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Q8NF37

- PCAT1_HUMAN

UniProt

Q8NF37 - PCAT1_HUMAN

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Protein

Lysophosphatidylcholine acyltransferase 1

Gene

LPCAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.1 Publication
Acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine.1 Publication

Enzyme regulationi

Not activated by inflammatory stimulation. Inhibited by Cu2+ and Fe2+. Activity is not affected by Co2+, Mg2+ or Mn2+ (By similarity).By similarity

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi392 – 403121PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. 1-acylglycerophosphocholine O-acyltransferase activity Source: UniProtKB
  2. 1-alkenylglycerophosphocholine O-acyltransferase activity Source: Ensembl
  3. 1-alkylglycerophosphocholine O-acetyltransferase activity Source: UniProtKB-EC
  4. 1-alkylglycerophosphocholine O-acyltransferase activity Source: Ensembl
  5. calcium ion binding Source: InterPro

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. glycerophospholipid biosynthetic process Source: Reactome
  3. negative regulation of phosphatidylcholine biosynthetic process Source: Ensembl
  4. phosphatidic acid biosynthetic process Source: Reactome
  5. phosphatidylcholine acyl-chain remodeling Source: UniProtKB
  6. phosphatidylglycerol acyl-chain remodeling Source: Reactome
  7. phospholipid biosynthetic process Source: UniProtKB
  8. phospholipid metabolic process Source: Reactome
  9. positive regulation of protein catabolic process Source: Ensembl
  10. retina development in camera-type eye Source: Ensembl
  11. small molecule metabolic process Source: Reactome
  12. surfactant homeostasis Source: Ensembl
  13. triglyceride biosynthetic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_1190. Triglyceride Biosynthesis.
REACT_120829. Acyl chain remodelling of PC.
REACT_120906. Synthesis of PA.
REACT_121324. Acyl chain remodelling of PG.
UniPathwayiUPA00085.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophosphatidylcholine acyltransferase 1 (EC:2.3.1.23)
Short name:
LPC acyltransferase 1
Short name:
LPCAT-1
Short name:
LysoPC acyltransferase 1
Alternative name(s):
1-acylglycerophosphocholine O-acyltransferase
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 namesi
Name:LPCAT1
Synonyms:AYTL2, PFAAP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:25718. LPCAT1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Lipid droplet 1 Publication
Note: May adopt a monotopic topology when embedded in the lipid monolayer of the lipid droplet, with both termini exposed to the cytoplasm.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei58 – 7821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini79 – 534456LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: Reactome
  3. Golgi apparatus Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. lipid particle Source: UniProtKB
  6. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Lipid droplet, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162394232.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 534534Lysophosphatidylcholine acyltransferase 1PRO_0000247064Add
BLAST

Proteomic databases

MaxQBiQ8NF37.
PaxDbiQ8NF37.
PeptideAtlasiQ8NF37.
PRIDEiQ8NF37.

PTM databases

PhosphoSiteiQ8NF37.

Expressioni

Gene expression databases

BgeeiQ8NF37.
CleanExiHS_LPCAT1.
ExpressionAtlasiQ8NF37. baseline and differential.
GenevestigatoriQ8NF37.

Organism-specific databases

HPAiHPA012501.
HPA022268.

Interactioni

Protein-protein interaction databases

BioGridi122973. 18 interactions.
IntActiQ8NF37. 4 interactions.
STRINGi9606.ENSP00000283415.

Structurei

3D structure databases

ProteinModelPortaliQ8NF37.
SMRiQ8NF37. Positions 326-485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini379 – 41436EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini451 – 48636EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi135 – 1406HXXXXD motif
Motifi531 – 5344Di-lysine motif

