Gene_Locus Report

Biblio print

Add to basket

Go to basket

Tree Display

AceDB Schema

XML Display

Feedback

Gene_locus Report for: human-CEL

Homo sapiens (Human) bile-salt-activated lipase, BSSL BAL CEL CEH carboxyl ester lipase chr 9

Comment
The human lactating mammary gland and pancreas produce a lipolytic enzyme, carboxyl-ester lipase, earlier called bile salt-stimulated lipase. Carboxyl-ester lipase is a major component of pancreatic juice and is responsible for the hydrolysis of cholesterol esters as well as a variety of other dietary esters. The enzyme exerts its function in duodenal juice, is activated when mixed with bile salts, and plays an important role in the digestion of milk fat in newborn infants. By genomewide screen in one of their families with diabetes and exocrine pancreatic dysfunction, Raeder et al. (2006) linked diabetes to 9q34 (maximum lod score 5.07). In each of the 2 families with autosomal dominantly inherited diabetes and exocrine pancreas dysfunction described by them, Raeder et al. (2006) demonstrated a different single-base deletion causing frameshift in the variable number of tandem repeats (VNTR normal range 7-23 repeats in healthy controls) of the gene encoding carboxyl-ester lipase (CEL; 114840).tandem repeat domain may contribute to different short and long range interactions with the globular core domain and other macromolecules, including cell membranes. CEL-MODY is a protein misfolding disease caused by a negative gain-of-function effect of the mutant proteins in pancreatic tissues. (AF081673 O75612 onco fetal isoform feto-acinar pancreatic protein.slightly different c-terminus. Human protein for lipoamidase PIR S32318 Trembl Q9UCH1) (On chromosome 9 9q34 in the NT_000529 contig, the gene is followed by a carboxyl ester lipase pseudogene which includes exons 1, 8, 9, 10, and 11 of the wildtype gene peptide ENST00000252493 gene ENSG00000130210). Numerous repeats at the c-term excluded in ESTHER (only n-term Pfam A COesterase 1 544)


Relationship
Family|Cholesterol_esterase
Block| C
Position in NCBI Life Tree|Homo sapiens
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Deuterostomia: N E > Chordata: N E > Craniata: N E > Vertebrata: N E > Gnathostomata: N E > Teleostomi: N E > Euteleostomi: N E > Sarcopterygii: N E > Dipnotetrapodomorpha: N E > Tetrapoda: N E > Amniota: N E > Mammalia: N E > Theria: N E > Eutheria: N E > Boreoeutheria: N E > Euarchontoglires: N E > Primates: N E > Haplorrhini: N E > Simiiformes: N E > Catarrhini: N E > Hominoidea: N E > Hominidae: N E > Homininae: N E > Homo: N E > Homo sapiens: N E


Molecular evidence
Database
7 mutations: Table (e.g. : 1delVNTRsgt1_human-CEL, 1delVNTRsgt4_human-CEL, 3repeatVNTR_human-CEL ... more)
7 structures (e.g. : 1F6W, 1JMY, 6H0T... more)
Kinetic: human-CEL

Disease: Maturity-onset diabetes of the Young, Type8, with exocrine dysfunction, MODY8 -



2 substrates: C8-MGDG, Tributyrin
4 inhibitors (e.g. : IMP-pNP, NEDPA, NEMP... more)
>3 Genbank links 15 more: AL162417, X54457, M94579
3 UniProt : P19835, B4DSX9, A0A024R8D0
>3 Ncbi-nid links 4 more: 29500, 3421402, 180243
>3 Ncbi-pid links 2 more: 228133, 3421403, 3320604
>3 Structure links 4 more: 1F6W, 6H19, 6H1A
>3 UniProt links 4 more: O75612, P19835, Q9UMB1
>3 Interpro links 4 more: O75612, P19835, Q9UMB1
>3 Prodom links 4 more: O75612, P19835, Q9UMB1
>3 Pfam links 4 more: O75612, P19835, Q9UMB1
>3 PIRSF links 4 more: O75612, P19835, Q9UMB1
>3 SUPERFAM links 4 more: O75612, P19835, Q9UMB1
1 EntrezGene : 1056
1 SNP : 1056
1 UniGene : 533258
1 HUGO HGNC : 1848
1 IUPHAR : 2872
3 OMIM : 114840, 609812, 606391
1 Ensembl : ENSG00000170835
Sequence
Graphical view for this peptide sequence: human-CEL
Colored MSA for Cholesterol_esterase (raw)
MLTMGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSV
DIFKGIPFAAPTKALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGD
EDCLYLNIWVPQGRKQVSRDLPVMIWIYGGAFLMGSGHGANFLNNYLYDG
EEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNYGLRDQHMAIAWVKRN
IAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQSGVALSPW
VIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGL
EYPMLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASI
DMPAINKGNKKVTEEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQ
ENKKKTVVDFETDVLFLVPTEIALAQHRANAKSAKTYAYLFSHPSRMPVY
PKWVGADHADDIQYVFGKPFATPTGYRPQDRTVSKAMIAYWTNFAKTGDP
NMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLRYWTLTYL
ALPTVTD
Legend This 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

MLTMGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSV
DIFKGIPFAAPTKALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGD
EDCLYLNIWVPQGRKQVSRDLPVMIWIYGGAFLMGSGHGANFLNNYLYDG
EEIATRGNVIVVTFNYRVGPLGFLSTGDANLPGNYGLRDQHMAIAWVKRN
IAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQSGVALSPW
VIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGL
EYPMLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASI
DMPAINKGNKKVTEEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQ
ENKKKTVVDFETDVLFLVPTEIALAQHRANAKSAKTYAYLFSHPSRMPVY
PKWVGADHADDIQYVFGKPFATPTGYRPQDRTVSKAMIAYWTNFAKTGDP
NMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLRYWTLTYL
ALPTVTD


References
31 more
    Title: X-ray structures of human bile-salt activated lipase conjugated to nerve agents surrogates
    Touvrey C, Courageux C, Guillon V, Terreux R, Nachon F, Brazzolotto X
    Ref: Toxicology, 411:15, 2019 : PubMed

            

    Title: Molecular biology of enzymes involved with cholesterol ester hydrolysis in mammalian tissues
    Hui DY
    Ref: Biochimica & Biophysica Acta, 1303:1996, 1996 : PubMed

            

    Title: Bile salt-activated lipase. A multiple function lipolytic enzyme
    Wang CS, Hartsuck JA
    Ref: Biochimica & Biophysica Acta, 1166:1, 1993 : PubMed

            


Other Papers


Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer