Reviewed, UniProtKB/Swiss-Prot Q8R3I2 (MBOA2_MOUSE)

Names and origin

Protein names

Recommended name:
    Lysophospholipid acyltransferase 2
      Short name=LPLAT 2
    EC=2.3.1.-
Alternative name(s):
    1-acylglycerophosphocholine O-acyltransferase
    EC=2.3.1.23
    Lysophosphatidylcholine acyltransferase
      Short name=Lyso-PC acyltransferase
      Short name=LPCAT
    Lysophosphatidylcholine acyltransferase 4
      Short name=Lyso-PC acyltransferase 4
      Short name=mLPCAT4
    1-acylglycerophosphoethanolamine O-acyltransferase
    EC=2.3.1.n2
    Lysophosphatidylethanolamine acyltransferase
      Short name=Lyso-PE acyltransferase
      Short name=LPEAT
    Membrane-bound O-acyltransferase domain-containing protein 2
      Short name=O-acyltransferase domain-containing protein 2

Gene names

Name:	Mboat2
Synonyms:	Lpcat4, Oact2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	519 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). To a lesser extent, also catalyzes the acylation of lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT 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.2
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine. Acyl-CoA + 1-acyl-sn-glycero-3-phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-phosphoethanolamine.
Pathway	Lipid metabolism; phospholipid metabolism.
Subcellular location	Membrane; Multi-pass membrane protein Potential. Endoplasmic reticulum.
Tissue specificity	Highly expressed in epididymis, brain, testis, and ovary. Ref.2
Sequence similarities	Belongs to the membrane-bound acyltransferase family.
Biophysicochemical properties	Kinetic parameters: KM=5.3 µM for oleoyl-CoA (in the presence of LPC C16:0 as cosubstrate) KM=48.15 µM for oleoyl-CoA (in the presence of LPE C16:0 as cosubstrate) KM=7.9 µM for LPC C16:0 (in the presence of oleoyl-CoA as cosubstrate) KM=27.7 µM for LPE C16:0 (in the presence of oleoyl-CoA as cosubstrate) Vmax=24.24 nmol/min/mg enzyme with oleoyl-CoA and LPC C16:0 as substrates Vmax=26.3 nmol/min/mg enzyme with oleoyl-CoA and LPE C16:0 as substrates

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-acylglycerophosphocholine O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8R3I2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8R3I2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     100-132: QCCFVFALGYLSVCQITRVYIFDYGQYSADFSG → H

Isoform 3 (identifier: Q8R3I2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-141: Missing.
     142-150: TSLAYEIHD → MDNILLIFQ

