Reviewed, UniProtKB/Swiss-Prot Q1HAQ0 (PCAT1_RAT)

Names and origin

Protein names

Recommended name:
    Lysophosphatidylcholine acyltransferase 1
      Short name=LysoPC acyltransferase 1
      Short name=LPC acyltransferase 1
      Short name=LPCAT-1
    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 2

Gene names

Name:	Lpcat1
Synonyms:	Aytl2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	534 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology. Ref.1
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	Not activated by inflammatory stimulation. Inhibited by Cu2+ and Fe2+. Activity is not affected by Co2+, Mg2+ or Mn2+ 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.
Tissue specificity	Enriched in alveolar type II cells of lung. Also highly expressed in stomach. Ref.1 Ref.3
Induction	By FGF7. Ref.1
Domain	The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphocholine By similarity. The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins By similarity.
Sequence similarities	Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. Contains 2 EF-hand domains.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Domain	Repeat Signal-anchor Transmembrane
Ligand	Calcium
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Golgi apparatus 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 electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 534	534	Lysophosphatidylcholine acyltransferase 1		PRO_0000247066
Regions
	Topological domain	1 – 57	57	Cytoplasmic Potential
	Transmembrane	58 – 78	21	Signal-anchor for type II membrane protein Potential
	Topological domain	79 – 534	456	Lumenal Potential
	Domain	379 – 414	36	EF-hand 1
	Domain	451 – 486	36	EF-hand 2
	Calcium binding	392 – 403	12	1 Potential
	Motif	135 – 140	6	HXXXXD motif
	Motif	531 – 534	4	Di-lysine motif

Sequences

	Sequence		Length	Mass (Da)
	Q1HAQ0-1 [UniParc]. Last modified July 25, 2006. Version 2. Checksum: 952C0478DC66738A	FASTA	534	59,762
	10 20 30 40 50 60 MRLRGRGPRA APSSSSGAGD ARRLAPPGRN PFVHELRLSA LQKAQVAFMT LTLFPIRLLF 70 80 90 100 110 120 AAFMMLLAWP FALVASLGPP DKEPEQPLAL WRKVVDFLLK AIMRTMWFAG GFHRVAVKGR 130 140 150 160 170 180 QALPTEAAIL TLAPHSSYFD AIPVTMTMSS IVMKAESRDI PIWGTLIRYI RPVFVSRSDQ 190 200 210 220 230 240 DSRRKTVEEI KRRAQSNGKW PQIMIFPEGT CTNRTCLITF KPGAFIPGVP VQPVVLRYPN 250 260 270 280 290 300 KLDTITWTWQ GPGALKILWL TLCQFQNQVE IEFLPVYCPS EEEKRNPALY ASNVRRVMAK 310 320 330 340 350 360 ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPENLEK DLDKYSESAR 370 380 390 400 410 420 MKRGEKIRLP EFAAYLEVPV SDALEDMFSL FDESGGGEID LREYVVALSV VCRPSQTLAT 430 440 450 460 470 480 IQLAFKMYGS PEDGSIDEAD LSCILKTALG ISELTVTDLF QAIDQEERGR ITFDDFCGFA 490 500 510 520 530 EMYPDFAEDY LYPDQTHSDS CAQTPPAPTP NGFCIDFSPE HSDFGRKNSC KKVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells." Chen X., Hyatt B.A., Mucenski M.L., Mason R.J., Shannon J.M. Proc. Natl. Acad. Sci. U.S.A. 103:11724-11729(2006) [PubMed: 16864775] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[2]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed: 15057822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[3]	"Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1): expression in alveolar type II cells and possible involvement in surfactant production." Nakanishi H., Shindou H., Hishikawa D., Harayama T., Ogasawara R., Suwabe A., Taguchi R., Shimizu T. J. Biol. Chem. 281:20140-20147(2006) [PubMed: 16704971] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-534, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AABR03001349 Genomic DNA. No translation available. AABR03001854 Genomic DNA. No translation available. AB244983 mRNA. Translation: BAE94689.2.
IPI	IPI00365394.
RefSeq	NP_001094205.1.
UniGene	Rn.16547
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000024111; ENSRNOP00000024111; ENSRNOG00000017930; Rattus norvegicus. [Genome view]
GeneID	361467.
KEGG	rno:361467.
Organism-specific databases
CTD	361467.
RGD	1311599. Lpcat1.
Phylogenomic databases
HOVERGEN	Q1HAQ0.
Enzyme and pathway databases
BRENDA	2.3.1.23. 248.
Gene expression databases
ArrayExpress	Q1HAQ0.
Genevestigator	Q1HAQ0.
Family and domain databases
InterPro	IPR002123. Acyltransferase. IPR011992. EF-Hand_type. IPR018247. EF_HAND_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
ProDom	PD000012. EF-hand. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00054. EFh. 3 hits. SM00563. PlsC. 1 hit. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	676408.

Entry information

Entry name

PCAT1_RAT

Accession

Primary (citable) accession number: Q1HAQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 25, 2006
Last modified:	October 13, 2009
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)