MBOA4_RAT
ID MBOA4_RAT Reviewed; 435 AA.
AC B1Q005;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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:0000312|RGD:1566335};
GN Name=Mboat4 {ECO:0000312|EMBL:ACB05875.1, ECO:0000312|RGD:1566335};
GN Synonyms=Goat {ECO:0000303|PubMed:18443287};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ACB05875.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:ACB05875.1};
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; EU518497; ACB05875.1; -; mRNA.
DR RefSeq; NP_001100787.2; NM_001107317.2.
DR RefSeq; XP_017455622.1; XM_017600133.1.
DR AlphaFoldDB; B1Q005; -.
DR STRING; 10116.ENSRNOP00000046106; -.
DR SwissLipids; SLP:000001958; -.
DR PaxDb; B1Q005; -.
DR PRIDE; B1Q005; -.
DR Ensembl; ENSRNOT00000042003; ENSRNOP00000046106; ENSRNOG00000030102.
DR GeneID; 306515; -.
DR KEGG; rno:306515; -.
DR UCSC; RGD:1566335; rat.
DR CTD; 619373; -.
DR RGD; 1566335; Mboat4.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_1_1; -.
DR InParanoid; B1Q005; -.
DR OMA; MDWLQLF; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; B1Q005; -.
DR TreeFam; TF314906; -.
DR Reactome; R-RNO-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR PRO; PR:B1Q005; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000030102; Expressed in stomach and 7 other tissues.
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:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0051366; P:protein decanoylation; ISO:RGD.
DR GO; GO:0018190; P:protein octanoylation; ISO:RGD.
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_0000347277"
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"
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"
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|UniProtKB:P0C7A3"
FT ACT_SITE 338
FT /evidence="ECO:0000250|UniProtKB:P0C7A3"
SQ SEQUENCE 435 AA; 50008 MW; FD6B293FDEA44115 CRC64;
MDWLQFFFLH PVSLYQGAAF PFALLFNYLC ITESFPTRAR YLFLLAGGGV LALAAMGPYA
LLIFIPALCA VAMISSLSPQ EVHGLTFFFQ MGWQTLCHLG LHYKEYYLCE PPPVRFYITL
SSLMLLTQRV TSLSLDISEG KVEAAWRGTR SRSSLCEHLW DALPYISYLL FFPALLGGSL
CSFQRFQACV QRPRSLYPSI SFWALTWRGL QILGLECLKV ALRRVVSAGA GLDDCQRLEC
IYIMWSTAGL FKLTYYSHWI LDDSLLHAAG FGSEAGQRPG EERYVPDVDI WTLETTHRIS
LFARQWNRST AQWLKRLVFQ RSRRWPVLQT FAFSAWWHGL HPGQVFGFLC WSVMVKADYL
IHTFANGCIR SWPLRLLYRS LTWAHTQIII AYVMLAVEGR SFSSLCRLCC SYNSIFPVTY
CLLLFLLARR KHKCN
