Reviewed, UniProtKB/Swiss-Prot Q8BYI6 (PCAT2_MOUSE)

Names and origin

Protein names

Recommended name:
    Lysophosphatidylcholine acyltransferase 2
      Short name=LPC acyltransferase 2
      Short name=LPCAT-2
    EC=2.3.1.-
Alternative name(s):
    1-alkylglycerophosphocholine O-acetyltransferase
    EC=2.3.1.67
    Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
      Short name=Acetyl-CoA:lyso-PAF acetyltransferase
      Short name=Lyso-PAF acetyltransferase
      Short name=LysoPAFAT
    1-acylglycerophosphocholine O-acyltransferase
    EC=2.3.1.23
    Acyltransferase-like 1

Gene names

Name:	Lpcat2
Synonyms:	Aytl1, Aytl1a, Lpcat2a

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

General annotation (Comments)

Function	Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Involved in platelet-activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-alkyl-phosphatidylcholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases. Ref.1 Ref.3
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine. Acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine.
Enzyme regulation	Acetyltransferase activity is increased following acute inflammatory stimulation by lipopolysaccharide (LPS). Acyltransferase activity is unchanged. Ref.1
Pathway	Lipid metabolism; phospholipid metabolism.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein. Golgi apparatus membrane; Single-pass type II membrane protein. Ref.1 Ref.3
Tissue specificity	Highest expression is found in resident macrophages and casein-induced neutrophils followed by skin, colon, spleen and thioglycollate-induced macrophages. Detected in erythroleukemic cells but not in reticulocytes. Ref.1 Ref.3
Induction	By inflammatory stimulation by LPS and by ODN1826, a TLR9 ligand, but not by poly(I:C), a TLR3 ligand. Ref.1
Domain	The HXXXXD motif is essential for acyltransferase activity By similarity.
Sequence similarities	Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. Contains 2 EF-hand domains.
Biophysicochemical properties	Kinetic parameters: KM=50.4 µM for acetyl-CoA KM=21.1 µM for arachidonoyl-CoA Temperature dependence: Optimum temperature is 7.4 degrees Celsius.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal-anchor Transmembrane
Ligand	Calcium
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	membrane organization Ref.1 Inferred from direct assay. Source: UniProtKB platelet activating factor biosynthetic process Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi stack Ref.1 Inferred from direct assay. Source: UniProtKB endoplasmic reticulum Ref.1 Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-acylglycerophosphocholine O-acyltransferase activity Ref.1 Inferred from direct assay. Source: UniProtKB 1-alkylglycerophosphocholine O-acetyltransferase activity Ref.1 Inferred from direct assay. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8BYI6-1)

Also known as: a; Aytl1_v1;

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: Q8BYI6-2)

Also known as: b; Aytl1_v2;

The sequence of this isoform differs from the canonical sequence as follows:
     215-254: Missing.

Isoform 3 (identifier: Q8BYI6-3)

Also known as: c; Aytl1_v3;

The sequence of this isoform differs from the canonical sequence as follows:
     215-236: ILVFPEGTCTNRSCLITFKPGA → EPSSQEFQCSPSSSDTQTSWIL
     237-544: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 544	544	Lysophosphatidylcholine acyltransferase 2		PRO_0000247059
Regions
	Topological domain	1 – 58	58	Cytoplasmic Potential
	Transmembrane	59 – 79	21	Signal-anchor for type II membrane protein Potential
	Topological domain	80 – 544	465	Lumenal Potential
	Domain	391 – 426	36	EF-hand 1
	Domain	428 – 463	36	EF-hand 2
	Calcium binding	404 – 415	12	1 Potential
	Calcium binding	441 – 452	12	2 Potential
	Motif	146 – 151	6	HXXXXD motif
Natural variations
	Alternative sequence	215 – 254	40	Missing in isoform 2.		VSP_037079
	Alternative sequence	215 – 236	22	ILVFP…FKPGA → EPSSQEFQCSPSSSDTQTSW IL in isoform 3.		VSP_037080
	Alternative sequence	237 – 544	308	Missing in isoform 3.		VSP_037081

