MBOA4_DANRE
ID MBOA4_DANRE Reviewed; 415 AA.
AC B1Q006;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Ghrelin O-acyltransferase {ECO:0000303|PubMed:18443287};
DE EC=2.3.1.- {ECO:0000269|PubMed:18443287};
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 4 {ECO:0000250|UniProtKB:Q96T53};
GN Name=mboat4 {ECO:0000312|EMBL:ACB05876.1};
GN Synonyms=goat {ECO:0000303|PubMed:18443287};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACB05876.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
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).
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 (By similarity) (PubMed:18443287). In vitro uses
CC also acyl-CoA donors of different lengths from short-chain (C2) to
CC long-chain fatty acids (C16) knowing that acyl-CoA donors from
CC butanoyl-CoA (C4) to dodecanoyl-CoA (C12) are more efficient compared
CC to longer acyl-CoA donors, such as myristoyl-CoA (C14) and palmitoyl-
CC CoA (C16) that are not efficient (By similarity).
CC {ECO:0000250|UniProtKB:Q96T53, ECO:0000269|PubMed:18443287}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59965;
CC Evidence={ECO:0000269|PubMed:18443287};
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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59973;
CC Evidence={ECO:0000250|UniProtKB:Q96T53};
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=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:0000250|UniProtKB:Q96T53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68285;
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 -!- 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 -!- PTM: Not glycosylated. {ECO:0000250|UniProtKB:P0C7A3}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000255}.
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DR EMBL; EU518498; ACB05876.1; -; mRNA.
DR RefSeq; NP_001116416.1; NM_001122944.1.
DR AlphaFoldDB; B1Q006; -.
DR SMR; B1Q006; -.
DR STRING; 7955.ENSDARP00000068385; -.
DR SwissLipids; SLP:000001959; -.
DR PaxDb; B1Q006; -.
DR GeneID; 795709; -.
DR KEGG; dre:795709; -.
DR CTD; 619373; -.
DR ZFIN; ZDB-GENE-090421-3; mboat4.
DR eggNOG; KOG2704; Eukaryota.
DR InParanoid; B1Q006; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; B1Q006; -.
DR Reactome; R-DRE-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR PRO; PR:B1Q006; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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: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:0032094; P:response to food; IDA:ZFIN.
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..415
FT /note="Ghrelin O-acyltransferase"
FT /id="PRO_0000347278"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3, ECO:0000255"
FT TOPO_DOM 29..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..58
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3, ECO:0000255"
FT TOPO_DOM 59..61
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..78
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 79..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 85..103
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 104..122
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 123..138
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 139..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 215..227
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3, ECO:0000255"
FT TOPO_DOM 248..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 313..326
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 327..328
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 329..345
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT TOPO_DOM 346..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..394
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 295
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
FT ACT_SITE 326
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
SQ SEQUENCE 415 AA; 47626 MW; F1EE1B4471CF0D2C CRC64;
MIDLLWISSD GHPQLFYQFI NIPFAFLFHC LSSQGHLSII NRYVYLAMGG FMLAIATMGP
YSSLLFLSAI KLLLLIHYIH PMHLHRWILG LQMCWQTCWH LYVQYQIYWL QEAPDSRLLL
AISALMLMTQ RISSLSLDFQ EGTISNQSIL IPFLTYSLYF PALLGGPLCS FNAFVQSVER
QHTSMTSYLG NLTSKISQVI VLVWIKQLFS ELLKSATFNI DSVCLDVLWI WIFSLTLRLN
YYAHWKMSEC VNNAAGLGVY FHKHSGQTSW DELSDGSVLV TEASSRPSVF ARKWNQTTVD
WLRKIVFNRT SRSPLFMTFG FSALWHGLHP GQILGFLIWA VTVQADYKLH RFSHPKLNSL
WRKRLYVCVN WAFTQLTVAC VVVCVELQSL ASVKLLWSSC IAVFPLLSAL ILIIL
