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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

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 PublicationAdd
BLAST
Chaini19 – 597579Bile salt-activated lipasePRO_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

1
597
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 264Combined sources
Beta strandi29 – 324Combined sources
Beta strandi34 – 374Combined sources
Beta strandi40 – 423Combined sources
Beta strandi44 – 5512Combined sources
Beta strandi70 – 745Combined sources
Beta strandi83 – 864Combined sources
Beta strandi87 – 893Combined sources
Beta strandi90 – 945Combined sources
Beta strandi100 – 1078Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi115 – 1217Combined sources
Beta strandi126 – 1294Combined sources
Turni132 – 1343Combined sources
Helixi141 – 1433Combined sources
Helixi146 – 1527Combined sources
Beta strandi155 – 1595Combined sources
Helixi164 – 1685Combined sources
Helixi180 – 19516Combined sources
Helixi196 – 1994Combined sources
Beta strandi201 – 21111Combined sources
Helixi213 – 22311Combined sources
Helixi225 – 2273Combined sources
Turni228 – 2303Combined sources
Beta strandi232 – 2387Combined sources
Helixi244 – 2463Combined sources
Helixi251 – 26111Combined sources
Helixi269 – 27810Combined sources
Helixi281 – 2866Combined sources
Helixi299 – 3024Combined sources
Beta strandi311 – 3144Combined sources
Helixi318 – 3203Combined sources
Helixi322 – 3254Combined sources
Beta strandi328 – 3358Combined sources
Turni336 – 3394Combined sources
Helixi340 – 3467Combined sources
Helixi348 – 3503Combined sources
Beta strandi353 – 3553Combined sources
Helixi359 – 36911Combined sources
Helixi370 – 3734Combined sources
Helixi374 – 38613Combined sources
Helixi387 – 3893Combined sources
Helixi395 – 41016Combined sources
Helixi412 – 42514Combined sources
Beta strandi431 – 4366Combined sources
Beta strandi443 – 4453Combined sources
Turni453 – 4564Combined sources
Helixi457 – 4604Combined sources
Helixi463 – 4664Combined sources
Helixi468 – 4703Combined sources
Helixi473 – 49220Combined sources
Beta strandi497 – 5004Combined sources
Turni511 – 5133Combined sources
Beta strandi515 – 5217Combined sources
Helixi525 – 5273Combined sources
Beta strandi528 – 5303Combined sources
Helixi534 – 5418Combined sources
Helixi543 – 5464Combined sources
Beta strandi557 – 5593Combined sources
Beta strandi593 – 5953Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP30122.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP30122.

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

        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)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Sequence conflicti30 – 301F → P AA sequence (PubMed:10220579)Curated
Sequence conflicti45 – 451I → V in AAA56788. (PubMed:2590203)Curated

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 .
PIRi A33668.
UniGenei Bt.13160.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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.
InParanoidi P30122.

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: November 26, 2014
This is version 100 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