(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Deuterostomia: NE > Chordata: NE > Craniata: NE > Vertebrata: NE > Gnathostomata: NE > Teleostomi: NE > Euteleostomi: NE > Actinopterygii: NE > Actinopteri: NE > Neopterygii: NE > Teleostei: NE > Osteoglossocephalai: NE > Clupeocephala: NE > Euteleosteomorpha: NE > Neoteleostei: NE > Eurypterygia: NE > Ctenosquamata: NE > Acanthomorphata: NE > Euacanthomorphacea: NE > Percomorphaceae: NE > Eupercaria: NE > Spariformes: NE > Sparidae: NE > Pagrus: NE > Pagrus major: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MKAWRVVFLYFLVLNAVVQHVTSLEEELSDSIFGNFLDPLKDLIEHKDDA NQTVAKFSLRKPSHPDDDLCYIVPGKPDSLAACTFNSSSKTFLVIHGWTL SGMFESWVAKLVSALYEREQTANVIVVDWLTSAQNHYVVAAQNTKAVGQE IARFIDWIEETTNMPLENIHLIGYSLGAHVAGFAGSHATNKVGRITGLDP AGPDFEGMHAHRRLSPDDAHFVDVLHTFTRGSLGLSIGIQQPVGHVDIYP NGGSFQPGCNLRGALEKIANFGIFAITDAVKCEHERSIHLFIDSLLNEQE AAKAYRCGSSDMFNRGMCLSCRKGRCNTVGYDISKVRKARNVQMYTKTRA SMPFRVYHYQLKIHFSSKVNRSEMEPSLTVSLYGTNGEAENLELKLKEKI ATNKTHSFLLVTEKDIGDLLMLKFKWEETNGWSTSNMLKMVSSWWSGDSD GANMEVHKIRIRAGETQQKMVFCVKDPESQKLTQEVTFVKCKDAWRTNSK QTPKRVTLEKH
Reference
Title: Organization of the lipoprotein lipase gene of red sea bream Pagrus major Oku H, Ogata HY, Liang XF Ref: Comparative Biochemistry & Physiology B Biochem Mol Biol, 131:775, 2002 : PubMed
Lipoprotein lipase (LPL) is a key enzyme of lipid deposition and metabolism. To investigate the mechanism of lipid deposition in fish, as a first step, we have characterized the LPL gene of a marine teleost red sea bream Pagrus major by cDNA and genomic structure analysis. The red sea bream LPL gene encodes 511 amino acids and spans approximately 6.3 kb of the genome. The coding region is organized into ten exons and nine introns. In comparison with the LPL of other animals, the deduced amino acid sequence shows a high degree of similarity with a conservation of functional domains, e.g. catalytic triad, N-glycosylation sites, lipid and heparin binding regions. The 1.1 kb of 5' flanking region contains two CCAAT, sequences homologous to Oct-I site and response elements for hormones including glucocorticoid, insulin and thyroid hormone. The results of the present study will facilitate further study of the function and regulation of the LPL in non-mammalian vertebrates.
