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P0C1Q3 (PCAT2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysophosphatidylcholine acyltransferase 2
Short name=LPC acyltransferase 2
Short name=LPCAT-2
Short name=LysoPC acyltransferase 2
EC=2.3.1.-
Alternative name(s):
1-acylglycerophosphocholine O-acyltransferase
EC=2.3.1.23
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
Acyltransferase-like 1
Gene names
Name:Lpcat2
Synonyms:Aytl1, Aytl1a, Lpcat2a
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 544544Lysophosphatidylcholine acyltransferase 2
PRO_0000247060

Regions

Topological domain1 – 5858Cytoplasmic Potential
Transmembrane59 – 7921Helical; Signal-anchor for type II membrane protein; Potential
Topological domain80 – 544465Lumenal Potential
Domain391 – 42636EF-hand 1
Domain428 – 46336EF-hand 2
Calcium binding404 – 415121 Potential
Calcium binding441 – 452122 Potential
Motif146 – 1516HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
P0C1Q3 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: E729F09ED03A9342

FASTA54459,829
        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

« Hide

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. expand/collapse author list , 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.
IPIIPI00359383.

3D structure databases

ProteinModelPortalP0C1Q3.
ModBaseSearch...

Protein-protein interaction databases

STRINGP0C1Q3.

Proteomic databases

PRIDEP0C1Q3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD1563994. Lpcat2.

Phylogenomic databases

eggNOGmaNOG09885.
GeneTreeENSGT00390000004914.
InParanoidP0C1Q3.
OrthoDBEOG4VDPZF.
PhylomeDBP0C1Q3.

Gene expression databases

ArrayExpressP0C1Q3.
GenevestigatorP0C1Q3.

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR018248. EF-hand.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
IPR001125. Recoverin.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
PfamPF01553. Acyltransferase. 1 hit.
PF00036. efhand. 1 hit.
[Graphical view]
PRINTSPR00450. RECOVERIN.
SMARTSM00054. EFh. 2 hits.
SM00563. PlsC. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePCAT2_RAT
AccessionPrimary (citable) accession number: P0C1Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: September 21, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents