};
CC KM=13.6 uM for n-octanoyl-CoA {ECO:0000269|PubMed:19501572};
CC KM=0.6 uM for octanoyl CoA {ECO:0000269|PubMed:18669668};
CC KM=6 uM for proghrelin {ECO:0000269|PubMed:18669668};
CC pH dependence:
CC Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:19501572};
CC Temperature dependence:
CC Optimum temperature is 37-50 degrees Celsius.
CC {ECO:0000269|PubMed:19501572};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24045953}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18267071, ECO:0000269|PubMed:24045953}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:18267071}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stomach and pancreas
CC (PubMed:18267071). Lower expression in small intestine and colon
CC (PubMed:18267071). Very low expression in testis (PubMed:18267071).
CC {ECO:0000269|PubMed:18267071}.
CC -!- PTM: Not glycosylated. {ECO:0000269|PubMed:24045953}.
CC -!- DISRUPTION PHENOTYPE: Mice display a complete lack of octanoylated
CC ghrelin in blood. {ECO:0000269|PubMed:18443287}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI47845.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI47850.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EU721729; ACD93144.1; -; mRNA.
DR EMBL; EU518496; ACB05874.1; -; mRNA.
DR EMBL; AC167537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147844; AAI47845.1; ALT_INIT; mRNA.
DR EMBL; BC147849; AAI47850.1; ALT_INIT; mRNA.
DR CCDS; CCDS52540.1; -.
DR RefSeq; NP_001119786.1; NM_001126314.2.
DR AlphaFoldDB; P0C7A3; -.
DR SMR; P0C7A3; -.
DR STRING; 10090.ENSMUSP00000092988; -.
DR BindingDB; P0C7A3; -.
DR ChEMBL; CHEMBL1255134; -.
DR SwissLipids; SLP:000001957; -.
DR iPTMnet; P0C7A3; -.
DR PhosphoSitePlus; P0C7A3; -.
DR PaxDb; P0C7A3; -.
DR PRIDE; P0C7A3; -.
DR Antibodypedia; 54984; 213 antibodies from 23 providers.
DR Ensembl; ENSMUST00000095345; ENSMUSP00000092988; ENSMUSG00000071113.
DR GeneID; 234155; -.
DR KEGG; mmu:234155; -.
DR UCSC; uc012gch.1; mouse.
DR CTD; 619373; -.
DR MGI; MGI:2685017; Mboat4.
DR VEuPathDB; HostDB:ENSMUSG00000071113; -.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_1_1; -.
DR InParanoid; P0C7A3; -.
DR OMA; MDWLQLF; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; P0C7A3; -.
DR TreeFam; TF314906; -.
DR Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR BioGRID-ORCS; 234155; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Mboat4; mouse.
DR PRO; PR:P0C7A3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P0C7A3; protein.
DR Bgee; ENSMUSG00000071113; Expressed in morula and 65 other tissues.
DR Genevisible; P0C7A3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA: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:0016412; F:serine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0018191; P:peptidyl-serine octanoylation; IDA:UniProtKB.
DR GO; GO:0043543; P:protein acylation; IDA:UniProtKB.
DR GO; GO:0051366; P:protein decanoylation; IDA:UniProtKB.
DR GO; GO:0018190; P:protein octanoylation; IDA:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Ghrelin O-acyltransferase"
FT /id="PRO_0000329073"
FT CHAIN 56..435
FT /note="44,4 kDa frgament"
FT /evidence="ECO:0000269|PubMed:24045953"
FT /id="PRO_0000454294"
FT TOPO_DOM 1..5
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24045953"
FT TOPO_DOM 27..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 41..56
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24045953"
FT TOPO_DOM 57..59
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 60..76
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24045953"
FT TOPO_DOM 77..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24045953"
FT TOPO_DOM 102..120
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..136
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24045953"
FT TOPO_DOM 137..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:24045953"
FT TOPO_DOM 228..240
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:24045953"
FT TOPO_DOM 262..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..338
FT /note="Helical"
FT TOPO_DOM 339..340
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 341..357
FT /note="Helical"
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:0000305|PubMed:18267071"
FT ACT_SITE 338
FT /evidence="ECO:0000305|PubMed:18267071"
FT SITE 55..56
FT /note="Cleavage"
FT /evidence="ECO:0000305|PubMed:24045953"
FT MUTAGEN 27
FT /note="N->H: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 56
FT /note="M->A: Loss of 44,4 kDa fragment."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 56
FT /note="M->I: Loss of 44,4 kDa form."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 149
FT /note="I->N: Does not glycosylated."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 181
FT /note="C->A: No effect on ability to acylate ghrelin."
FT /evidence="ECO:0000269|PubMed:18267071"
FT MUTAGEN 191
FT /note="Q->N: Does not glycosylated."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 219
FT /note="K->R: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 252
FT /note="K->R: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 290
FT /note="I->N: Does not glycosylated."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 293
FT /note="L->N: Does not glycosylated."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 298
FT /note="R->N: Does not glycosylated."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 307
FT /note="N->A: Abolished ability to acylate ghrelin."
FT /evidence="ECO:0000269|PubMed:18267071"
FT MUTAGEN 307
FT /note="N->H: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 309
FT /note="S->A: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 321
FT /note="K->R: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 338
FT /note="H->A: Abolished ability to acylate ghrelin. Does not
FT affect proteic cleveage. loss of serine O-acyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:18267071,
FT ECO:0000269|PubMed:18669668, ECO:0000269|PubMed:24045953"
FT MUTAGEN 338
FT /note="H->N: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 356
FT /note="K->R: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 366
FT /note="N->H: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 368
FT /note="C->A: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 431
FT /note="K->R: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT MUTAGEN 433
FT /note="K->R: Does not affect protein cleveage."
FT /evidence="ECO:0000269|PubMed:24045953"
FT CONFLICT 31
FT /note="I -> V (in Ref. 4; AAI47845/AAI47850)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="F -> L (in Ref. 4; AAI47845/AAI47850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 49879 MW; C2B7E69E35185620 CRC64;
MDWLQLFFLH PLSFYQGAAF PFALLFNYLC ILDTFSTRAR YLFLLAGGGV LAFAAMGPYS
LLIFIPALCA VALVSFLSPQ EVHRLTFFFQ MGWQTLCHLG LHYTEYYLGE PPPVRFYITL
SSLMLLTQRV TSLSLDICEG KVEAPRRGIR SKSSFSEHLW DALPHFSYLL FFPALLGGSL
CSFRRFQACV QRSSSLYPSI SFRALTWRGL QILGLECLKV ALRSAVSAGA GLDDCQRLEC
IYLMWSTAWL FKLTYYSHWI LDDSLLHAAG FGAEAGQGPG EEGYVPDVDI WTLETTHRIS
LFARQWNRST ALWLRRLVFR KSRRWPLLQT FAFSAWWHGL HPGQVFGFLC WSVMVKADYL
IHTFANVCIR SWPLRLLYRA LTWAHTQLII AYIMLAVEGR SLSSLCQLCC SYNSLFPVMY
GLLLFLLAER KDKRN