Domaini

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 similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG236173.
GeneTreeiENSGT00390000004914.
HOGENOMiHOG000234374.
HOVERGENiHBG060273.
InParanoidiQ8NF37.
KOiK13510.
OMAiSNVRRVM.
OrthoDBiEOG7NCV5G.
PhylomeDBiQ8NF37.
TreeFamiTF323244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 2 hits.
SM00563. PlsC. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NF37-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLRGCGPRA APASSAGASD ARLLAPPGRN PFVHELRLSA LQKAQVALMT
60 70 80 90 100
LTLFPVRLLV AAAMMLLAWP LALVASLGSA EKEPEQPPAL WRKVVDFLLK
110 120 130 140 150
AIMRTMWFAG GFHRVAVKGR QALPTEAAIL TLAPHSSYFD AIPVTMTMSS
160 170 180 190 200
IVMKAESRDI PIWGTLIQYI RPVFVSRSDQ DSRRKTVEEI KRRAQSNGKW
210 220 230 240 250
PQIMIFPEGT CTNRTCLITF KPGAFIPGAP VQPVVLRYPN KLDTITWTWQ
260 270 280 290 300
GPGALEILWL TLCQFHNQVE IEFLPVYSPS EEEKRNPALY ASNVRRVMAE
310 320 330 340 350
ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPEKLEK
360 370 380 390 400
DLDRYSERAR MKGGEKIGIA EFAASLEVPV SDLLEDMFSL FDESGSGEVD
410 420 430 440 450
LRECVVALSV VCRPARTLDT IQLAFKMYGA QEDGSVGEGD LSCILKTALG
460 470 480 490 500
VAELTVTDLF RAIDQEEKGK ITFADFHRFA EMYPAFAEEY LYPDQTHFES
510 520 530
CAETSPAPIP NGFCADFSPE NSDAGRKPVR KKLD
Length:534
Mass (Da):59,151
Last modified:July 25, 2006 - v2
Checksum:i69A9C3AEC698F6BD
GO

Sequence cautioni

The sequence BAB14061.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB14065.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3864.1.
RefSeqiNP_079106.3. NM_024830.3.
UniGeneiHs.368853.

Genome annotation databases

EnsembliENST00000283415; ENSP00000283415; ENSG00000153395.
ENST00000475622; ENSP00000423472; ENSG00000153395.
GeneIDi79888.
KEGGihsa:79888.
UCSCiuc003jcm.3. human.

Polymorphism databases

DMDMi110815902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS3864.1.
RefSeqi NP_079106.3. NM_024830.3.
UniGenei Hs.368853.

3D structure databases

ProteinModelPortali Q8NF37.
SMRi Q8NF37. Positions 326-485.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122973. 18 interactions.
IntActi Q8NF37. 4 interactions.
STRINGi 9606.ENSP00000283415.

PTM databases

PhosphoSitei Q8NF37.

Polymorphism databases

DMDMi 110815902.

Proteomic databases

MaxQBi Q8NF37.
PaxDbi Q8NF37.
PeptideAtlasi Q8NF37.
PRIDEi Q8NF37.

Protocols and materials databases

DNASUi 79888.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000283415 ; ENSP00000283415 ; ENSG00000153395 .
ENST00000475622 ; ENSP00000423472 ; ENSG00000153395 .
GeneIDi 79888.
KEGGi hsa:79888.
UCSCi uc003jcm.3. human.

Organism-specific databases

CTDi 79888.
GeneCardsi GC05M001516.
HGNCi HGNC:25718. LPCAT1.
HPAi HPA012501.
HPA022268.
MIMi 610472. gene.
neXtProti NX_Q8NF37.
PharmGKBi PA162394232.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG236173.
GeneTreei ENSGT00390000004914.
HOGENOMi HOG000234374.
HOVERGENi HBG060273.
InParanoidi Q8NF37.
KOi K13510.
OMAi SNVRRVM.
OrthoDBi EOG7NCV5G.
PhylomeDBi Q8NF37.
TreeFami TF323244.

Enzyme and pathway databases

UniPathwayi UPA00085 .
Reactomei REACT_1190. Triglyceride Biosynthesis.
REACT_120829. Acyl chain remodelling of PC.
REACT_120906. Synthesis of PA.
REACT_121324. Acyl chain remodelling of PG.

Miscellaneous databases

ChiTaRSi LPCAT1. human.
GenomeRNAii 79888.
NextBioi 69702.
PROi Q8NF37.
SOURCEi Search...

Gene expression databases

Bgeei Q8NF37.
CleanExi HS_LPCAT1.
ExpressionAtlasi Q8NF37. baseline and differential.
Genevestigatori Q8NF37.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view ]
Pfami PF01553. Acyltransferase. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 2 hits.
SM00563. PlsC. 1 hit.
[Graphical view ]
PROSITEi PS50222. EF_HAND_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Human lysophosphatidylcholine acyltransferases 1 and 2 are located in lipid droplets where they catalyze the formation of phosphatidylcholine."
    Moessinger C., Kuerschner L., Spandl J., Shevchenko A., Thiele C.
    J. Biol. Chem. 286:21330-21339(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY.

Entry informationi

Entry nameiPCAT1_HUMAN
AccessioniPrimary (citable) accession number: Q8NF37
Secondary accession number(s): Q1HAQ1
, Q7Z4G6, Q8N3U7, Q8WUL8, Q9GZW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: October 29, 2014
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3