Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bile salt-activated lipase

Gene

CEL

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei212Acyl-ester intermediate1
Active sitei338Charge relay system1
Active sitei453Charge relay system1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Protein family/group databases

ESTHERibovin-balip. Cholesterol_esterase.
MEROPSiS09.985.

Chemistry databases

SwissLipidsiSLP:000000735.

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
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2988.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 181 PublicationAdd BLAST›18
ChainiPRO_000000863019 – 597Bile salt-activated lipaseAdd BLAST579

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi82 ↔ 98
Glycosylationi205N-linked (GlcNAc...)1
Disulfide bondi264 ↔ 275
Glycosylationi379N-linked (GlcNAc...)1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP30122.
PRIDEiP30122.

Interactioni

Subunit structurei

Interacts with CLC.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000032584.

Chemistry databases

BindingDBiP30122.

Structurei

Secondary structure

1597
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 26Combined sources4
Beta strandi29 – 32Combined sources4
Beta strandi34 – 37Combined sources4
Beta strandi40 – 42Combined sources3
Beta strandi44 – 55Combined sources12
Beta strandi70 – 74Combined sources5
Beta strandi83 – 86Combined sources4
Beta strandi87 – 89Combined sources3
Beta strandi90 – 94Combined sources5
Beta strandi100 – 107Combined sources8
Beta strandi109 – 111Combined sources3
Beta strandi115 – 121Combined sources7
Beta strandi126 – 129Combined sources4
Turni132 – 134Combined sources3
Helixi141 – 143Combined sources3
Helixi146 – 152Combined sources7
Beta strandi155 – 159Combined sources5
Helixi164 – 168Combined sources5
Helixi180 – 195Combined sources16
Helixi196 – 199Combined sources4
Beta strandi201 – 211Combined sources11
Helixi213 – 223Combined sources11
Helixi225 – 227Combined sources3
Turni228 – 230Combined sources3
Beta strandi232 – 238Combined sources7
Helixi244 – 246Combined sources3
Helixi251 – 261Combined sources11
Helixi269 – 278Combined sources10
Helixi281 – 286Combined sources6
Helixi299 – 302Combined sources4
Beta strandi311 – 314Combined sources4
Helixi318 – 320Combined sources3
Helixi322 – 325Combined sources4
Beta strandi328 – 335Combined sources8
Turni336 – 339Combined sources4
Helixi340 – 346Combined sources7
Helixi348 – 350Combined sources3
Beta strandi353 – 355Combined sources3
Helixi359 – 369Combined sources11
Helixi370 – 373Combined sources4
Helixi374 – 386Combined sources13
Helixi387 – 389Combined sources3
Helixi395 – 410Combined sources16
Helixi412 – 425Combined sources14
Beta strandi431 – 436Combined sources6
Beta strandi443 – 445Combined sources3
Turni453 – 456Combined sources4
Helixi457 – 460Combined sources4
Helixi463 – 466Combined sources4
Helixi468 – 470Combined sources3
Helixi473 – 492Combined sources20
Beta strandi497 – 500Combined sources4
Turni511 – 513Combined sources3
Beta strandi515 – 521Combined sources7
Helixi525 – 527Combined sources3
Beta strandi528 – 530Combined sources3
Helixi534 – 541Combined sources8
Helixi543 – 546Combined sources4
Beta strandi557 – 559Combined sources3
Beta strandi593 – 595Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AKNX-ray2.80A19-597[»]
1AQLX-ray2.80A/B19-550[»]
2BCEX-ray1.60A19-597[»]
ProteinModelPortaliP30122.
SMRiP30122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30122.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP30122.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR033560. BAL.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PANTHERiPTHR11559:SF139. PTHR11559:SF139. 1 hit.
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

        10         20         30         40         50
LGASRLGPSP GCLAVASAAK LGSVYTEGGF VEGVNKKLSL FGDSIDIFKG
60 70 80 90 100
IPFAAAPKAL EKPERHPGWQ GTLKAKSFKK RCLQATLTQD STYGNEDCLY
110 120 130 140 150
LNIWVPQGRK EVSHDLPVMI WIYGGAFLMG ASQGANFLSN YLYDGEEIAT
160 170 180 190 200
RGNVIVVTFN YRVGPLGFLS TGDSNLPGNY GLWDQHMAIA WVKRNIEAFG
210 220 230 240 250
GDPDNITLFG ESAGGASVSL QTLSPYNKGL IKRAISQSGV GLCPWAIQQD
260 270 280 290 300
PLFWAKRIAE KVGCPVDDTS KMAGCLKITD PRALTLAYKL PLGSTEYPKL
310 320 330 340 350
HYLSFVPVID GDFIPDDPVN LYANAADVDY IAGTNDMDGH LFVGMDVPAI
360 370 380 390 400
NSNKQDVTEE DFYKLVSGLT VTKGLRGANA TYEVYTEPWA QDSSQETRKK
410 420 430 440 450
TMVDLETDIL FLIPTKIAVA QHKSHAKSAN TYTYLFSQPS RMPIYPKWMG
460 470 480 490 500
ADHADDLQYV FGKPFATPLG YRAQDRTVSK AMIAYWTNFA RTGDPNTGHS
510 520 530 540 550
TVPANWDPYT LEDDNYLEIN KQMDSNSMKL HLRTNYLQFW TQTYQALPTV
560 570 580 590
TSAGASLLPP EDNSQASPVP PADNSGAPTE PSAGDSEVAQ MPVVIGF
Length:597
Mass (Da):65,162
Last modified:July 15, 1998 - v2
Checksum:iB23EB7AED90EBFD1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Sequence conflicti30F → P AA sequence (PubMed:10220579).Curated1
Sequence conflicti45I → V in AAA56788 (PubMed:2590203).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28402 mRNA. Translation: AAA56788.1.
PIRiA33668.
UniGeneiBt.13160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28402 mRNA. Translation: AAA56788.1.
PIRiA33668.
UniGeneiBt.13160.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AKNX-ray2.80A19-597[»]
1AQLX-ray2.80A/B19-550[»]
2BCEX-ray1.60A19-597[»]
ProteinModelPortaliP30122.
SMRiP30122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000032584.

Chemistry databases

BindingDBiP30122.
ChEMBLiCHEMBL2988.
SwissLipidsiSLP:000000735.

Protein family/group databases

ESTHERibovin-balip. Cholesterol_esterase.
MEROPSiS09.985.

Proteomic databases

PaxDbiP30122.
PRIDEiP30122.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP30122.

Miscellaneous databases

EvolutionaryTraceiP30122.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR033560. BAL.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PANTHERiPTHR11559:SF139. PTHR11559:SF139. 1 hit.
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 112 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.