LYPLA1

From Wikipedia, the free encyclopedia

Lysophospholipase I

PDB rendering based on 1fj2.

Available structures: 1fj2

Identifiers

Symbol(s)

LYPLA1; APT-1; LPL1; LYSOPLA

External IDs

OMIM: 605599 MGI: 1344588 HomoloGene: 4616

Gene ontology
Molecular Function:	• lysophospholipase activity • hydrolase activity
Cellular Component:	• membrane fraction • mitochondrion
Biological Process:	• lipid metabolic process • fatty acid metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006330 (mRNA)
NP_006321 (protein)

NM_008866 (mRNA)
NP_032892 (protein)

Location

Chr 8: 55.12 - 55.18 Mb

Chr 1: 4.8 - 4.84 Mb

Pubmed search

[1]

[2]

Lysophospholipase I, also known as LYPLA1, is a human gene.^[1]

Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene hydrolyzes lysophosphatidylcholine in both monomeric and micellar forms. The use of alternate polyadenylation sites has been found for this gene. There are alternatively spliced transcript variants described for this gene but the full length nature is not known yet.^[1]

[edit] References

^ ^a ^b Entrez Gene: LYPLA1 lysophospholipase I.

[edit] Further reading

Wang A, Dennis EA (1999). "Mammalian lysophospholipases.". Biochim. Biophys. Acta 1439 (1): 1–16. PMID 10395961.
Bohn E, Gerke V, Kresse H, et al. (1992). "Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase.". FEBS Lett. 296 (3): 237–40. PMID 1531641.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
Wang A, Yang HC, Friedman P, et al. (1999). "A specific human lysophospholipase: cDNA cloning, tissue distribution and kinetic characterization.". Biochim. Biophys. Acta 1437 (2): 157–69. PMID 10064899.
Wang A, Johnson CA, Jones Y, et al. (2000). "Subcellular localization and PKC-dependent regulation of the human lysophospholipase A/acyl-protein thioesterase in WISH cells.". Biochim. Biophys. Acta 1484 (2-3): 207–14. PMID 10760470.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.". Genome Res. 10 (10): 1546–60. PMID 11042152.
Devedjiev Y, Dauter Z, Kuznetsov SR, et al. (2001). "Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A.". Structure 8 (11): 1137–46. PMID 11080636.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.