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P30122

- CEL_BOVIN

UniProt

P30122 - CEL_BOVIN

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Protein
Bile salt-activated lipase
Gene
CEL
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.
A steryl ester + H2O = a sterol + a fatty acid.

Enzyme regulationi

Activated by bile salts containing a 7-hydroxyl group in the infants intestine where it aids to digest milk fats.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei212 – 2121Acyl-ester intermediate
Active sitei338 – 3381Charge relay system
Active sitei453 – 4531Charge relay system

GO - Molecular functioni

  1. acylglycerol lipase activity Source: RefGenome
  2. sterol esterase activity Source: UniProtKB-EC
  3. triglyceride lipase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Protein family/group databases

MEROPSiS09.985.

Names & Taxonomyi

Protein namesi
Recommended name:
Bile salt-activated lipase (EC:3.1.1.13, EC:3.1.1.3)
Short name:
BAL
Alternative name(s):
Bile salt-stimulated lipase
Short name:
BSSL
Carboxyl ester lipase
Cholesterol esterase
Pancreatic lysophospholipase
Sterol esterase
Gene namesi
Name:CEL
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RefGenome
  3. extracellular space Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 18›181 Publication
Add
BLAST
Chaini19 – 597579Bile salt-activated lipase
PRO_0000008630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi82 ↔ 98
Glycosylationi205 – 2051N-linked (GlcNAc...)
Disulfide bondi264 ↔ 275
Glycosylationi379 – 3791N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP30122.

Interactioni

Subunit structurei

Interacts with CLC By similarity.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000032584.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 264
Beta strandi29 – 324
Beta strandi34 – 374
Beta strandi40 – 423
Beta strandi44 – 5512
Beta strandi70 – 745
Beta strandi83 – 864
Beta strandi87 – 893
Beta strandi90 – 945
Beta strandi100 – 1078
Beta strandi109 – 1113
Beta strandi115 – 1217
Beta strandi126 – 1294
Turni132 – 1343
Helixi141 – 1433
Helixi146 – 1527
Beta strandi155 – 1595
Helixi164 – 1685
Helixi180 – 19516
Helixi196 – 1994
Beta strandi201 – 21111
Helixi213 – 22311
Helixi225 – 2273
Turni228 – 2303
Beta strandi232 – 2387
Helixi244 – 2463
Helixi251 – 26111
Helixi269 – 27810
Helixi281 – 2866
Helixi299 – 3024
Beta strandi311 – 3144
Helixi318 – 3203
Helixi322 – 3254
Beta strandi328 – 3358
Turni336 – 3394
Helixi340 – 3467
Helixi348 – 3503
Beta strandi353 – 3553
Helixi359 – 36911
Helixi370 – 3734
Helixi374 – 38613
Helixi387 – 3893
Helixi395 – 41016
Helixi412 – 42514
Beta strandi431 – 4366
Beta strandi443 – 4453
Turni453 – 4564
Helixi457 – 4604
Helixi463 – 4664
Helixi468 – 4703
Helixi473 – 49220
Beta strandi497 – 5004
Turni511 – 5133
Beta strandi515 – 5217
Helixi525 – 5273
Beta strandi528 – 5303
Helixi534 – 5418
Helixi543 – 5464
Beta strandi557 – 5593
Beta strandi593 – 5953

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKNX-ray2.80A19-597[»]
1AQLX-ray2.80A/B19-550[»]
2BCEX-ray1.60A19-597[»]
ProteinModelPortaliP30122.
SMRiP30122. Positions 19-565.

Miscellaneous databases

EvolutionaryTraceiP30122.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30122-1 [UniParc]FASTAAdd to Basket

« Hide

LGASRLGPSP GCLAVASAAK LGSVYTEGGF VEGVNKKLSL FGDSIDIFKG    50
IPFAAAPKAL EKPERHPGWQ GTLKAKSFKK RCLQATLTQD STYGNEDCLY 100
LNIWVPQGRK EVSHDLPVMI WIYGGAFLMG ASQGANFLSN YLYDGEEIAT 150
RGNVIVVTFN YRVGPLGFLS TGDSNLPGNY GLWDQHMAIA WVKRNIEAFG 200
GDPDNITLFG ESAGGASVSL QTLSPYNKGL IKRAISQSGV GLCPWAIQQD 250
PLFWAKRIAE KVGCPVDDTS KMAGCLKITD PRALTLAYKL PLGSTEYPKL 300
HYLSFVPVID GDFIPDDPVN LYANAADVDY IAGTNDMDGH LFVGMDVPAI 350
NSNKQDVTEE DFYKLVSGLT VTKGLRGANA TYEVYTEPWA QDSSQETRKK 400
TMVDLETDIL FLIPTKIAVA QHKSHAKSAN TYTYLFSQPS RMPIYPKWMG 450
ADHADDLQYV FGKPFATPLG YRAQDRTVSK AMIAYWTNFA RTGDPNTGHS 500
TVPANWDPYT LEDDNYLEIN KQMDSNSMKL HLRTNYLQFW TQTYQALPTV 550
TSAGASLLPP EDNSQASPVP PADNSGAPTE PSAGDSEVAQ MPVVIGF 597
Length:597
Mass (Da):65,162
Last modified:July 15, 1998 - v2
Checksum:iB23EB7AED90EBFD1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301F → P AA sequence 1 Publication
Sequence conflicti45 – 451I → V in AAA56788. 1 Publication

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28402 mRNA. Translation: AAA56788.1.
PIRiA33668.
UniGeneiBt.13160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M28402 mRNA. Translation: AAA56788.1 .
PIRi A33668.
UniGenei Bt.13160.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AKN X-ray 2.80 A 19-597 [» ]
1AQL X-ray 2.80 A/B 19-550 [» ]
2BCE X-ray 1.60 A 19-597 [» ]
ProteinModelPortali P30122.
SMRi P30122. Positions 19-565.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000032584.

Chemistry

BindingDBi P30122.
ChEMBLi CHEMBL2988.

Protein family/group databases

MEROPSi S09.985.

Proteomic databases

PRIDEi P30122.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG2272.
HOGENOMi HOG000091866.
HOVERGENi HBG008839.

Miscellaneous databases

EvolutionaryTracei P30122.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning of the bovine pancreatic cholesterol esterase/lysophospholipase."
    Kyger E.M., Wiegand R.C., Lange L.G.
    Biochem. Biophys. Res. Commun. 164:1302-1309(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Purification and characterization of bovine pancreatic bile salt-activated lipase."
    Tanaka H., Mierau I., Ito F.
    J. Biochem. 125:883-890(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-40.
    Tissue: Pancreas.
  3. "The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism."
    Wang X., Wang C.S., Tang J., Dyda F., Zhang X.C.
    Structure 5:1209-1218(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 19-565, SEQUENCE REVISION TO 45.
  4. "Structure of bovine pancreatic cholesterol esterase at 1.6 A: novel structural features involved in lipase activation."
    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.
    Biochemistry 37:5107-5117(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-597.

Entry informationi

Entry nameiCEL_BOVIN
AccessioniPrimary (citable) accession number: P30122
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 15, 1998
Last modified: July 9, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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