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 519	519	Lysophospholipid acyltransferase 2		PRO_0000273021
Regions
	Transmembrane	22 – 42	21	Potential
	Transmembrane	61 – 81	21	Potential
	Transmembrane	88 – 108	21	Potential
	Transmembrane	184 – 204	21	Potential
	Transmembrane	236 – 256	21	Potential
	Transmembrane	263 – 283	21	Potential
	Transmembrane	365 – 385	21	Potential
	Transmembrane	415 – 435	21	Potential
	Transmembrane	443 – 463	21	Potential
Natural variations
	Alternative sequence	1 – 141	141	Missing in isoform 3.		VSP_022457
	Alternative sequence	100 – 132	33	QCCFV…ADFSG → H in isoform 2.		VSP_022458
	Alternative sequence	142 – 150	9	TSLAYEIHD → MDNILLIFQ in isoform 3.		VSP_022459
Experimental info
	Sequence conflict	28	1	F → S in BAB28556. Ref.3
	Sequence conflict	40	1	V → L in BAB28556. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: A21F3947612314EE	FASTA	519	58,995
	10 20 30 40 50 60 MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAV WFRTYLHSSK TSSFIRHVVA 70 80 90 100 110 120 TLLGLYLAFF CFGWYALHFL VQSGISYCIM IIAGVESMQQ CCFVFALGYL SVCQITRVYI 130 140 150 160 170 180 FDYGQYSADF SGPMMIITQK ITSLAYEIHD GMFRKDEELT PSQRGLAVRR MPSLLEYVSY 190 200 210 220 230 240 TCNFMGILAG PLCSYKDYIA FIEGRASHVA QPSENGKDEQ HGKADPSPNA AVTEKLLVCG 250 260 270 280 290 300 LSLLFHLTIS NMLPVEYNID EHFQATASWP TKATYLYVSL LAARPKYYFA WTLADAINNA 310 320 330 340 350 360 AGFGFRGYDK NGVARWDLIS NLRIQQIEMS TSFKMFLDNW NIQTALWLKR VCYERATFSP 370 380 390 400 410 420 TIQTFFLSAI WHGVYPGYYL TFLTGVLMTL AARAVRNNFR HYFLEPPQLK LFYDLITWVA 430 440 450 460 470 480 TQITISYTVV PFVLLSIKPS FTFYSSWYYC LHVCSILVLL LLPVKKSQRR TSTQENVHLS 490 500 510 QAKKFDERDN PLGQNSFSTM NNVCNQNRDT GSRHSSLTQ
	Isoform 2. Checksum: 351F46E21169C1A6	FASTA	487	55,385
	10 20 30 40 50 60 MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAV WFRTYLHSSK TSSFIRHVVA 70 80 90 100 110 120 TLLGLYLAFF CFGWYALHFL VQSGISYCIM IIAGVESMQH PMMIITQKIT SLAYEIHDGM 130 140 150 160 170 180 FRKDEELTPS QRGLAVRRMP SLLEYVSYTC NFMGILAGPL CSYKDYIAFI EGRASHVAQP 190 200 210 220 230 240 SENGKDEQHG KADPSPNAAV TEKLLVCGLS LLFHLTISNM LPVEYNIDEH FQATASWPTK 250 260 270 280 290 300 ATYLYVSLLA ARPKYYFAWT LADAINNAAG FGFRGYDKNG VARWDLISNL RIQQIEMSTS 310 320 330 340 350 360 FKMFLDNWNI QTALWLKRVC YERATFSPTI QTFFLSAIWH GVYPGYYLTF LTGVLMTLAA 370 380 390 400 410 420 RAVRNNFRHY FLEPPQLKLF YDLITWVATQ ITISYTVVPF VLLSIKPSFT FYSSWYYCLH 430 440 450 460 470 480 VCSILVLLLL PVKKSQRRTS TQENVHLSQA KKFDERDNPL GQNSFSTMNN VCNQNRDTGS RHSSLTQ
	Isoform 3. Checksum: 0B9F5DCABA3A4454	FASTA	378	43,297
	10 20 30 40 50 60 MDNILLIFQG MFRKDEELTP SQRGLAVRRM PSLLEYVSYT CNFMGILAGP LCSYKDYIAF 70 80 90 100 110 120 IEGRASHVAQ PSENGKDEQH GKADPSPNAA VTEKLLVCGL SLLFHLTISN MLPVEYNIDE 130 140 150 160 170 180 HFQATASWPT KATYLYVSLL AARPKYYFAW TLADAINNAA GFGFRGYDKN GVARWDLISN 190 200 210 220 230 240 LRIQQIEMST SFKMFLDNWN IQTALWLKRV CYERATFSPT IQTFFLSAIW HGVYPGYYLT 250 260 270 280 290 300 FLTGVLMTLA ARAVRNNFRH YFLEPPQLKL FYDLITWVAT QITISYTVVP FVLLSIKPSF 310 320 330 340 350 360 TFYSSWYYCL HVCSILVLLL LPVKKSQRRT STQENVHLSQ AKKFDERDNP LGQNSFSTMN 370 NVCNQNRDTG SRHSSLTQ

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] (ISOFORM 1).
[2]	"Discovery of a lysophospholipid acyltransferase family essential for membrane asymmetry and diversity." Hishikawa D., Shindou H., Kobayashi S., Nakanishi H., Taguchi R., Shimizu T. Proc. Natl. Acad. Sci. U.S.A. 105:2830-2835(2008) [PubMed: 18287005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Strain: C57BL/6J. Tissue: Embryoid bodies, Medulla oblongata and Testis.
[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] (ISOFORM 2). Strain: Czech II. Tissue: Eye and Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB305046 mRNA. Translation: BAF93902.1. AB297383 mRNA. Translation: BAG12122.1. AK012931 mRNA. Translation: BAB28556.1. AK031824 mRNA. Translation: BAC27567.1. Different initiation. AK033106 mRNA. Translation: BAC28154.1. AK034873 mRNA. Translation: BAC28863.1. AK076045 mRNA. Translation: BAC36144.1. BC025020 mRNA. Translation: AAH25020.1.
IPI	IPI00153761. IPI00468901. IPI00828734.
RefSeq	NP_001076810.1. NP_080313.2.
UniGene	Mm.167671
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q8R3I2.
Proteomic databases
PRIDE	Q8R3I2.
Genome annotation databases
Ensembl	ENSMUST00000020976; ENSMUSP00000020976; ENSMUSG00000020646; Mus musculus. [Genome view] ENSMUST00000078902; ENSMUSP00000077937; ENSMUSG00000020646; Mus musculus. [Genome view] ENSMUST00000110942; ENSMUSP00000106567; ENSMUSG00000020646; Mus musculus. [Genome view] ENSMUST00000116439; ENSMUSP00000112140; ENSMUSG00000020646; Mus musculus. [Genome view]
GeneID	67216.
KEGG	mmu:67216.
UCSC	uc007neu.1. mouse. uc007nev.1. mouse. uc007new.1. mouse.
Organism-specific databases
CTD	67216.
MGI	MGI:1914466. Mboat2.
Phylogenomic databases
HOVERGEN	Q8R3I2.
OMA	FYSSWYY.
Gene expression databases
ArrayExpress	Q8R3I2.
Bgee	Q8R3I2.
Genevestigator	Q8R3I2.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	323902.
SOURCE	Search...

Entry information

Entry name

MBOA2_MOUSE

Accession

Primary (citable) accession number: Q8R3I2
Secondary accession number(s): A9EDS7 , Q8BHH5, Q8BM56, Q8R192, Q9CZ73

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	June 1, 2002
Last modified:	November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)