PLD3

Phospholipase D family, member 3

Identifiers

PLD3 ; AD19; HU-K4; HUK4

External IDs

OMIM: 615698 HomoloGene: 7893 GeneCards: PLD3 Gene

3.1.4.4

Gene ontology
Molecular function	• phospholipase D activity • protein binding • N-acylphosphatidylethanolamine-specific phospholipase D activity
Cellular component	• endoplasmic reticulum membrane • integral component of membrane • extracellular exosome
Biological process	• phospholipid metabolic process • phosphatidylglycerol biosynthetic process • lipid catabolic process • small molecule metabolic process • glycerophospholipid biosynthetic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
40.35 – 40.38 Mb

Chr 7:
27.53 – 27.55 Mb

PubMed search

Phospholipase D family, member 3 is a protein that in humans is encoded by the PLD3 gene.^[1]

Function

This gene encodes a member of the phospholipase D (PLD) family of enzymes that catalyze the hydrolysis of membrane phospholipids. The encoded protein is a single-pass type II membrane protein and contains two PLD phosphodiesterase domains. This protein influences processing of amyloid-beta precursor protein. Mutations in this gene are associated with Alzheimer disease risk.^[1]

References

1 2 "Entrez Gene: Phospholipase D family, member 3".

Munck A, Böhm C, Seibel NM, Hashemol Hosseini Z, Hampe W (Apr 2005). "Hu-K4 is a ubiquitously expressed type 2 transmembrane protein associated with the endoplasmic reticulum". The FEBS Journal 272 (7): 1718–26. doi:10.1111/j.1742-4658.2005.04601.x. PMID 15794758.
Idkowiak-Baldys J, Baldys A, Raymond JR, Hannun YA (Aug 2009). "Sustained receptor stimulation leads to sequestration of recycling endosomes in a classical protein kinase C- and phospholipase D-dependent manner". The Journal of Biological Chemistry 284 (33): 22322–31. doi:10.1074/jbc.M109.026765. PMID 19525236.
Miyamoto-Sato E, Fujimori S, Ishizaka M, Hirai N, Masuoka K, Saito R, Ozawa Y, Hino K, Washio T, Tomita M, Yamashita T, Oshikubo T, Akasaka H, Sugiyama J, Matsumoto Y, Yanagawa H (2010). "A comprehensive resource of interacting protein regions for refining human transcription factor networks". PLOS ONE 5 (2): e9289. doi:10.1371/journal.pone.0009289. PMC 2827538. PMID 20195357.
Walker LC, Waddell N, Ten Haaf A, Grimmond S, Spurdle AB (Nov 2008). "Use of expression data and the CGEMS genome-wide breast cancer association study to identify genes that may modify risk in BRCA1/2 mutation carriers". Breast Cancer Research and Treatment 112 (2): 229–36. doi:10.1007/s10549-007-9848-5. PMID 18095154.
Pridgeon JW, Webber EA, Sha D, Li L, Chin LS (Jan 2009). "Proteomic analysis reveals Hrs ubiquitin-interacting motif-mediated ubiquitin signaling in multiple cellular processes". The FEBS Journal 276 (1): 118–31. doi:10.1111/j.1742-4658.2008.06760.x. PMC 2647816. PMID 19019082.
Zhang J, Chen S, Zhang S, Lu Z, Yang H, Wang H (Oct 2009). "[Over-expression of phospholipase D3 inhibits Akt phosphorylation in C2C12 myoblasts]". Sheng Wu Gong Cheng Xue Bao = Chinese Journal of Biotechnology 25 (10): 1524–31. PMID 20112697.
Russo P, Venezia A, Lauria F, Strazzullo P, Cappuccio FP, Iacoviello L, Barba G, Siani A (Apr 2006). "HindIII(+/-) polymorphism of the Y chromosome, blood pressure, and serum lipids: no evidence of association in three white populations". American Journal of Hypertension 19 (4): 331–8. doi:10.1016/j.amjhyper.2005.10.003. PMID 16580565.
Cheng J, Kapranov P, Drenkow J, Dike S, Brubaker S, Patel S, Long J, Stern D, Tammana H, Helt G, Sementchenko V, Piccolboni A, Bekiranov S, Bailey DK, Ganesh M, Ghosh S, Bell I, Gerhard DS, Gingeras TR (May 2005). "Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution". Science 308 (5725): 1149–54. doi:10.1126/science.1108625. PMID 15790807.
Pedersen KM, Finsen B, Celis JE, Jensen NA (Nov 1998). "Expression of a novel murine phospholipase D homolog coincides with late neuronal development in the forebrain". The Journal of Biological Chemistry 273 (47): 31494–504. doi:10.1074/jbc.273.47.31494. PMID 9813063.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

This article is issued from Wikipedia - version of the Sunday, January 24, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

PLD3

Function

References

Further reading