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P02754

- LACB_BOVIN

UniProt

P02754 - LACB_BOVIN

Protein

Beta-lactoglobulin

Gene

LGB

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.

    GO - Molecular functioni

    1. retinol binding Source: UniProtKB-KW

    GO - Biological processi

    1. transport Source: UniProtKB-KW

    Keywords - Molecular functioni

    Milk protein

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Retinol-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactoglobulin
    Short name:
    Beta-LG
    Alternative name(s):
    Allergen: Bos d 5
    Gene namesi
    Name:LGB
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Allergenic propertiesi

    Causes an allergic reaction in human. Is one of the causes of cow's milk allergy.

    Keywords - Diseasei

    Allergen

    Protein family/group databases

    Allergomei164. Bos d 5.
    2739. Bos d 5.0101.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16162 PublicationsAdd
    BLAST
    Chaini17 – 178162Beta-lactoglobulinPRO_0000017903Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi82 ↔ 1762 Publications
    Disulfide bondi122 ↔ 137Alternate1 Publication
    Disulfide bondi122 ↔ 1352 Publications

    Post-translational modificationi

    Alternate disulfide bonds occur in equal amounts in all variants examined.

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP02754.
    PRIDEiP02754.

    PTM databases

    UniCarbKBiP02754.

    Expressioni

    Tissue specificityi

    Synthesized in mammary gland and secreted in milk.

    Interactioni

    Subunit structurei

    Under physiological conditions beta-lactoglobulin exists as an equilibrium mixture of monomeric and dimeric forms.

    Protein-protein interaction databases

    DIPiDIP-29525N.

    Structurei

    Secondary structure

    1
    178
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 213
    Helixi28 – 314
    Beta strandi36 – 449
    Helixi45 – 473
    Beta strandi48 – 503
    Beta strandi57 – 648
    Beta strandi70 – 789
    Beta strandi81 – 9111
    Beta strandi97 – 1004
    Beta strandi102 – 1043
    Beta strandi107 – 1137
    Beta strandi115 – 12410
    Beta strandi126 – 1283
    Helixi129 – 1313
    Beta strandi133 – 14311
    Helixi146 – 15611
    Beta strandi157 – 1593
    Beta strandi163 – 1664
    Helixi169 – 1724
    Helixi175 – 1773

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B0OX-ray2.50A17-178[»]
    1B8EX-ray1.95A17-178[»]
    1BEBX-ray1.80A/B17-178[»]
    1BSOX-ray2.23A17-178[»]
    1BSQX-ray2.22A17-178[»]
    1BSYX-ray2.24A17-178[»]
    1CJ5NMR-A19-178[»]
    1DV9NMR-A17-178[»]
    1GX8X-ray2.40A17-178[»]
    1GX9X-ray2.34A17-178[»]
    1GXAX-ray2.35A17-178[»]
    1QG5X-ray2.00A17-178[»]
    1UZ2X-ray1.95X17-178[»]
    1YUPX-ray2.10D18-176[»]
    2AKQX-ray3.00A/B/C/D17-178[»]
    2BLGX-ray2.46A17-178[»]
    2GJ5X-ray2.40A17-178[»]
    2Q2MX-ray2.10A17-178[»]
    2Q2PX-ray2.96A17-178[»]
    2Q39X-ray2.50A/B17-178[»]
    2R56X-ray2.80A/B17-178[»]
    3BLGX-ray2.56A17-178[»]
    3KZAX-ray2.00A/B33-169[»]
    3NPOX-ray2.20A17-178[»]
    3NQ3X-ray1.90A17-178[»]
    3NQ9X-ray1.90A17-178[»]
    3PH5X-ray2.40A/B18-178[»]
    3PH6X-ray2.53A/B18-178[»]
    3UEUX-ray2.10A17-178[»]
    3UEVX-ray1.90A17-178[»]
    3UEWX-ray2.00A17-178[»]
    3UEXX-ray2.10A17-178[»]
    4DQ3X-ray1.95A17-178[»]
    4DQ4X-ray1.90A17-178[»]
    4GNYX-ray1.64A17-178[»]
    4IB6X-ray2.20A17-178[»]
    4IB7X-ray2.20A17-178[»]
    4IB8X-ray2.30A17-178[»]
    4IB9X-ray2.20A17-178[»]
    4IBAX-ray2.30A17-178[»]
    4KIIX-ray1.85A17-178[»]
    DisProtiDP00193.
    ProteinModelPortaliP02754.
    SMRiP02754. Positions 17-178.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02754.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the calycin superfamily. Lipocalin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG73754.
    HOGENOMiHOG000113272.
    HOVERGENiHBG104361.
    InParanoidiP02754.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR002447. Blactoglobulin.
    IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view]
    PfamiPF00061. Lipocalin. 1 hit.
    [Graphical view]
    PRINTSiPR01172. BLCTOGLOBULN.
    PR00179. LIPOCALIN.
    SUPFAMiSSF50814. SSF50814. 1 hit.
    PROSITEiPS00213. LIPOCALIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P02754-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKCLLLALAL TCGAQALIVT QTMKGLDIQK VAGTWYSLAM AASDISLLDA    50
    QSAPLRVYVE ELKPTPEGDL EILLQKWENG ECAQKKIIAE KTKIPAVFKI 100
    DALNENKVLV LDTDYKKYLL FCMENSAEPE QSLACQCLVR TPEVDDEALE 150
    KFDKALKALP MHIRLSFNPT QLEEQCHI 178
    Length:178
    Mass (Da):19,883
    Last modified:August 1, 1991 - v3
    Checksum:i225F10A78C63A6B2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti121 – 1211F → V in CAA32835. (PubMed:2701948)Curated
    Sequence conflicti136 – 1361Q → E(PubMed:6897774)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611E → Q in variant D. 1 Publication
    Natural varianti72 – 721I → L in variant W. 1 Publication
    Natural varianti75 – 751Q → H in variant C; found only in the Jersey breed. 1 Publication
    Natural varianti80 – 801G → D in variant A. 3 Publications
    Natural varianti134 – 1341A → V in variant A. 4 Publications

