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Protein

Lysophospholipid acyltransferase 2

Gene

MBOAT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Acyltransferase which mediates the conversion of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Catalyzes also the acylation of lysophosphatidic acid (LPA) into phosphatidic acid (PA) (LPAAT activity). Has also a very weak lysophosphatidylcholine acyltransferase (LPCAT activity). Prefers oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle.1 Publication

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycero-3-phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-phosphoethanolamine.
Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Enzyme regulationi

Partially inhibited by thimerosal.

Pathway:iphospholipid metabolism

This protein is involved in the pathway phospholipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phospholipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei342 – 3421By similarity
Active sitei373 – 3731By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.23. 2681.
ReactomeiREACT_120829. Acyl chain remodelling of PC.
REACT_121369. Acyl chain remodelling of PE.
UniPathwayiUPA00085.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipid acyltransferase 2 (EC:2.3.1.-)
Short name:
LPLAT 2
Alternative name(s):
1-acylglycerophosphate O-acyltransferase (EC:2.3.1.51)
1-acylglycerophosphoethanolamine O-acyltransferase (EC:2.3.1.n7)
Lysophosphatidic acid acyltransferase
Short name:
LPAAT
Short name:
Lyso-PA acyltransferase
Lysophosphatidylethanolamine acyltransferase
Short name:
LPEAT
Short name:
Lyso-PE acyltransferase
Membrane-bound O-acyltransferase domain-containing protein 2
Short name:
O-acyltransferase domain-containing protein 2
Gene namesi
Name:MBOAT2
Synonyms:OACT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:25193. MBOAT2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei22 – 4221HelicalSequence AnalysisAdd
BLAST
Transmembranei61 – 8121HelicalSequence AnalysisAdd
BLAST
Transmembranei88 – 10821HelicalSequence AnalysisAdd
BLAST
Transmembranei184 – 20421HelicalSequence AnalysisAdd
BLAST
Transmembranei237 – 25721HelicalSequence AnalysisAdd
BLAST
Transmembranei264 – 28421HelicalSequence AnalysisAdd
BLAST
Transmembranei366 – 38621HelicalSequence AnalysisAdd
BLAST
Transmembranei416 – 43621HelicalSequence AnalysisAdd
BLAST
Transmembranei444 – 46421HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134987740.

Polymorphism and mutation databases

BioMutaiMBOAT2.
DMDMi143811417.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Lysophospholipid acyltransferase 2PRO_0000273020Add
BLAST

Proteomic databases

MaxQBiQ6ZWT7.
PaxDbiQ6ZWT7.
PRIDEiQ6ZWT7.

PTM databases

PhosphoSiteiQ6ZWT7.

Expressioni

Tissue specificityi

Expressed in neutrophils.1 Publication

Gene expression databases

BgeeiQ6ZWT7.
CleanExiHS_MBOAT2.
ExpressionAtlasiQ6ZWT7. baseline and differential.
GenevisibleiQ6ZWT7. HS.

Organism-specific databases

HPAiHPA014836.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000302177.

Structurei

3D structure databases

ProteinModelPortaliQ6ZWT7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5202.
GeneTreeiENSGT00550000074565.
HOGENOMiHOG000015994.
HOVERGENiHBG058823.
InParanoidiQ6ZWT7.
KOiK13517.
OMAiEGRSYHI.
OrthoDBiEOG73Z2SW.
PhylomeDBiQ6ZWT7.
TreeFamiTF314906.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6ZWT7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAI WFRTYLHSSK
60 70 80 90 100
TSSFIRHVVA TLLGLYLALF CFGWYALHFL VQSGISYCIM IIIGVENMHN
110 120 130 140 150
YCFVFALGYL TVCQVTRVYI FDYGQYSADF SGPMMIITQK ITSLACEIHD
160 170 180 190 200
GMFRKDEELT SSQRDLAVRR MPSLLEYLSY NCNFMGILAG PLCSYKDYIT
210 220 230 240 250
FIEGRSYHIT QSGENGKEET QYERTEPSPN TAVVQKLLVC GLSLLFHLTI
260 270 280 290 300
CTTLPVEYNI DEHFQATASW PTKIIYLYIS LLAARPKYYF AWTLADAINN
310 320 330 340 350
AAGFGFRGYD ENGAARWDLI SNLRIQQIEM STSFKMFLDN WNIQTALWLK
360 370 380 390 400
RVCYERTSFS PTIQTFILSA IWHGVYPGYY LTFLTGVLMT LAARAMRNNF
410 420 430 440 450
RHYFIEPSQL KLFYDVITWI VTQVAISYTV VPFVLLSIKP SLTFYSSWYY
460 470 480 490 500
CLHILGILVL LLLPVKKTQR RKNTHENIQL SQSKKFDEGE NSLGQNSFST
510 520
TNNVCNQNQE IASRHSSLKQ
Length:520
Mass (Da):59,527
Last modified:April 3, 2007 - v2
Checksum:i27FFC44815B21288
GO

