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Q9NRZ5

- PLCD_HUMAN

UniProt

Q9NRZ5 - PLCD_HUMAN

Protein

1-acyl-sn-glycerol-3-phosphate acyltransferase delta

Gene

AGPAT4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone.By similarity

    Catalytic activityi

    Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

    Pathwayi

    GO - Molecular functioni

    1. 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
    2. cellular lipid metabolic process Source: Reactome
    3. glycerophospholipid biosynthetic process Source: Reactome
    4. phosphatidic acid biosynthetic process Source: Reactome
    5. phospholipid biosynthetic process Source: UniProtKB
    6. phospholipid metabolic process Source: Reactome
    7. small molecule metabolic process Source: Reactome
    8. triglyceride biosynthetic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00452-MONOMER.
    ReactomeiREACT_1190. Triglyceride Biosynthesis.
    REACT_120906. Synthesis of PA.
    UniPathwayiUPA00557; UER00613.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-acyl-sn-glycerol-3-phosphate acyltransferase delta (EC:2.3.1.51)
    Alternative name(s):
    1-acylglycerol-3-phosphate O-acyltransferase 4
    Short name:
    1-AGP acyltransferase 4
    Short name:
    1-AGPAT 4
    Lysophosphatidic acid acyltransferase delta
    Short name:
    LPAAT-delta
    Gene namesi
    Name:AGPAT4
    ORF Names:UNQ499/PRO1016
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:20885. AGPAT4.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134961047.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3783781-acyl-sn-glycerol-3-phosphate acyltransferase deltaPRO_0000208197Add
    BLAST

    Proteomic databases

    MaxQBiQ9NRZ5.
    PaxDbiQ9NRZ5.
    PRIDEiQ9NRZ5.

    PTM databases

    PhosphoSiteiQ9NRZ5.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels in skeletal muscle, followed by heart, liver, prostate and thymus.1 Publication

    Gene expression databases

    ArrayExpressiQ9NRZ5.
    BgeeiQ9NRZ5.
    CleanExiHS_AGPAT4.
    GenevestigatoriQ9NRZ5.

    Organism-specific databases

    HPAiHPA053287.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CRKP461081EBI-1754287,EBI-886

    Protein-protein interaction databases

    BioGridi121225. 1 interaction.
    IntActiQ9NRZ5. 1 interaction.
    STRINGi9606.ENSP00000314036.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NRZ5.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei125 – 14521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei307 – 32721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei338 – 35821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi96 – 1016HXXXXD motif

    Domaini

    The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0204.
    HOGENOMiHOG000006110.
    HOVERGENiHBG008205.
    InParanoidiQ9NRZ5.
    KOiK13523.
    OMAiPEKYFFL.
    OrthoDBiEOG7H7928.
    PhylomeDBiQ9NRZ5.
    TreeFamiTF314065.

    Family and domain databases

    InterProiIPR002123. Plipid/glycerol_acylTrfase.
    [Graphical view]
    PfamiPF01553. Acyltransferase. 1 hit.
    [Graphical view]
    SMARTiSM00563. PlsC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NRZ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLAGLLKSQ FLCHLVFCYV FIASGLIINT IQLFTLLLWP INKQLFRKIN    50
    CRLSYCISSQ LVMLLEWWSG TECTIFTDPR AYLKYGKENA IVVLNHKFEI 100
    DFLCGWSLSE RFGLLGGSKV LAKKELAYVP IIGWMWYFTE MVFCSRKWEQ 150
    DRKTVATSLQ HLRDYPEKYF FLIHCEGTRF TEKKHEISMQ VARAKGLPRL 200
    KHHLLPRTKG FAITVRSLRN VVSAVYDCTL NFRNNENPTL LGVLNGKKYH 250
    ADLYVRRIPL EDIPEDDDEC SAWLHKLYQE KDAFQEEYYR TGTFPETPMV 300
    PPRRPWTLVN WLFWASLVLY PFFQFLVSMI RSGSSLTLAS FILVFFVASV 350
    GVRWMIGVTE IDKGSAYGNS DSKQKLND 378
    Length:378
    Mass (Da):44,021
    Last modified:October 1, 2000 - v1
    Checksum:i3EFC13D196F8CDC5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF156776 mRNA. Translation: AAF80338.1.
    AY358506 mRNA. Translation: AAQ88870.1.
    AL109942 Genomic DNA. Translation: CAI21478.1.
    BC020209 mRNA. Translation: AAH20209.1.
    CCDSiCCDS5280.1.
    RefSeqiNP_064518.1. NM_020133.2.
    XP_006715575.1. XM_006715512.1.
    XP_006715576.1. XM_006715513.1.
    UniGeneiHs.353175.

