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Protein

Lysophospholipid acyltransferase LPCAT4

Gene

LPCAT4

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

Functioni

Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors.1 Publication

Catalytic activityi

Acyl-CoA + 1-acyl-sn-glycero-3-phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-phosphoethanolamine.1 Publication
Acyl-CoA + 1-alkenylglycerophosphoethanolamine = CoA + 1-alkenyl-2-acylglycerophosphoethanolamine.1 Publication
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
Acyl-CoA + 1-acyl-sn-glycero-3-phosphatidylserine = CoA + 1,2-diacyl-sn-glycero-3-phosphatidylserine.1 Publication

Kineticsi

  1. KM=80 µM for lysophosphatidylethanolamine1 Publication
  2. KM=20 µM for oleoyl-CoA1 Publication
  1. Vmax=270 pmol/min/mg enzyme with lysophosphatidylethanolamine and oleoyl-CoA as substrates1 Publication

Pathwayi: phospholipid metabolism

This protein is involved in the pathway phospholipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phospholipid metabolism and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDAi2.3.1.23. 2681.
2.3.1.51. 2681.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482925. Acyl chain remodelling of PG.
R-HSA-1483166. Synthesis of PA.
R-HSA-75109. Triglyceride Biosynthesis.
UniPathwayiUPA00085.

Chemistry

SwissLipidsiSLP:000000294.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysophospholipid acyltransferase LPCAT4
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 7
Short name:
1-AGP acyltransferase 7
Short name:
1-AGPAT 7
1-acylglycerophosphocholine O-acyltransferase (EC:2.3.1.23)
1-acylglycerophosphoserine O-acyltransferase (EC:2.3.1.n6)
1-alkenylglycerophosphoethanolamine O-acyltransferase (EC:2.3.1.121)
1-alkylglycerophosphocholine O-acetyltransferase (EC:2.3.1.67)
Acyltransferase-like 3
Lysophosphatidylcholine acyltransferase 4
Lysophosphatidylethanolamine acyltransferase 2 (EC:2.3.1.n7)
Plasmalogen synthase
Gene namesi
Name:LPCAT4
Synonyms:AGPAT7, AYTL3, LPEAT2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:30059. LPCAT4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei40 – 6223HelicalSequence analysisAdd
BLAST
Transmembranei87 – 10721HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162394297.

Polymorphism and mutation databases

BioMutaiLPCAT4.
DMDMi74736281.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524Lysophospholipid acyltransferase LPCAT4PRO_0000247054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ643R3.
MaxQBiQ643R3.
PaxDbiQ643R3.
PRIDEiQ643R3.

PTM databases

iPTMnetiQ643R3.
PhosphoSiteiQ643R3.
SwissPalmiQ643R3.

Expressioni

Tissue specificityi

Widely expressed with predominant level in brain.2 Publications

Gene expression databases

BgeeiQ643R3.
CleanExiHS_LPCAT4.
ExpressionAtlasiQ643R3. baseline and differential.
GenevisibleiQ643R3. HS.

Organism-specific databases

HPAiHPA030719.

Interactioni

Protein-protein interaction databases

BioGridi129039. 10 interactions.
STRINGi9606.ENSP00000317300.

Structurei

3D structure databases

ProteinModelPortaliQ643R3.
SMRiQ643R3. Positions 369-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi129 – 1346HXXXXD motif

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4666. Eukaryota.
ENOG410XSIQ. LUCA.
GeneTreeiENSGT00390000004914.
HOGENOMiHOG000234374.
InParanoidiQ643R3.
KOiK13512.
OMAiLRPPHTS.
OrthoDBiEOG7NCV5G.
PhylomeDBiQ643R3.
TreeFamiTF323244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q643R3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQGSPGDWA PLDPTPGPPA SPNPFVHELH LSRLQRVKFC LLGALLAPIR
60 70 80 90 100
VLLAFIVLFL LWPFAWLQVA GLSEEQLQEP ITGWRKTVCH NGVLGLSRLL
110 120 130 140 150
FFLLGFLRIR VRGQRASRLQ APVLVAAPHS TFFDPIVLLP CDLPKVVSRA
160 170 180 190 200
ENLSVPVIGA LLRFNQAILV SRHDPASRRR VVEEVRRRAT SGGKWPQVLF
210 220 230 240 250
FPEGTCSNKK ALLKFKPGAF IAGVPVQPVL IRYPNSLDTT SWAWRGPGVL
260 270 280 290 300
KVLWLTASQP CSIVDVEFLP VYHPSPEESR DPTLYANNVQ RVMAQALGIP
310 320 330 340 350
ATECEFVGSL PVIVVGRLKV ALEPQLWELG KVLRKAGLSA GYVDAGAEPG
360 370 380 390 400
RSRMISQEEF ARQLQLSDPQ TVAGAFGYFQ QDTKGLVDFR DVALALAALD
410 420 430 440 450
GGRSLEELTR LAFELFAEEQ AEGPNRLLYK DGFSTILHLL LGSPHPAATA
460 470 480 490 500
LHAELCQAGS SQGLSLCQFQ NFSLHDPLYG KLFSTYLRPP HTSRGTSQTP
510 520
NASSPGNPTA LANGTVQAPK QKGD
Length:524
Mass (Da):57,219
Last modified:October 25, 2004 - v1
Checksum:i3A2A12656E1241BC
GO

