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Bile salt-activated lipase (BAL) (EC 3.1.1.13) (EC 3.1.1.3) (Bile salt-stimulated lipase) (BSSL) (Carboxyl ester lipase) (Cholesterol esterase) (Pancreatic lysophospholipase) (Sterol esterase)

 CEL_RAT                 Reviewed;         612 AA.
P07882; P14722;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 2.
05-DEC-2018, entry version 135.
RecName: Full=Bile salt-activated lipase;
Short=BAL;
EC=3.1.1.13;
EC=3.1.1.3;
AltName: Full=Bile salt-stimulated lipase;
Short=BSSL;
AltName: Full=Carboxyl ester lipase;
AltName: Full=Cholesterol esterase;
AltName: Full=Pancreatic lysophospholipase;
AltName: Full=Sterol esterase;
Flags: Precursor;
Name=Cel;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Pancreas;
PubMed=2688744; DOI=10.1016/0005-2760(89)90201-4;
Kissel J.A., Fontaine R.N., Turck C.W., Brockman H.L., Hui D.Y.;
"Molecular cloning and expression of cDNA for rat pancreatic
cholesterol esterase.";
Biochim. Biophys. Acta 1006:227-237(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3593682; DOI=10.1021/bi00380a020;
Han J.H., Stratowa C., Rutter W.J.;
"Isolation of full-length putative rat lysophospholipase cDNA using
improved methods for mRNA isolation and cDNA cloning.";
Biochemistry 26:1617-1625(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2069957; DOI=10.1021/bi00242a028;
Fontaine R.N., Carter C.P., Hui D.Y.;
"Structure of the rat pancreatic cholesterol esterase gene.";
Biochemistry 30:7008-7014(1991).
[4]
ACTIVE SITE SER-214.
PubMed=2211595;
Dipersio L.P., Fontaine R.N., Hui D.Y.;
"Identification of the active site serine in pancreatic cholesterol
esterase by chemical modification and site-specific mutagenesis.";
J. Biol. Chem. 265:16801-16806(1990).
[5]
ACTIVE SITE HIS-455.
PubMed=1999399;
Dipersio L.P., Fontaine R.N., Hui D.Y.;
"Site-specific mutagenesis of an essential histidine residue in
pancreatic cholesterol esterase.";
J. Biol. Chem. 266:4033-4036(1991).
-!- FUNCTION: Catalyzes fat and vitamin absorption. Acts in concert
with pancreatic lipase and colipase for the complete digestion of
dietary triglycerides.
-!- CATALYTIC ACTIVITY:
Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid
+ H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035,
ChEBI:CHEBI:28868; EC=3.1.1.3;
-!- CATALYTIC ACTIVITY:
Reaction=a steryl ester + H2O = a fatty acid + a sterol + H(+);
Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915;
EC=3.1.1.13;
-!- ACTIVITY REGULATION: Activated by bile salts containing a 7-
hydroxyl group.
-!- SUBUNIT: Interacts with CLC. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Synthesized primarily in the pancreas and then
transported to the intestine.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
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EMBL; X16054; CAA34189.1; -; mRNA.
EMBL; M15893; AAA41540.1; -; mRNA.
EMBL; M69157; AAB46376.1; -; Genomic_DNA.
PIR; A34967; A34967.
UniGene; Rn.91234; -.
ProteinModelPortal; P07882; -.
SMR; P07882; -.
STRING; 10116.ENSRNOP00000014572; -.
ESTHER; ratno-balip; Cholesterol_esterase.
MEROPS; S09.985; -.
PaxDb; P07882; -.
PRIDE; P07882; -.
UCSC; RGD:2331; rat.
RGD; 2331; Cel.
eggNOG; KOG1516; Eukaryota.
eggNOG; COG2272; LUCA.
HOGENOM; HOG000091866; -.
HOVERGEN; HBG008839; -.
InParanoid; P07882; -.
PhylomeDB; P07882; -.
PRO; PR:P07882; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009986; C:cell surface; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:0042588; C:zymogen granule; IDA:RGD.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:RGD.
GO; GO:0043208; F:glycosphingolipid binding; IDA:RGD.
GO; GO:0004622; F:lysophospholipase activity; IDA:RGD.
GO; GO:0042043; F:neurexin family protein binding; IBA:GO_Central.
GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
GO; GO:0050253; F:retinyl-palmitate esterase activity; IDA:RGD.
GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
GO; GO:0004771; F:sterol esterase activity; IDA:RGD.
GO; GO:0004806; F:triglyceride lipase activity; IDA:RGD.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
GO; GO:0007158; P:neuron cell-cell adhesion; IBA:GO_Central.
GO; GO:0097104; P:postsynaptic membrane assembly; IBA:GO_Central.
GO; GO:0097105; P:presynaptic membrane assembly; IBA:GO_Central.
GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR033560; BAL.
InterPro; IPR002018; CarbesteraseB.
InterPro; IPR019826; Carboxylesterase_B_AS.
InterPro; IPR019819; Carboxylesterase_B_CS.
PANTHER; PTHR43903:SF1; PTHR43903:SF1; 1.
Pfam; PF00135; COesterase; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
Lipid degradation; Lipid metabolism; Reference proteome; Repeat;
Secreted; Serine esterase; Signal.
SIGNAL 1 20
CHAIN 21 612 Bile salt-activated lipase.
/FTId=PRO_0000008633.
REPEAT 556 566 1.
REPEAT 567 577 2.
REPEAT 578 588 3.
REPEAT 589 599 4.
REGION 556 599 4 X 11 AA tandem repeats, O-glycosylated
region.
ACT_SITE 214 214 Acyl-ester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10039}.
ACT_SITE 340 340 Charge relay system. {ECO:0000250}.
ACT_SITE 455 455 Charge relay system. {ECO:0000250}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 84 100 {ECO:0000250}.
DISULFID 266 277 {ECO:0000250}.
MUTAGEN 440 440 H->Q: No effect on activity.
MUTAGEN 455 455 H->Q,R,A,S,D: Abolishes activity.
CONFLICT 26 26 V -> L (in Ref. 2; AAA41540).
{ECO:0000305}.
CONFLICT 154 154 G -> A (in Ref. 2; AAA41540).
{ECO:0000305}.
CONFLICT 217 217 A -> G (in Ref. 2; AAA41540).
{ECO:0000305}.
CONFLICT 219 219 S -> I (in Ref. 2; AAA41540).
{ECO:0000305}.
CONFLICT 419 419 M -> T (in Ref. 3; AAB46376).
{ECO:0000305}.
CONFLICT 513 513 T -> M (in Ref. 2; AAA41540 and 3;
AAB46376). {ECO:0000305}.
CONFLICT 576 577 GG -> VV (in Ref. 3; AAB46376).
{ECO:0000305}.
CONFLICT 608 609 GP -> VA (in Ref. 3; AAB46376).
{ECO:0000305}.
CONFLICT 611 611 G -> A (in Ref. 3; AAB46376).
{ECO:0000305}.
SEQUENCE 612 AA; 67040 MW; 1569CE4EA71ED02A CRC64;
MGRLEVLFLG LTCCLAAACA AKLGAVYTEG GFVEGVNKKL SLLGGDSVDI FKGIPFATAK
TLENPQRHPG WQGTLKATDF KKRCLQATIT QDDTYGQEDC LYLNIWVPQG RKQVSHDLPV
MVWIYGGAFL MGSGQGANFL KNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG
NFGLRDQHMA IAWVKRNIAA FGGDPDNITI FGESAGAASV SLQTLSPYNK GLIRRAISQS
GVALSPWAIQ ENPLFWAKTI AKKVGCPTED TAKMAGCLKI TDPRALTLAY RLPLKSQEYP
IVHYLAFIPV VDGDFIPDDP INLYDNAADI DYLAGINDMD GHLFATVDVP AIDKAKQDVT
EEDFYRLVSG HTVAKGLKGT QATFDIYTES WAQDPSQENM KKTVVAFETD ILFLIPTEMA
LAQHRAHAKS AKTYSYLFSH PSRMPIYPKW MGADHADDLQ YVFGKPFATP LGYRAQDRTV
SKAMIAYWTN FAKSGDPNMG NSPVPTHWYP YTTENGNYLD INKKITSTSM KEHLREKFLK
FWAVTFEMLP TVVGDHTPPE DDSEAAPVPP TDDSQGGPVP PTDDSQTTPV PPTDNSQAGD
SVEAQMPGPI GF


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