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P30122

- CEL_BOVIN

UniProt

P30122 - CEL_BOVIN

Protein

Bile salt-activated lipase

Gene

CEL

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    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

    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

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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:
    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...
    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.

    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: October 1, 2014
    This is version 98 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