    Genome annotation databases

    EnsembliENST00000320285; ENSP00000314036; ENSG00000026652.
    GeneIDi56895.
    KEGGihsa:56895.
    UCSCiuc003qtr.1. human.

    Polymorphism databases

    DMDMi12230468.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF156776 mRNA. Translation: AAF80338.1 .
    AY358506 mRNA. Translation: AAQ88870.1 .
    AL109942 Genomic DNA. Translation: CAI21478.1 .
    BC020209 mRNA. Translation: AAH20209.1 .
    CCDSi CCDS5280.1.
    RefSeqi NP_064518.1. NM_020133.2.
    XP_006715575.1. XM_006715512.1.
    XP_006715576.1. XM_006715513.1.
    UniGenei Hs.353175.

    3D structure databases

    ProteinModelPortali Q9NRZ5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121225. 1 interaction.
    IntActi Q9NRZ5. 1 interaction.
    STRINGi 9606.ENSP00000314036.

    PTM databases

    PhosphoSitei Q9NRZ5.

    Polymorphism databases

    DMDMi 12230468.

    Proteomic databases

    MaxQBi Q9NRZ5.
    PaxDbi Q9NRZ5.
    PRIDEi Q9NRZ5.

    Protocols and materials databases

    DNASUi 56895.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320285 ; ENSP00000314036 ; ENSG00000026652 .
    GeneIDi 56895.
    KEGGi hsa:56895.
    UCSCi uc003qtr.1. human.

    Organism-specific databases

    CTDi 56895.
    GeneCardsi GC06M161471.
    HGNCi HGNC:20885. AGPAT4.
    HPAi HPA053287.
    MIMi 614795. gene.
    neXtProti NX_Q9NRZ5.
    PharmGKBi PA134961047.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0204.
    HOGENOMi HOG000006110.
    HOVERGENi HBG008205.
    InParanoidi Q9NRZ5.
    KOi K13523.
    OMAi PEKYFFL.
    OrthoDBi EOG7H7928.
    PhylomeDBi Q9NRZ5.
    TreeFami TF314065.

    Enzyme and pathway databases

    UniPathwayi UPA00557 ; UER00613 .
    BioCyci MetaCyc:HS00452-MONOMER.
    Reactomei REACT_1190. Triglyceride Biosynthesis.
    REACT_120906. Synthesis of PA.

    Miscellaneous databases

    ChiTaRSi AGPAT4. human.
    GenomeRNAii 56895.
    NextBioi 62325.
    PROi Q9NRZ5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRZ5.
    Bgeei Q9NRZ5.
    CleanExi HS_AGPAT4.
    Genevestigatori Q9NRZ5.

    Family and domain databases

    InterProi IPR002123. Plipid/glycerol_acylTrfase.
    [Graphical view ]
    Pfami PF01553. Acyltransferase. 1 hit.
    [Graphical view ]
    SMARTi SM00563. PlsC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The structure and functions of human lysophosphatidic acid acyltransferases."
      Leung D.W.
      Front. Biosci. 6:D944-D953(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Spleen.
    5. "Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria."
      Prasad S.S., Garg A., Agarwal A.K.
      J. Lipid Res. 52:451-462(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPLCD_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRZ5
    Secondary accession number(s): Q5TEF0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 116 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 6
      Human chromosome 6: 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