Reviewed, UniProtKB/Swiss-Prot Q7L5N7 (PCAT2_HUMAN)

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

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	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 By similarity.
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 By similarity.
Pathway	Lipid metabolism; phospholipid metabolism.
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity. Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
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.
Sequence caution	The sequence BAA91199.1 differs from that shown. Reason: Frameshift at position 44. The sequence CAE46034.1 differs from that shown. Reason: Frameshift at position 295.

Ontologies

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q7L5N7-1)

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: Q7L5N7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-270: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 544	544	Lysophosphatidylcholine acyltransferase 2		PRO_0000247058
Regions
	Topological domain	1 – 57	57	Cytoplasmic Potential
	Transmembrane	58 – 78	21	Signal-anchor for type II membrane protein Potential
	Topological domain	79 – 544	466	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	1 – 270	270	Missing in isoform 2.		VSP_019912
	Natural variant	163	1	M → I: dbSNP rs837550.		VAR_027058

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: B823D86272A739C0	FASTA	544	60,208
	10 20 30 40 50 60 MSRCAQAAEV AATVPGAGVG NVGLRPPMVP RQASFFPPPV PNPFVQQTQI GSARRVQIVL 70 80 90 100 110 120 LGIILLPIRV LLVALILLLA WPFAAISTVC CPEKLTHPIT GWRRKITQTA LKFLGRAMFF 130 140 150 160 170 180 SMGFIVAVKG KIASPLEAPV FVAAPHSTFF DGIACVVAGL PSMVSRNENA QVPLIGRLLR 190 200 210 220 230 240 AVQPVLVSRV DPDSRKNTIN EIIKRTTSGG EWPQILVFPE GTCTNRSCLI TFKPGAFIPG 250 260 270 280 290 300 VPVQPVLLRY PNKLDTVTWT WQGYTFIQLC MLTFCQLFTK VEVEFMPVQV PNDEEKNDPV 310 320 330 340 350 360 LFANKVRNLM AEALGIPVTD HTYEDCRLMI SAGQLTLPME AGLVEFTKIS RKLKLDWDGV 370 380 390 400 410 420 RKHLDEYASI ASSSKGGRIG IEEFAKYLKL PVSDVLRQLF ALFDRNHDGS IDFREYVIGL 430 440 450 460 470 480 AVLCNPSNTE EIIQVAFKLF DVDEDGYITE EEFSTILQAS LGVPDLDVSG LFKEIAQGDS 490 500 510 520 530 540 ISYEEFKSFA LKHPEYAKIF TTYLDLQTCH VFSLPKEVQT TPSTASNKVS PEKHEESTSD KKDD
	Isoform 2. Checksum: 1B7DE26E0D7791EA	FASTA	274	30,895
	10 20 30 40 50 60 MLTFCQLFTK VEVEFMPVQV PNDEEKNDPV LFANKVRNLM AEALGIPVTD HTYEDCRLMI 70 80 90 100 110 120 SAGQLTLPME AGLVEFTKIS RKLKLDWDGV RKHLDEYASI ASSSKGGRIG IEEFAKYLKL 130 140 150 160 170 180 PVSDVLRQLF ALFDRNHDGS IDFREYVIGL AVLCNPSNTE EIIQVAFKLF DVDEDGYITE 190 200 210 220 230 240 EEFSTILQAS LGVPDLDVSG LFKEIAQGDS ISYEEFKSFA LKHPEYAKIF TTYLDLQTCH 250 260 270 VFSLPKEVQT TPSTASNKVS PEKHEESTSD KKDD

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).
[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] (ISOFORM 1). Tissue: Carcinoma.
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Fetal kidney.
[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 1). Tissue: Kidney.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB244718 mRNA. Translation: BAF47696.1. AK000488 mRNA. Translation: BAA91199.1. Frameshift. BX641069 mRNA. Translation: CAE46034.1. Frameshift. BC002472 mRNA. Translation: AAH02472.2.
IPI	IPI00016418. IPI00643943.
RefSeq	NP_060309.2.
UniGene	Hs.460857
3D structure databases
ModBase	Search...
Proteomic databases
PeptideAtlas	Q7L5N7.
PRIDE	Q7L5N7.
Genome annotation databases
Ensembl	ENST00000262134; ENSP00000262134; ENSG00000087253; Homo sapiens. [Genome view]
GeneID	54947.
KEGG	hsa:54947.
UCSC	uc002eib.1. human. uc002eic.1. human.
Organism-specific databases
CTD	54947.
GeneCards	GC16P054102.
HGNC	HGNC:26032. LPCAT2.
HPA	HPA007891.
MIM	612040. gene.
PharmGKB	PA142672566.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q7L5N7.
HOVERGEN	Q7L5N7.
OMA	TSGGEWP.
Gene expression databases
ArrayExpress	Q7L5N7.
Bgee	Q7L5N7.
CleanEx	HS_LPCAT2.
Genevestigator	Q7L5N7.
GermOnline	ENSG00000087253. Homo sapiens.
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.
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	58111.
SOURCE	Search...

Entry information

Entry name

PCAT2_HUMAN

Accession

Primary (citable) accession number: Q7L5N7
Secondary accession number(s): A3KBM1, Q6MZJ6, Q9NX23

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 51 of the entry and version 1 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.