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Q8NF37

- PCAT1_HUMAN

UniProt

Q8NF37 - PCAT1_HUMAN

Protein

Lysophosphatidylcholine acyltransferase 1

Gene

LPCAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (25 Jul 2006)
      Previous versions | rss
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    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

    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.

    GO - Cellular componenti

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

    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

    ArrayExpressiQ8NF37.
    BgeeiQ8NF37.
    CleanExiHS_LPCAT1.
    GenevestigatoriQ8NF37.

    Organism-specific databases

    HPAiHPA012501.
    HPA022268.

    Interactioni

    Protein-protein interaction databases

    BioGridi122973. 13 interactions.
    IntActiQ8NF37. 4 interactions.
    STRINGi9606.ENSP00000283415.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NF37.
    SMRiQ8NF37. Positions 348-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5757CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini79 – 534456LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei58 – 7821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    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

    MRLRGCGPRA APASSAGASD ARLLAPPGRN PFVHELRLSA LQKAQVALMT    50
    LTLFPVRLLV AAAMMLLAWP LALVASLGSA EKEPEQPPAL WRKVVDFLLK 100
    AIMRTMWFAG GFHRVAVKGR QALPTEAAIL TLAPHSSYFD AIPVTMTMSS 150
    IVMKAESRDI PIWGTLIQYI RPVFVSRSDQ DSRRKTVEEI KRRAQSNGKW 200
    PQIMIFPEGT CTNRTCLITF KPGAFIPGAP VQPVVLRYPN KLDTITWTWQ 250
    GPGALEILWL TLCQFHNQVE IEFLPVYSPS EEEKRNPALY ASNVRRVMAE 300
    ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPEKLEK 350
    DLDRYSERAR MKGGEKIGIA EFAASLEVPV SDLLEDMFSL FDESGSGEVD 400
    LRECVVALSV VCRPARTLDT IQLAFKMYGA QEDGSVGEGD LSCILKTALG 450
    VAELTVTDLF RAIDQEEKGK ITFADFHRFA EMYPAFAEEY LYPDQTHFES 500
    CAETSPAPIP NGFCADFSPE NSDAGRKPVR KKLD 534
    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.
    The sequence BAB14065.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 348-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122973. 13 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.
    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

    ArrayExpressi Q8NF37.
    Bgeei Q8NF37.
    CleanExi HS_LPCAT1.
    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

    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 1, 2014
    This is version 102 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