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (a) (Aytl1_v1) [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 8A790A4C71BB8898	FASTA	544	60,254
	10 20 30 40 50 60 MNRCAEAAAV AATVPGSGVG DAGLRPPMVP RQASFFPPPV PNPFVQQTTI SASRRLQMFL 70 80 90 100 110 120 LGIILLPVRA LLVGIILLLA WPFAVISTAC CPEKLTHPIS NWRRKITRPA LTFLARAMFF 130 140 150 160 170 180 SMGFTVTVKG KVASPLEAPI FVVAPHSTFF DGIACVVAGL PSLVSRNENA QTPLVGRLLR 190 200 210 220 230 240 ALQPVLVSRV DPDSRKNTIN EIKKRATSGG EWPQILVFPE GTCTNRSCLI TFKPGAFIPG 250 260 270 280 290 300 VPVQPVLLRY PNKLDTVTWT WQGYTFLQLC VLTFCQLFTK VEIEFMPVQA PSEEEKNDPV 310 320 330 340 350 360 LFASRIRNLM AEALEIPVTD HTYEDCRLMI SAGQLTLPME AGLVEFSKIS RKLKLDWDGI 370 380 390 400 410 420 RKHLDEYASI ASSSKGGRIG IEEFAEYLKL PVSDVLRQLF ALFDRNNDGS IDFREYVIGL 430 440 450 460 470 480 AVLCNPANTE EIIQVAFKLF DVDEDGYITE EEFCTILQAS LGVPDLNVSG LFREIAQRDS 490 500 510 520 530 540 VSYEEFKSFA LKHPEYAKIF TTYLDLQTCH VFSLPEEVQT APSVASNKVS PESQEEGTSD KKVD
	Isoform 2 (b) (Aytl1_v2). Checksum: A8F8F2F31006CAD9	FASTA	504	55,871
	10 20 30 40 50 60 MNRCAEAAAV AATVPGSGVG DAGLRPPMVP RQASFFPPPV PNPFVQQTTI SASRRLQMFL 70 80 90 100 110 120 LGIILLPVRA LLVGIILLLA WPFAVISTAC CPEKLTHPIS NWRRKITRPA LTFLARAMFF 130 140 150 160 170 180 SMGFTVTVKG KVASPLEAPI FVVAPHSTFF DGIACVVAGL PSLVSRNENA QTPLVGRLLR 190 200 210 220 230 240 ALQPVLVSRV DPDSRKNTIN EIKKRATSGG EWPQDTVTWT WQGYTFLQLC VLTFCQLFTK 250 260 270 280 290 300 VEIEFMPVQA PSEEEKNDPV LFASRIRNLM AEALEIPVTD HTYEDCRLMI SAGQLTLPME 310 320 330 340 350 360 AGLVEFSKIS RKLKLDWDGI RKHLDEYASI ASSSKGGRIG IEEFAEYLKL PVSDVLRQLF 370 380 390 400 410 420 ALFDRNNDGS IDFREYVIGL AVLCNPANTE EIIQVAFKLF DVDEDGYITE EEFCTILQAS 430 440 450 460 470 480 LGVPDLNVSG LFREIAQRDS VSYEEFKSFA LKHPEYAKIF TTYLDLQTCH VFSLPEEVQT 490 500 APSVASNKVS PESQEEGTSD KKVD
	Isoform 3 (c) (Aytl1_v3). Checksum: 51FA6EC5F42CC049	FASTA	236	25,486
	10 20 30 40 50 60 MNRCAEAAAV AATVPGSGVG DAGLRPPMVP RQASFFPPPV PNPFVQQTTI SASRRLQMFL 70 80 90 100 110 120 LGIILLPVRA LLVGIILLLA WPFAVISTAC CPEKLTHPIS NWRRKITRPA LTFLARAMFF 130 140 150 160 170 180 SMGFTVTVKG KVASPLEAPI FVVAPHSTFF DGIACVVAGL PSLVSRNENA QTPLVGRLLR 190 200 210 220 230 ALQPVLVSRV DPDSRKNTIN EIKKRATSGG EWPQEPSSQE FQCSPSSSDT QTSWIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:lyso-PAF acetyltransferase." Shindou H., Hishikawa D., Nakanishi H., Harayama T., Ishii S., Taguchi R., Shimizu T. J. Biol. Chem. 282:6532-6539(2007) [PubMed: 17182612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[2]	"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] (ISOFORM 1). Strain: C57BL/6J. Tissue: Spinal cord.
[3]	"Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes." Soupene E., Fyrst H., Kuypers F.A. Proc. Natl. Acad. Sci. U.S.A. 105:88-93(2008) [PubMed: 18156367] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 175-299 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 175-544 (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB244716 mRNA. Translation: BAF47695.1. AK039431 mRNA. Translation: BAC30345.1. EF442783 mRNA. Translation: ABR20912.1. EF442784 mRNA. Translation: ABR20913.1.
IPI	IPI00227121. IPI00886263. IPI00929876.
RefSeq	NP_766602.1.
UniGene	Mm.21463
3D structure databases
HSSP	HSSP built from PDB template 1OZS based on UniProtKB P02590.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BYI6.
Proteomic databases
PRIDE	Q8BYI6.
Genome annotation databases
Ensembl	ENSMUST00000046290; ENSMUSP00000049252; ENSMUSG00000033192; Mus musculus. [Genome view]
GeneID	270084.
KEGG	mmu:270084.
UCSC	uc009mug.1. mouse.
Organism-specific databases
CTD	270084.
MGI	MGI:3606214. Lpcat2.
Phylogenomic databases
HOVERGEN	Q8BYI6.
OMA	TSGGEWP.
Gene expression databases
ArrayExpress	Q8BYI6.
Bgee	Q8BYI6.
CleanEx	MM_LPCAT2.
Genevestigator	Q8BYI6.
GermOnline	ENSMUSG00000033192. Mus musculus.
Family and domain databases
InterPro	IPR002123. Acyltransferase. IPR011992. EF-Hand_type. IPR018248. EF_hand. IPR018247. EF_HAND_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR001125. Recoverin. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
Pfam	PF01553. Acyltransferase. 1 hit. PF00036. efhand. 2 hits. [Graphical view]
PRINTS	PR00450. RECOVERIN.
ProDom	PD000012. EF-hand. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00054. EFh. 2 hits. SM00563. PlsC. 1 hit. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	393188.
SOURCE	Search...

Entry information

Entry name

PCAT2_MOUSE

Accession

Primary (citable) accession number: Q8BYI6
Secondary accession number(s): A3KBM0, A9Q1G2, A9Q1G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)