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Q6ZWT7 (MBOA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysophospholipid acyltransferase 2

Short name=LPLAT 2
EC=2.3.1.-
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 names
Name:MBOAT2
Synonyms:OACT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

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 regulation

Partially inhibited by thimerosal.

Pathway

Lipid metabolism; phospholipid metabolism.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Expressed in neutrophils. Ref.6

Sequence similarities

Belongs to the membrane-bound acyltransferase family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Lysophospholipid acyltransferase 2
PRO_0000273020

Regions

Transmembrane22 – 4221Helical; Potential
Transmembrane61 – 8121Helical; Potential
Transmembrane88 – 10821Helical; Potential
Transmembrane184 – 20421Helical; Potential
Transmembrane237 – 25721Helical; Potential
Transmembrane264 – 28421Helical; Potential
Transmembrane366 – 38621Helical; Potential
Transmembrane416 – 43621Helical; Potential
Transmembrane444 – 46421Helical; Potential

Sites

Active site3421 By similarity
Active site3731 By similarity

Natural variations

Natural variant5011T → A.
Corresponds to variant rs16866827 [ dbSNP | Ensembl ].
VAR_030068

Experimental info

Sequence conflict4021H → R in BAC11204. Ref.5
Sequence conflict4841K → R in BAC85105. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6ZWT7 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 27FFC44815B21288

FASTA52059,527
        10         20         30         40         50         60 
MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAI WFRTYLHSSK TSSFIRHVVA 

        70         80         90        100        110        120 
TLLGLYLALF CFGWYALHFL VQSGISYCIM IIIGVENMHN YCFVFALGYL TVCQVTRVYI 

       130        140        150        160        170        180 
FDYGQYSADF SGPMMIITQK ITSLACEIHD GMFRKDEELT SSQRDLAVRR MPSLLEYLSY 

       190        200        210        220        230        240 
NCNFMGILAG PLCSYKDYIT FIEGRSYHIT QSGENGKEET QYERTEPSPN TAVVQKLLVC 

       250        260        270        280        290        300 
GLSLLFHLTI CTTLPVEYNI DEHFQATASW PTKIIYLYIS LLAARPKYYF AWTLADAINN 

       310        320        330        340        350        360 
AAGFGFRGYD ENGAARWDLI SNLRIQQIEM STSFKMFLDN WNIQTALWLK RVCYERTSFS 

       370        380        390        400        410        420 
PTIQTFILSA IWHGVYPGYY LTFLTGVLMT LAARAMRNNF RHYFIEPSQL KLFYDVITWI 

       430        440        450        460        470        480 
VTQVAISYTV VPFVLLSIKP SLTFYSSWYY CLHILGILVL LLLPVKKTQR RKNTHENIQL 

       490        500        510        520 
SQSKKFDEGE NSLGQNSFST TNNVCNQNQE IASRHSSLKQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_620154.2. NM_138799.2.
UniGeneHs.467634.
Hs.593538.

3D structure databases

ProteinModelPortalQ6ZWT7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000302177.

PTM databases

PhosphoSiteQ6ZWT7.

Polymorphism databases

DMDM143811417.

Proteomic databases

PaxDbQ6ZWT7.
PRIDEQ6ZWT7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305997; ENSP00000302177; ENSG00000143797.
GeneID129642.
KEGGhsa:129642.
UCSCuc002qzg.1. human.

Organism-specific databases

CTD129642.
GeneCardsGC02M008910.
H-InvDBHIX0001805.
HGNCHGNC:25193. MBOAT2.
HPAHPA014836.
MIM611949. gene.
neXtProtNX_Q6ZWT7.
PharmGKBPA134987740.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5202.
HOGENOMHOG000015994.
HOVERGENHBG058823.
InParanoidQ6ZWT7.
KOK13517.
OMAIVTQVAI.
OrthoDBEOG73Z2SW.
PhylomeDBQ6ZWT7.
TreeFamTF314906.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00085.

Gene expression databases

ArrayExpressQ6ZWT7.
BgeeQ6ZWT7.
CleanExHS_MBOAT2.
GenevestigatorQ6ZWT7.

Family and domain databases

InterProIPR004299. MBOAT_fam.
[Graphical view]
PfamPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMBOAT2. human.
GenomeRNAi129642.
NextBio82616.
PROQ6ZWT7.
SOURCESearch...

Entry information

Entry nameMBOA2_HUMAN
AccessionPrimary (citable) accession number: Q6ZWT7
Secondary accession number(s): A9EDR2, Q8NCE7, Q96KY4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM