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Q7L5N7 (PCAT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 544544Lysophosphatidylcholine acyltransferase 2
PRO_0000247058

Regions

Topological domain1 – 5757Cytoplasmic Potential
Transmembrane58 – 7821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain79 – 544466Lumenal Potential
Domain391 – 42636EF-hand 1
Domain428 – 46336EF-hand 2
Calcium binding404 – 415121 Potential
Calcium binding441 – 452122 Potential
Motif146 – 1516HXXXXD motif

Natural variations

Alternative sequence1 – 270270Missing in isoform 2.
VSP_019912
Natural variant1631M → I.
Corresponds to variant rs837550 [ dbSNP | Ensembl ].
VAR_027058

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B823D86272A739C0

FASTA54460,208
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 1B7DE26E0D7791EA
Show »

FASTA27430,895

References

« Hide '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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB244718 mRNA. Translation: BAF47696.1.
AK000488 mRNA. Translation: BAA91199.1. Frameshift.
BX641069 mRNA. Translation: CAE46034.1. Frameshift.
BC002472 mRNA. Translation: AAH02472.2.
IPIIPI00016418.
IPI00643943.
RefSeqNP_060309.2. NM_017839.4.
UniGeneHs.460857.

3D structure databases

ProteinModelPortalQ7L5N7.
SMRQ7L5N7. Positions 343-501.
ModBaseSearch...

Protein-protein interaction databases

IntActQ7L5N7. 1 interaction.
STRINGQ7L5N7.

PTM databases

PhosphoSiteQ7L5N7.

Polymorphism databases

DMDM74738601.

Proteomic databases

PeptideAtlasQ7L5N7.
PRIDEQ7L5N7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262134; ENSP00000262134; ENSG00000087253.
GeneID54947.
KEGGhsa:54947.
UCSCuc002eib.1. human.
uc002eic.1. human.

Organism-specific databases

CTD54947.
GeneCardsGC16P055542.
H-InvDBHIX0202246.
HGNCHGNC:26032. LPCAT2.
HPAHPA007891.
MIM612040. gene.
neXtProtNX_Q7L5N7.
PharmGKBPA162394265.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18039.
GeneTreeENSGT00390000004914.
HOGENOMHBG446767.
HOVERGENHBG060273.
InParanoidQ7L5N7.
OMATSGGEWP.
OrthoDBEOG4VDPZF.
PhylomeDBQ7L5N7.

Gene expression databases

ArrayExpressQ7L5N7.
BgeeQ7L5N7.
CleanExHS_LPCAT2.
GenevestigatorQ7L5N7.
GermOnlineENSG00000087253. Homo sapiens.

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.
KOK13510.
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...

Other

NextBio58111.
SOURCESearch...

Entry information

Entry namePCAT2_HUMAN
AccessionPrimary (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: January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families