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LYPLA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1FJ2
Identifiers
Aliases	LYPLA1, APT-1, APT1, LPL-I, LPL1, hAPT1, lysophospholipase I, lysophospholipase 1
External IDs	OMIM: 605599; MGI: 1344588; HomoloGene: 100781; GeneCards: LYPLA1; OMA:LYPLA1 - orthologs
Gene location (Human) Chr. Chromosome 8 (human) Band 8q11.23 Start 54,046,367 bp End 54,102,017 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1|1 A1 Start 4,878,011 bp End 4,918,633 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in human penis oral cavity gonad vulva right ventricle skin of thigh mucosa of sigmoid colon epithelium of nasopharynx superior surface of tongue biceps brachii Top expressed in right kidney gallbladder superior surface of tongue intercostal muscle jejunum epithelium of small intestine cardiac muscle tissue of left ventricle gastrula extensor digitorum longus muscle plantaris muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function lysophospholipase activity hydrolase activity lipase activity palmitoyl-(protein) hydrolase activity carboxylic ester hydrolase activity protein binding Cellular component cytoplasm cytosol extracellular exosome mitochondrion Biological process protein depalmitoylation regulation of nitric-oxide synthase activity negative regulation of Golgi to plasma membrane protein transport fatty acid metabolic process lipid metabolism metabolism Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10434 18777 Ensembl ENSG00000120992 ENSMUSG00000025903 UniProt O75608 Q6IAQ1 P97823 RefSeq (mRNA) NM_001279356 NM_001279357 NM_001279358 NM_001279359 NM_001279360 NM_006330 NM_008866 NM_001355712 RefSeq (protein) NP_001266285 NP_001266286 NP_001266287 NP_001266288 NP_001266289 NP_006321 NP_006321.1 NP_032892 NP_001342641 Location (UCSC) Chr 8: 54.05 – 54.1 Mb Chr 1: 4.88 – 4.92 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Acyl-protein thioesterase 1 is an enzyme that in humans is encoded by the LYPLA1 gene.

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.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000120992 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000025903 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Wang A, Yang HC, Friedman P, Johnson CA, Dennis EA (Apr 1999). "A specific human lysophospholipase: cDNA cloning, tissue distribution and kinetic characterization". Biochim Biophys Acta. 1437 (2): 157–69. doi:10.1016/s1388-1981(99)00012-8. PMID 10064899.
6. ^ "Entrez Gene: LYPLA1 lysophospholipase I".

Further reading

• Wang A, Dennis EA (1999). "Mammalian lysophospholipases". Biochim. Biophys. Acta. 1439 (1): 1–16. doi:10.1016/s1388-1981(99)00063-3. 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. doi:10.1016/0014-5793(92)80294-Q. PMID 1531641. S2CID 19633878.
• 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. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• 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. doi:10.1016/s1388-1981(00)00020-2. PMID 10760470. S2CID 24130546.
• 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. doi:10.1101/gr.140200. PMC 310934. 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. doi:10.1016/S0969-2126(00)00529-3. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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. PMC 528928. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

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