Sequence cautioni

The sequence BAC11204.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti402 – 4021H → R in BAC11204 (PubMed:16303743).Curated
Sequence conflicti484 – 4841K → R in BAC85105 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti501 – 5011T → A.
Corresponds to variant rs16866827 [ dbSNP | Ensembl ].
VAR_030068

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB305044 mRNA. Translation: BAF93900.1.
AK027321 mRNA. Translation: BAC85105.1.
AC012495 Genomic DNA. No translation available.
AC112723 Genomic DNA. No translation available.
BC016005 mRNA. Translation: AAH16005.1.
BC146871 mRNA. Translation: AAI46872.1.
BC157827 mRNA. Translation: AAI57828.1.
AK074779 mRNA. Translation: BAC11204.1. Different initiation.
CCDSiCCDS1660.1.
RefSeqiNP_620154.2. NM_138799.2.
UniGeneiHs.467634.
Hs.593538.

Genome annotation databases

EnsembliENST00000305997; ENSP00000302177; ENSG00000143797.
GeneIDi129642.
KEGGihsa:129642.
UCSCiuc002qzg.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB305044 mRNA. Translation: BAF93900.1.
AK027321 mRNA. Translation: BAC85105.1.
AC012495 Genomic DNA. No translation available.
AC112723 Genomic DNA. No translation available.
BC016005 mRNA. Translation: AAH16005.1.
BC146871 mRNA. Translation: AAI46872.1.
BC157827 mRNA. Translation: AAI57828.1.
AK074779 mRNA. Translation: BAC11204.1. Different initiation.
CCDSiCCDS1660.1.
RefSeqiNP_620154.2. NM_138799.2.
UniGeneiHs.467634.
Hs.593538.

3D structure databases

ProteinModelPortaliQ6ZWT7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000302177.

PTM databases

PhosphoSiteiQ6ZWT7.

Polymorphism and mutation databases

BioMutaiMBOAT2.
DMDMi143811417.

Proteomic databases

MaxQBiQ6ZWT7.
PaxDbiQ6ZWT7.
PRIDEiQ6ZWT7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305997; ENSP00000302177; ENSG00000143797.
GeneIDi129642.
KEGGihsa:129642.
UCSCiuc002qzg.1. human.

Organism-specific databases

CTDi129642.
GeneCardsiGC02M008996.
H-InvDBHIX0001805.
HGNCiHGNC:25193. MBOAT2.
HPAiHPA014836.
MIMi611949. gene.
neXtProtiNX_Q6ZWT7.
PharmGKBiPA134987740.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5202.
GeneTreeiENSGT00550000074565.
HOGENOMiHOG000015994.
HOVERGENiHBG058823.
InParanoidiQ6ZWT7.
KOiK13517.
OMAiEGRSYHI.
OrthoDBiEOG73Z2SW.
PhylomeDBiQ6ZWT7.
TreeFamiTF314906.

Enzyme and pathway databases

UniPathwayiUPA00085.
BRENDAi2.3.1.23. 2681.
ReactomeiREACT_120829. Acyl chain remodelling of PC.
REACT_121369. Acyl chain remodelling of PE.

Miscellaneous databases

ChiTaRSiMBOAT2. human.
GenomeRNAii129642.
NextBioi82616.
PROiQ6ZWT7.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZWT7.
CleanExiHS_MBOAT2.
ExpressionAtlasiQ6ZWT7. baseline and differential.
GenevisibleiQ6ZWT7. HS.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation of lysophospholipids in the yeast Saccharomyces cerevisiae."
    Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M., Miyagawa H., Nozaki H., Nakayama R., Kumagai H.
    J. Biol. Chem. 282:34288-34298(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain, Lung and Testis.
  5. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-520.
    Tissue: Teratocarcinoma.
  6. "Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils."
    Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.
    J. Biol. Chem. 283:30235-30245(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiMBOA2_HUMAN
AccessioniPrimary (citable) accession number: Q6ZWT7
Secondary accession number(s): A9EDR2, Q8NCE7, Q96KY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: April 3, 2007
Last modified: July 22, 2015
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.