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Q9NRZ5

- PLCD_HUMAN

UniProt

Q9NRZ5 - PLCD_HUMAN

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Protein
1-acyl-sn-glycerol-3-phosphate acyltransferase delta
Gene
AGPAT4, UNQ499/PRO1016
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121Helical; Reviewed prediction
Add
BLAST
Transmembranei125 – 14521Helical; Reviewed prediction
Add
BLAST
Transmembranei307 – 32721Helical; Reviewed prediction
Add
BLAST
Transmembranei338 – 35821Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 delta
PRO_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.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 115 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

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