Reviewed, UniProtKB/Swiss-Prot P0C1Q3 (PCAT2_RAT)

Names and origin

Protein names

Recommended name:
    Lysophosphatidylcholine acyltransferase 2
      Short name=LysoPC 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

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	544 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.

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	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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 544	544	Lysophosphatidylcholine acyltransferase 2		PRO_0000247060
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

Sequences

	Sequence		Length	Mass (Da)
	P0C1Q3-1 [UniParc]. Last modified July 25, 2006. Version 1. Checksum: E729F09ED03A9342	FASTA	544	59,829
	10 20 30 40 50 60 MNRCAEAAAV AATVPGSGVG DSGLRPPMVP RQASFFPPPV PNPFVQQTRI SAARRLQMIL 70 80 90 100 110 120 LGIILLPVRA LLVGLVLLLA WPFAVISTVC CPKKLTHPIS DWRRKITQPA LKFLGRAMFF 130 140 150 160 170 180 SMGFRVTVKG KVASPLEAPI FVVAPHSTFF DGIACVVAGL PSLVSRNENA QTPLVGRLLR 190 200 210 220 230 240 ALQPVLVSRV DPDSRKNTIN EIKKRAMSGG EWPQILVFPE GTCTNRSCLI TFKPGAFIPG 250 260 270 280 290 300 VPVQPVLLRY PNKLDTVTWT WQGYTFIQLC VLTFCQLFTK VEVEFMPVQA PSEEERNDPV 310 320 330 340 350 360 LFASRVRNLM AEALEIPVTD HTYEDCRLMI SAGQLTLPME AGLVEFTKIS RKLKLDWDGI 370 380 390 400 410 420 RKHLDEYASI ASSAKGGRIG ASSAKGGRIG PVSDVLRQLF ALFDRNNDGS IDFREYVIGL 430 440 450 460 470 480 AVLCNPANTE DIIQVAFKLF DVDEDGYITE EEFCTILQAS LGVPDLNVSG LFREIAQGDS 490 500 510 520 530 540 VSYEEFKSFA LKHPEYAKIF TTYLDLQTCH VFSLPEDVQT APSVASNKVS PESHEEGTSG KKVD

References

[1]

"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03113567 Genomic DNA. No translation available. AABR03114401 Genomic DNA. No translation available. AABR03114727 Genomic DNA. No translation available. AABR03115009 Genomic DNA. No translation available. AABR03115067 Genomic DNA. No translation available. AABR03115529 Genomic DNA. No translation available.
IPI	IPI00359383.
3D structure databases
SMR	P0C1Q3. Positions 320-456, 322-491, 353-501.
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000022359; ENSRNOP00000022359; ENSRNOG00000016643; Rattus norvegicus. [Genome view]
Organism-specific databases
RGD	1563994. Lpcat2.
Phylogenomic databases
eggNOG	maNOG09885.
HOVERGEN	P0C1Q3.
InParanoid	P0C1Q3.
PhylomeDB	P0C1Q3.
Gene expression databases
ArrayExpress	P0C1Q3.
Genevestigator	P0C1Q3.
Family and domain databases
InterPro	IPR002123. Acyltransferase. IPR011992. EF-hand-like_dom. 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. [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...

Entry information

Entry name

PCAT2_RAT

Accession

Primary (citable) accession number: P0C1Q3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 25, 2006
Last modified:	February 9, 2010
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)