Sequence cautioni

The sequence AAC19156.1 differs from that shown.Probable cloning artifact.Curated
The sequence AAC19156.1 differs from that shown. Reason: Frameshift at position 328. Curated
The sequence AAN33178.1 differs from that shown. Reason: Frameshift at position 198. Curated
The sequence AAP97722.1 differs from that shown. Reason: Frameshift at positions 188 and 198. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY734233 mRNA. Translation: AAU34184.1.
AF529233 mRNA. Translation: AAP97722.1. Frameshift.
AF542964 mRNA. Translation: AAN33178.1. Frameshift.
AK290273 mRNA. Translation: BAF82962.1.
CH471125 Genomic DNA. Translation: EAW92306.1.
BC024892 mRNA. Translation: AAH24892.2.
BC092463 mRNA. Translation: AAH92463.1.
AF007155 mRNA. Translation: AAC19156.1. Sequence problems.
CCDSiCCDS32191.1.
RefSeqiNP_705841.2. NM_153613.2.
UniGeneiHs.352614.

Genome annotation databases

EnsembliENST00000314891; ENSP00000317300; ENSG00000176454.
GeneIDi254531.
KEGGihsa:254531.
UCSCiuc001zig.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY734233 mRNA. Translation: AAU34184.1.
AF529233 mRNA. Translation: AAP97722.1. Frameshift.
AF542964 mRNA. Translation: AAN33178.1. Frameshift.
AK290273 mRNA. Translation: BAF82962.1.
CH471125 Genomic DNA. Translation: EAW92306.1.
BC024892 mRNA. Translation: AAH24892.2.
BC092463 mRNA. Translation: AAH92463.1.
AF007155 mRNA. Translation: AAC19156.1. Sequence problems.
CCDSiCCDS32191.1.
RefSeqiNP_705841.2. NM_153613.2.
UniGeneiHs.352614.

3D structure databases

ProteinModelPortaliQ643R3.
SMRiQ643R3. Positions 369-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129039. 10 interactions.
STRINGi9606.ENSP00000317300.

Chemistry

SwissLipidsiSLP:000000294.

PTM databases

iPTMnetiQ643R3.
PhosphoSiteiQ643R3.
SwissPalmiQ643R3.

Polymorphism and mutation databases

BioMutaiLPCAT4.
DMDMi74736281.

Proteomic databases

EPDiQ643R3.
MaxQBiQ643R3.
PaxDbiQ643R3.
PRIDEiQ643R3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314891; ENSP00000317300; ENSG00000176454.
GeneIDi254531.
KEGGihsa:254531.
UCSCiuc001zig.4. human.

Organism-specific databases

CTDi254531.
GeneCardsiLPCAT4.
HGNCiHGNC:30059. LPCAT4.
HPAiHPA030719.
MIMi612039. gene.
neXtProtiNX_Q643R3.
PharmGKBiPA162394297.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4666. Eukaryota.
ENOG410XSIQ. LUCA.
GeneTreeiENSGT00390000004914.
HOGENOMiHOG000234374.
InParanoidiQ643R3.
KOiK13512.
OMAiLRPPHTS.
OrthoDBiEOG7NCV5G.
PhylomeDBiQ643R3.
TreeFamiTF323244.

Enzyme and pathway databases

UniPathwayiUPA00085.
BRENDAi2.3.1.23. 2681.
2.3.1.51. 2681.
ReactomeiR-HSA-1482788. Acyl chain remodelling of PC.
R-HSA-1482801. Acyl chain remodelling of PS.
R-HSA-1482839. Acyl chain remodelling of PE.
R-HSA-1482925. Acyl chain remodelling of PG.
R-HSA-1483166. Synthesis of PA.
R-HSA-75109. Triglyceride Biosynthesis.

Miscellaneous databases

GenomeRNAii254531.
NextBioi92364.
PROiQ643R3.
SOURCEiSearch...

Gene expression databases

BgeeiQ643R3.
CleanExiHS_LPCAT4.
ExpressionAtlasiQ643R3. baseline and differential.
GenevisibleiQ643R3. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization a novel human 1-acyl-sn-glycerol-3-phosphate acyltransferase gene AGPAT7."
    Ye G.-M., Chen C., Huang S., Han D.-D., Guo J.-H., Wan B., Yu L.
    DNA Seq. 16:386-390(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  2. Guo J.H., Yu L.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  3. "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].
    Tissue: Colon.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Placenta.
  6. Yu W., Sarginson J., Gibbs R.A.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 268-414.
    Tissue: Brain.
  7. "Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2."
    Cao J., Shan D., Revett T., Li D., Wu L., Liu W., Tobin J.F., Gimeno R.E.
    J. Biol. Chem. 283:19049-19057(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLPCT4_HUMAN
AccessioniPrimary (citable) accession number: Q643R3
Secondary accession number(s): A8K2K8
, O43412, Q7Z4P4, Q8IUL7, Q8TB38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: October 25, 2004
Last modified: March 16, 2016
This is version 119 of the entry and version 1 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 15
    Human chromosome 15: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.