Reviewed, UniProtKB/Swiss-Prot Q6ZWT7 (MBOA2_HUMAN)

Names and origin

Protein names

Recommended name:
    Lysophospholipid acyltransferase 2
      Short name=LPLAT 2
    EC=2.3.1.-
Alternative name(s):
    1-acylglycerophosphoethanolamine O-acyltransferase
    EC=2.3.1.n2
    Lysophosphatidylethanolamine acyltransferase
      Short name=Lyso-PE acyltransferase
      Short name=LPEAT
    1-acylglycerophosphate O-acyltransferase
    EC=2.3.1.51
    Lysophosphatidic acid acyltransferase
      Short name=Lyso-PA acyltransferase
      Short name=LPAAT
    Membrane-bound O-acyltransferase domain-containing protein 2
      Short name=O-acyltransferase domain-containing protein 2

Gene names

Name:	MBOAT2
Synonyms:	OACT2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	Lysophospholipid acyltransferase 2		PRO_0000273020
Regions
	Transmembrane	22 – 42	21	Potential
	Transmembrane	61 – 81	21	Potential
	Transmembrane	88 – 108	21	Potential
	Transmembrane	184 – 204	21	Potential
	Transmembrane	237 – 257	21	Potential
	Transmembrane	264 – 284	21	Potential
	Transmembrane	366 – 386	21	Potential
	Transmembrane	416 – 436	21	Potential
	Transmembrane	444 – 464	21	Potential
Natural variations
	Natural variant	501	1	T → A: dbSNP rs16866827.		VAR_030068
Experimental info
	Sequence conflict	402	1	H → R in BAC11204. Ref.5
	Sequence conflict	484	1	K → R in BAC85105. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q6ZWT7-1 [UniParc]. Last modified April 3, 2007. Version 2. Checksum: 27FFC44815B21288	FASTA	520	59,527
	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

References

	« Hide 'large scale' referencesShow '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: 17890783] [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: 14702039] [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: 15815621] [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: 15489334] [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: 16303743] [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: 18772128] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00419221.
RefSeq	NP_620154.2.
UniGene	Hs.467634 Hs.593538
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6ZWT7.
PTM databases
PhosphoSite	Q6ZWT7.
Genome annotation databases
Ensembl	ENST00000305997; ENSP00000302177; ENSG00000143797; Homo sapiens. [Genome view]
GeneID	129642.
KEGG	hsa:129642.
UCSC	uc002qzg.1. human.
Organism-specific databases
CTD	129642.
GeneCards	GC02M008910.
HGNC	HGNC:25193. MBOAT2.
HPA	HPA014836.
MIM	611949. gene.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q6ZWT7.
OMA	FYSSWYY.
Gene expression databases
ArrayExpress	Q6ZWT7.
Bgee	Q6ZWT7.
CleanEx	HS_MBOAT2.
Genevestigator	Q6ZWT7.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	82616.
SOURCE	Search...

Entry information

Entry name

MBOA2_HUMAN

Accession

Primary (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:	November 3, 2009
This is version 40 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.