Reviewed, UniProtKB/Swiss-Prot Q91V01 (MBOA5_MOUSE)

Names and origin

Protein names

Recommended name:
    Lysophospholipid acyltransferase 5
      Short name=LPLAT 5
    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 3
      Short name=Lyso-PC acyltransferase 3
      Short name=mLPCAT3
    1-acylglycerophosphoethanolamine O-acyltransferase
    EC=2.3.1.n2
    Lysophosphatidylethanolamine acyltransferase
      Short name=Lyso-PE acyltransferase
      Short name=LPEAT
    1-acylglycerophosphoserine O-acyltransferase
    EC=2.3.1.n3
    Lysophosphatidylserine acyltransferase
      Short name=Lyso-PS acyltransferase
      Short name=LPSAT
    Membrane-bound O-acyltransferase domain-containing protein 5
      Short name=O-acyltransferase domain-containing protein 5

Gene names

Name:	Lpcat3
Synonyms:	Grcc3f, Mboat5, Oact5

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	487 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), and the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. 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. Acyl-CoA + 1-acyl-sn-glycero-3-phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3-phosphatidylserine.
Pathway	Lipid metabolism; phospholipid metabolism.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Ref.2
Tissue specificity	Detected ubiquitously, with high expression levels in testis. Ref.2
Domain	The di-lysine motif confers endoplasmic reticulum localization By similarity.
Sequence similarities	Belongs to the membrane-bound acyltransferase family.
Biophysicochemical properties	Kinetic parameters: KM=7.8 µM for arachidonoyl-CoA (in the presence of LPC C16:0 as cosubstrate) KM=44.1 µM for arachidonoyl-CoA (in the presence of LPE C18:1 as cosubstrate) KM=28 µM for arachidonoyl-CoA (in the presence of LPS C18:1 as cosubstrate) KM=34.5 µM for LPC C16:0 (in the presence of arachidonoyl-CoA as cosubstrate) KM=29.7 µM for LPE C18:1 (in the presence of arachidonoyl-CoA as cosubstrate) KM=22.3 µM for LPS C18:1 (in the presence of arachidonoyl-CoA as cosubstrate) Vmax=1085.5 nmol/min/mg enzyme with arachidonoyl-CoA and LPC C16:0 as substrates Vmax=389.25 nmol/min/mg enzyme with arachidonoyl-CoA and LPE C18:1 as substrates Vmax=335.75 nmol/min/mg enzyme with arachidonoyl-CoA and LPS C18:1 as substrates

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein
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-KW 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 487	487	Lysophospholipid acyltransferase 5		PRO_0000233383
Regions
	Transmembrane	44 – 64	21	Potential
	Transmembrane	84 – 104	21	Potential
	Transmembrane	111 – 131	21	Potential
	Transmembrane	180 – 200	21	Potential
	Transmembrane	236 – 256	21	Potential
	Transmembrane	285 – 305	21	Potential
	Transmembrane	364 – 384	21	Potential
	Transmembrane	422 – 442	21	Potential
	Transmembrane	453 – 473	21	Potential
	Motif	484 – 487	4	Di-lysine motif
Sites
	Active site	428	1	Potential
Amino acid modifications
	Glycosylation	225	1	N-linked (GlcNAc...) Potential
	Glycosylation	308	1	N-linked (GlcNAc...) Potential
	Glycosylation	331	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	48 – 49	2	IF → SH in AAC36007. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q91V01-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: EBC51DB3734B17C7	FASTA	487	56,147
	10 20 30 40 50 60 MASTADGDMG ETLEQMRGLW PGVEDLSLNK LATSLGASEQ ALRLIFSIFL GYPLALFYRH 70 80 90 100 110 120 YLFYKDSYLI HLFHTFTGLS IAYFNFGHQF YHSLLCVVLQ FLILRLMGRT VTAVITTLCF 130 140 150 160 170 180 QMAYLLAGYY YTATGDYDIK WTMPHCVLTL KLIGLCIDYY DGGKDGNSLT SEQQKYAIRG 190 200 210 220 230 240 VPSLLEVAGF SYFYGAFLVG PQFSMNHYMK LVRGQLTDIP GKMPNSTIPA LKRLSLGLVY 250 260 270 280 290 300 LVGYTLLSPH ITDDYLLTED YDNRPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILSGL 310 320 330 340 350 360 GFNGFDENGT VRWDACANMK VWLFETTPRF NGTIASFNIN TNAWVARYIF KRLKFLGNKE 370 380 390 400 410 420 LSQGLSLLFL ALWHGLHSGY LICFQMEFLI VIVEKQVSSL IRDSPALSSL ASITALQPFY 430 440 450 460 470 480 YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV YRSIYFLGHV FFLSLLFILP YIHKAMVPRK EKLKKRE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and initial characterization of mouse PTG cDNA, whose expression is in a PPAR alpha dependent manner." Zhu Y., Han Y., Reddy J.K. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J. Tissue: Liver.
[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], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]. Strain: FVB/N. Tissue: Mammary gland.
[5]	"Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6." Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A. Genome Res. 8:29-40(1998) [PubMed: 9445485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-487.
[6]	"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] OF 114-487. Strain: C57BL/6J.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY028317 mRNA. Translation: AAK20915.1. AB294194 mRNA. Translation: BAG12120.1. CH466523 Genomic DNA. Translation: EDK99746.1. BC006753 mRNA. Translation: AAH06753.2. AC002397 Genomic DNA. Translation: AAC36007.1. AK083687 mRNA. Translation: BAC38993.1.
IPI	IPI00380082.
RefSeq	NP_660112.1.
UniGene	Mm.273915
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q91V01.
Proteomic databases
PRIDE	Q91V01.
Genome annotation databases
Ensembl	ENSMUST00000004381; ENSMUSP00000004381; ENSMUSG00000004270; Mus musculus. [Genome view]
GeneID	14792.
KEGG	mmu:14792.
UCSC	uc009drf.1. mouse.
Organism-specific databases
CTD	14792.
MGI	MGI:1315211. Lpcat3.
Phylogenomic databases
HOVERGEN	Q91V01.
OMA	GYSMTAF.
Enzyme and pathway databases
BRENDA	2.3.1.23. 244.
Gene expression databases
ArrayExpress	Q91V01.
Bgee	Q91V01.
Genevestigator	Q91V01.
GermOnline	ENSMUSG00000004270. Mus musculus.
Family and domain databases
InterPro	IPR004299. MBOAT_fam. [Graphical view]
Pfam	PF03062. MBOAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	286935.
SOURCE	Search...

Entry information

Entry name

MBOA5_MOUSE

Accession

Primary (citable) accession number: Q91V01
Secondary accession number(s): B1B362, O35131, Q8BNH6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 2, 2006
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)