MBOA2_CHICK
ID MBOA2_CHICK Reviewed; 518 AA.
AC Q5ZKL6;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Lysophospholipid acyltransferase 2 {ECO:0000250|UniProtKB:Q6ZWT7};
DE Short=LPLAT 2;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q6ZWT7};
DE AltName: Full=1-acylglycerophosphate O-acyltransferase {ECO:0000250|UniProtKB:Q6ZWT7};
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q6ZWT7};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase {ECO:0000250|UniProtKB:Q6ZWT7};
DE EC=2.3.1.23 {ECO:0000250|UniProtKB:Q6ZWT7};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase {ECO:0000250|UniProtKB:Q6ZWT7};
DE EC=2.3.1.n7 {ECO:0000250|UniProtKB:Q6ZWT7};
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 2 {ECO:0000250|UniProtKB:Q6ZWT7};
DE Short=O-acyltransferase domain-containing protein 2;
DE EC=2.3.-.- {ECO:0000250|UniProtKB:Q6ZWT7};
GN Name=mboat2 {ECO:0000250|UniProtKB:Q6ZWT7}; Synonyms=oact2;
GN ORFNames=RCJMB04_10b24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Acyltransferase which catalyzes the transfert of an acyl
CC group from an acyl-CoA to a lysophospholipid leading to the production
CC of a phospholipid and participates in the reacylation step of the
CC phospholipid remodeling pathway also known as the Lands cycle. May
CC catalyze preferentially the acylation of lysophosphatidylethanolamine
CC (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) and lysophosphatidic
CC acid (LPA) and to a lesser extend lysophosphatidylcholine (LPC) and
CC lysophosphatidylserine (LPS). Prefers oleoyl-CoA as the acyl donor.
CC {ECO:0000250|UniProtKB:Q6ZWT7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:36015, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36016;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z)-hexadecenoyl-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37419, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:73004, ChEBI:CHEBI:73999;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37420;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine +
CC hexadecanoyl-CoA = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-
CC phosphoserine + CoA; Xref=Rhea:RHEA:37415, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:74617, ChEBI:CHEBI:74909;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37416;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35995,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-[(9Z)-hexadec-9-enoyl]-sn-glycero-3-phosphate +
CC CoA; Xref=Rhea:RHEA:37223, ChEBI:CHEBI:57287, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:73998;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37224;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphocholine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37627, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:77287, ChEBI:CHEBI:77294;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37628;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37631,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:77288,
CC ChEBI:CHEBI:77291; Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37632;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37523, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75036, ChEBI:CHEBI:75038;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37524;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphocholine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37519, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73858, ChEBI:CHEBI:75034;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37520;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37500;
CC Evidence={ECO:0000250|UniProtKB:Q8R3I2};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:Q6ZWT7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6ZWT7}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q6ZWT7}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q8R3I2}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ720068; CAG31727.1; -; mRNA.
DR RefSeq; NP_001026261.1; NM_001031090.1.
DR AlphaFoldDB; Q5ZKL6; -.
DR SMR; Q5ZKL6; -.
DR STRING; 9031.ENSGALP00000026423; -.
DR PaxDb; Q5ZKL6; -.
DR PRIDE; Q5ZKL6; -.
DR Ensembl; ENSGALT00000026473; ENSGALP00000026423; ENSGALG00000016412.
DR GeneID; 421925; -.
DR KEGG; gga:421925; -.
DR CTD; 129642; -.
DR VEuPathDB; HostDB:geneid_421925; -.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_0_1; -.
DR InParanoid; Q5ZKL6; -.
DR OMA; WAISIFE; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q5ZKL6; -.
DR TreeFam; TF314906; -.
DR Reactome; R-GGA-1482788; Acyl chain remodelling of PC.
DR Reactome; R-GGA-1482839; Acyl chain remodelling of PE.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q5ZKL6; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000016412; Expressed in cerebellum and 11 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISS:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..518
FT /note="Lysophospholipid acyltransferase 2"
FT /id="PRO_0000273023"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 341
FT /evidence="ECO:0000250"
FT ACT_SITE 372
FT /evidence="ECO:0000250"
SQ SEQUENCE 518 AA; 59552 MW; 4173ECC36901C261 CRC64;
MATSTTGSTL LQPLSNAVRL PVDQVNFVVC QLFALLAAIW FRTYLHSSKT SPFIRHVVAT
LLGLYLALFC FGWYALHFVI QSGISYYLMI IIGVENMHKY CFVFALGYLT VCQITRVYIF
DYGQYSADFS GPMMIITQKI TSLAFEIHDG MFRKNEDLTP SQRCLAVRRM PSLLEYLSYN
CNFMGILAGP LCSYKDYITF IEGRSYQLQQ SEANGKEDTK YEQTDPSPNI AVAQKLLICG
LSLLFHMTIT KTLPVEYNID ENFRATASWP VRVFYLYLSL MAARPKYYFA WTLADAINNA
AGFGFRGYDK NGVTRWDLIS NLRIQQIESS TSFKMFLDNW NIQTALWLKR VCYERATFSP
TIQTFILSAI WHGVYPGYYL TFLTGVLMTL AARAIRNNIR HYFVESPAVK LCYDIITWMT
TQVAISYTVV PFVLLSVKPS FTFYSSCYFC LHIASILVLL VFPLKRTQKG NKQHESIQPV
WSKKLEEENL LQKNSYSTTN NSFSQKEEIT CRYQALKQ
