Q8NF37 (PCAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysophosphatidylcholine acyltransferase 1
Short name=LPC acyltransferase 1
Short name=LPCAT-1
Short name=LysoPC acyltransferase 1
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 2
Phosphonoformate immuno-associated protein 3

Gene names

Name:	LPCAT1
Synonyms:	AYTL2, PFAAP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	534 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.7
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.
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.
Sequence caution	The sequence BAB14061.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB14065.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Domain	Repeat Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of phosphatidylcholine biosynthetic process Inferred from electronic annotation. Source: Compara phosphatidic acid biosynthetic process Traceable author statement. Source: Reactome phosphatidylcholine acyl-chain remodeling Traceable author statement. Source: Reactome phosphatidylglycerol acyl-chain remodeling Traceable author statement. Source: Reactome positive regulation of protein catabolic process Inferred from electronic annotation. Source: Compara retina development in camera-type eye Inferred from electronic annotation. Source: Compara surfactant homeostasis Inferred from electronic annotation. Source: Compara triglyceride biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro
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_0000247064
Regions
	Topological domain	1 – 57	57	Cytoplasmic Potential
	Transmembrane	58 – 78	21	Helical; 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)
	Q8NF37 [UniParc]. Last modified July 25, 2006. Version 2. Checksum: 69A9C3AEC698F6BD	FASTA	534	59,151
	10 20 30 40 50 60 MRLRGCGPRA APASSAGASD ARLLAPPGRN PFVHELRLSA LQKAQVALMT LTLFPVRLLV 70 80 90 100 110 120 AAAMMLLAWP LALVASLGSA EKEPEQPPAL WRKVVDFLLK AIMRTMWFAG GFHRVAVKGR 130 140 150 160 170 180 QALPTEAAIL TLAPHSSYFD AIPVTMTMSS IVMKAESRDI PIWGTLIQYI RPVFVSRSDQ 190 200 210 220 230 240 DSRRKTVEEI KRRAQSNGKW PQIMIFPEGT CTNRTCLITF KPGAFIPGAP VQPVVLRYPN 250 260 270 280 290 300 KLDTITWTWQ GPGALEILWL TLCQFHNQVE IEFLPVYSPS EEEKRNPALY ASNVRRVMAE 310 320 330 340 350 360 ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPEKLEK DLDRYSERAR 370 380 390 400 410 420 MKGGEKIGIA EFAASLEVPV SDLLEDMFSL FDESGSGEVD LRECVVALSV VCRPARTLDT 430 440 450 460 470 480 IQLAFKMYGA QEDGSVGEGD LSCILKTALG VAELTVTDLF RAIDQEEKGK ITFADFHRFA 490 500 510 520 530 EMYPAFAEEY LYPDQTHFES CAETSPAPIP NGFCADFSPE NSDAGRKPVR KKLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones." Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O. DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-534. Tissue: Spleen.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-534. Tissue: Eye.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-534. Tissue: Teratocarcinoma.
[5]	"Screening and cloning of a new immuno-associated gene regulated by phosphonoformate." Liu Y., Cheng J., Lu Y. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 298-534.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-534. Tissue: Amygdala.
[7]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, FUNCTION.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB244719 mRNA. Translation: BAE94688.1. AK090444 mRNA. Translation: BAC03425.1. BC020166 mRNA. Translation: AAH20166.3. AK022505 mRNA. Translation: BAB14065.1. Different initiation. AK022499 mRNA. Translation: BAB14061.1. Different initiation. AF530061 mRNA. Translation: AAQ09945.1. AL831864 mRNA. Translation: CAD38556.1.
IPI	IPI00171626.
RefSeq	NP_079106.3. NM_024830.3.
UniGene	Hs.368853.
3D structure databases
ProteinModelPortal	Q8NF37.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NF37. 3 interactions.
STRING	9606.ENSP00000283415.
PTM databases
PhosphoSite	Q8NF37.
Polymorphism databases
DMDM	110815902.
Proteomic databases
PaxDb	Q8NF37.
PeptideAtlas	Q8NF37.
PRIDE	Q8NF37.
Protocols and materials databases
DNASU	79888.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000283415; ENSP00000283415; ENSG00000153395. ENST00000475622; ENSP00000423472; ENSG00000153395.
GeneID	79888.
KEGG	hsa:79888.
UCSC	uc003jcm.3. human.
Organism-specific databases
CTD	79888.
GeneCards	GC05M001516.
HGNC	HGNC:25718. LPCAT1.
HPA	HPA012501. HPA022268.
MIM	610472. gene.
neXtProt	NX_Q8NF37.
PharmGKB	PA162394232.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG236173.
HOGENOM	HOG000234374.
HOVERGEN	HBG060273.
InParanoid	Q8NF37.
KO	K13510.
OMA	LAFKMYG.
PhylomeDB	Q8NF37.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00085.
Gene expression databases
ArrayExpress	Q8NF37.
Bgee	Q8NF37.
CleanEx	HS_LPCAT1.
Genevestigator	Q8NF37.
GermOnline	ENSG00000153395. Homo sapiens.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR011992. EF-hand-like_dom. IPR002048. EF_hand_dom. IPR002123. Plipid/glycerol_acylTrfase. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. PF13405. EF_hand_4. 1 hit. [Graphical view]
SMART	SM00054. EFh. 2 hits. SM00563. PlsC. 1 hit. [Graphical view]
PROSITE	PS00018. EF_HAND_1. False negative. PS50222. EF_HAND_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LPCAT1. human.
GenomeRNAi	79888.
NextBio	69702.
SOURCE	Search...

Entry information

Entry name

PCAT1_HUMAN

Accession

Primary (citable) accession number: Q8NF37
Secondary accession number(s): Q1HAQ1 , Q7Z4G6, Q8N3U7, Q8WUL8, Q9GZW6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	July 25, 2006
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.