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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) (Fragment)

 CEL_BOVIN               Reviewed;         597 AA.
P30122;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
05-DEC-2018, entry version 119.
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; Fragment;
Name=CEL;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2590203; DOI=10.1016/0006-291X(89)91811-1;
Kyger E.M., Wiegand R.C., Lange L.G.;
"Cloning of the bovine pancreatic cholesterol
esterase/lysophospholipase.";
Biochem. Biophys. Res. Commun. 164:1302-1309(1989).
[2]
PROTEIN SEQUENCE OF 19-40.
TISSUE=Pancreas;
PubMed=10220579; DOI=10.1093/oxfordjournals.jbchem.a022364;
Tanaka H., Mierau I., Ito F.;
"Purification and characterization of bovine pancreatic bile salt-
activated lipase.";
J. Biochem. 125:883-890(1999).
[3]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 19-565, AND SEQUENCE REVISION
TO 45.
PubMed=9331420; DOI=10.1016/S0969-2126(97)00271-2;
Wang X., Wang C.S., Tang J., Dyda F., Zhang X.C.;
"The crystal structure of bovine bile salt activated lipase: insights
into the bile salt activation mechanism.";
Structure 5:1209-1218(1997).
[4]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-597.
PubMed=9548741; DOI=10.1021/bi972989g;
Chen J.C.-H., Miercke L.J.W., Krucinski J., Starr J.R., Saenz G.,
Wang X., Spilburg C.A., Lange L.G., Ellsworth J.L., Stroud R.M.;
"Structure of bovine pancreatic cholesterol esterase at 1.6 A: novel
structural features involved in lipase activation.";
Biochemistry 37:5107-5117(1998).
-!- 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 in the infants intestine where it aids to digest
milk fats.
-!- SUBUNIT: Interacts with CLC. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
{ECO:0000305}.
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EMBL; M28402; AAA56788.1; -; mRNA.
PIR; A33668; A33668.
UniGene; Bt.13160; -.
PDB; 1AKN; X-ray; 2.80 A; A=19-597.
PDB; 1AQL; X-ray; 2.80 A; A/B=19-550.
PDB; 2BCE; X-ray; 1.60 A; A=19-597.
PDBsum; 1AKN; -.
PDBsum; 1AQL; -.
PDBsum; 2BCE; -.
ProteinModelPortal; P30122; -.
SMR; P30122; -.
STRING; 9913.ENSBTAP00000032584; -.
BindingDB; P30122; -.
ChEMBL; CHEMBL2988; -.
SwissLipids; SLP:000000735; -.
ESTHER; bovin-balip; Cholesterol_esterase.
MEROPS; S09.985; -.
PaxDb; P30122; -.
PRIDE; P30122; -.
eggNOG; KOG1516; Eukaryota.
eggNOG; COG2272; LUCA.
HOGENOM; HOG000091866; -.
HOVERGEN; HBG008839; -.
InParanoid; P30122; -.
EvolutionaryTrace; P30122; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0009986; C:cell surface; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:0042043; F:neurexin family protein binding; IBA:GO_Central.
GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
GO; GO:0004771; F:sterol esterase activity; IBA:GO_Central.
GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
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;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
Lipid metabolism; Reference proteome; Secreted; Serine esterase;
Signal.
SIGNAL <1 18 {ECO:0000269|PubMed:10220579}.
CHAIN 19 597 Bile salt-activated lipase.
/FTId=PRO_0000008630.
ACT_SITE 212 212 Acyl-ester intermediate.
ACT_SITE 338 338 Charge relay system.
ACT_SITE 453 453 Charge relay system.
CARBOHYD 205 205 N-linked (GlcNAc...) asparagine.
CARBOHYD 379 379 N-linked (GlcNAc...) asparagine.
DISULFID 82 98
DISULFID 264 275
CONFLICT 30 30 F -> P (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 45 45 I -> V (in Ref. 1; AAA56788).
{ECO:0000305}.
NON_TER 1 1
STRAND 23 26 {ECO:0000244|PDB:2BCE}.
STRAND 29 32 {ECO:0000244|PDB:2BCE}.
STRAND 34 37 {ECO:0000244|PDB:2BCE}.
STRAND 40 42 {ECO:0000244|PDB:1AQL}.
STRAND 44 55 {ECO:0000244|PDB:2BCE}.
STRAND 70 74 {ECO:0000244|PDB:2BCE}.
STRAND 83 86 {ECO:0000244|PDB:2BCE}.
STRAND 87 89 {ECO:0000244|PDB:1AKN}.
STRAND 90 94 {ECO:0000244|PDB:2BCE}.
STRAND 100 107 {ECO:0000244|PDB:2BCE}.
STRAND 109 111 {ECO:0000244|PDB:2BCE}.
STRAND 115 121 {ECO:0000244|PDB:2BCE}.
STRAND 126 129 {ECO:0000244|PDB:2BCE}.
TURN 132 134 {ECO:0000244|PDB:1AKN}.
HELIX 141 143 {ECO:0000244|PDB:2BCE}.
HELIX 146 152 {ECO:0000244|PDB:2BCE}.
STRAND 155 159 {ECO:0000244|PDB:2BCE}.
HELIX 164 168 {ECO:0000244|PDB:2BCE}.
HELIX 180 195 {ECO:0000244|PDB:2BCE}.
HELIX 196 199 {ECO:0000244|PDB:2BCE}.
STRAND 201 211 {ECO:0000244|PDB:2BCE}.
HELIX 213 223 {ECO:0000244|PDB:2BCE}.
HELIX 225 227 {ECO:0000244|PDB:2BCE}.
TURN 228 230 {ECO:0000244|PDB:2BCE}.
STRAND 232 238 {ECO:0000244|PDB:2BCE}.
HELIX 244 246 {ECO:0000244|PDB:2BCE}.
HELIX 251 261 {ECO:0000244|PDB:2BCE}.
HELIX 269 278 {ECO:0000244|PDB:2BCE}.
HELIX 281 286 {ECO:0000244|PDB:2BCE}.
HELIX 299 302 {ECO:0000244|PDB:2BCE}.
STRAND 311 314 {ECO:0000244|PDB:2BCE}.
HELIX 318 320 {ECO:0000244|PDB:2BCE}.
HELIX 322 325 {ECO:0000244|PDB:2BCE}.
STRAND 328 335 {ECO:0000244|PDB:2BCE}.
TURN 336 339 {ECO:0000244|PDB:1AKN}.
HELIX 340 346 {ECO:0000244|PDB:2BCE}.
HELIX 348 350 {ECO:0000244|PDB:2BCE}.
STRAND 353 355 {ECO:0000244|PDB:2BCE}.
HELIX 359 369 {ECO:0000244|PDB:2BCE}.
HELIX 370 373 {ECO:0000244|PDB:2BCE}.
HELIX 374 386 {ECO:0000244|PDB:2BCE}.
HELIX 387 389 {ECO:0000244|PDB:2BCE}.
HELIX 395 410 {ECO:0000244|PDB:2BCE}.
HELIX 412 425 {ECO:0000244|PDB:2BCE}.
STRAND 431 436 {ECO:0000244|PDB:2BCE}.
STRAND 443 445 {ECO:0000244|PDB:2BCE}.
TURN 453 456 {ECO:0000244|PDB:2BCE}.
HELIX 457 460 {ECO:0000244|PDB:2BCE}.
HELIX 463 466 {ECO:0000244|PDB:2BCE}.
HELIX 468 470 {ECO:0000244|PDB:2BCE}.
HELIX 473 492 {ECO:0000244|PDB:2BCE}.
STRAND 497 500 {ECO:0000244|PDB:2BCE}.
TURN 511 513 {ECO:0000244|PDB:2BCE}.
STRAND 515 521 {ECO:0000244|PDB:2BCE}.
HELIX 525 527 {ECO:0000244|PDB:1AKN}.
STRAND 528 530 {ECO:0000244|PDB:2BCE}.
HELIX 534 541 {ECO:0000244|PDB:2BCE}.
HELIX 543 546 {ECO:0000244|PDB:2BCE}.
STRAND 557 559 {ECO:0000244|PDB:1AKN}.
STRAND 593 595 {ECO:0000244|PDB:2BCE}.
SEQUENCE 597 AA; 65162 MW; B23EB7AED90EBFD1 CRC64;
LGASRLGPSP GCLAVASAAK LGSVYTEGGF VEGVNKKLSL FGDSIDIFKG IPFAAAPKAL
EKPERHPGWQ GTLKAKSFKK RCLQATLTQD STYGNEDCLY LNIWVPQGRK EVSHDLPVMI
WIYGGAFLMG ASQGANFLSN YLYDGEEIAT RGNVIVVTFN YRVGPLGFLS TGDSNLPGNY
GLWDQHMAIA WVKRNIEAFG GDPDNITLFG ESAGGASVSL QTLSPYNKGL IKRAISQSGV
GLCPWAIQQD PLFWAKRIAE KVGCPVDDTS KMAGCLKITD PRALTLAYKL PLGSTEYPKL
HYLSFVPVID GDFIPDDPVN LYANAADVDY IAGTNDMDGH LFVGMDVPAI NSNKQDVTEE
DFYKLVSGLT VTKGLRGANA TYEVYTEPWA QDSSQETRKK TMVDLETDIL FLIPTKIAVA
QHKSHAKSAN TYTYLFSQPS RMPIYPKWMG ADHADDLQYV FGKPFATPLG YRAQDRTVSK
AMIAYWTNFA RTGDPNTGHS TVPANWDPYT LEDDNYLEIN KQMDSNSMKL HLRTNYLQFW
TQTYQALPTV TSAGASLLPP EDNSQASPVP PADNSGAPTE PSAGDSEVAQ MPVVIGF


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