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14712 mRNA. Translation: CAA32835.1.
    Z48305 Genomic DNA. Translation: CAA88303.1.
    DQ489319 Genomic DNA. Translation: ABF48380.1.
    BC108213 mRNA. Translation: AAI08214.1.
    X52581 Genomic DNA. Translation: CAA36812.1.
    M19088 Genomic DNA. Translation: AAA30411.1.
    M27732 mRNA. Translation: AAA30412.1.
    K01086 mRNA. Translation: AAA30413.1.
    PIRiS10179. LGBO.
    RefSeqiNP_776354.2. NM_173929.3.
    UniGeneiBt.385.

    Genome annotation databases

    GeneIDi280838.
    KEGGibta:280838.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14712 mRNA. Translation: CAA32835.1 .
    Z48305 Genomic DNA. Translation: CAA88303.1 .
    DQ489319 Genomic DNA. Translation: ABF48380.1 .
    BC108213 mRNA. Translation: AAI08214.1 .
    X52581 Genomic DNA. Translation: CAA36812.1 .
    M19088 Genomic DNA. Translation: AAA30411.1 .
    M27732 mRNA. Translation: AAA30412.1 .
    K01086 mRNA. Translation: AAA30413.1 .
    PIRi S10179. LGBO.
    RefSeqi NP_776354.2. NM_173929.3.
    UniGenei Bt.385.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B0O X-ray 2.50 A 17-178 [» ]
    1B8E X-ray 1.95 A 17-178 [» ]
    1BEB X-ray 1.80 A/B 17-178 [» ]
    1BSO X-ray 2.23 A 17-178 [» ]
    1BSQ X-ray 2.22 A 17-178 [» ]
    1BSY X-ray 2.24 A 17-178 [» ]
    1CJ5 NMR - A 19-178 [» ]
    1DV9 NMR - A 17-178 [» ]
    1GX8 X-ray 2.40 A 17-178 [» ]
    1GX9 X-ray 2.34 A 17-178 [» ]
    1GXA X-ray 2.35 A 17-178 [» ]
    1QG5 X-ray 2.00 A 17-178 [» ]
    1UZ2 X-ray 1.95 X 17-178 [» ]
    1YUP X-ray 2.10 D 18-176 [» ]
    2AKQ X-ray 3.00 A/B/C/D 17-178 [» ]
    2BLG X-ray 2.46 A 17-178 [» ]
    2GJ5 X-ray 2.40 A 17-178 [» ]
    2Q2M X-ray 2.10 A 17-178 [» ]
    2Q2P X-ray 2.96 A 17-178 [» ]
    2Q39 X-ray 2.50 A/B 17-178 [» ]
    2R56 X-ray 2.80 A/B 17-178 [» ]
    3BLG X-ray 2.56 A 17-178 [» ]
    3KZA X-ray 2.00 A/B 33-169 [» ]
    3NPO X-ray 2.20 A 17-178 [» ]
    3NQ3 X-ray 1.90 A 17-178 [» ]
    3NQ9 X-ray 1.90 A 17-178 [» ]
    3PH5 X-ray 2.40 A/B 18-178 [» ]
    3PH6 X-ray 2.53 A/B 18-178 [» ]
    3UEU X-ray 2.10 A 17-178 [» ]
    3UEV X-ray 1.90 A 17-178 [» ]
    3UEW X-ray 2.00 A 17-178 [» ]
    3UEX X-ray 2.10 A 17-178 [» ]
    4DQ3 X-ray 1.95 A 17-178 [» ]
    4DQ4 X-ray 1.90 A 17-178 [» ]
    4GNY X-ray 1.64 A 17-178 [» ]
    4IB6 X-ray 2.20 A 17-178 [» ]
    4IB7 X-ray 2.20 A 17-178 [» ]
    4IB8 X-ray 2.30 A 17-178 [» ]
    4IB9 X-ray 2.20 A 17-178 [» ]
    4IBA X-ray 2.30 A 17-178 [» ]
    4KII X-ray 1.85 A 17-178 [» ]
    DisProti DP00193.
    ProteinModelPortali P02754.
    SMRi P02754. Positions 17-178.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29525N.

    Chemistry

    ChEMBLi CHEMBL1075053.

    Protein family/group databases

    Allergomei 164. Bos d 5.
    2739. Bos d 5.0101.

    PTM databases

    UniCarbKBi P02754.

    Proteomic databases

    PaxDbi P02754.
    PRIDEi P02754.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 280838.
    KEGGi bta:280838.

    Organism-specific databases

    CTDi 5047.

    Phylogenomic databases

    eggNOGi NOG73754.
    HOGENOMi HOG000113272.
    HOVERGENi HBG104361.
    InParanoidi P02754.

    Miscellaneous databases

    EvolutionaryTracei P02754.
    NextBioi 20804987.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR002447. Blactoglobulin.
    IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR01172. BLCTOGLOBULN.
    PR00179. LIPOCALIN.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00213. LIPOCALIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASP-80 AND VAL-134.
      Tissue: Mammary gland.
    2. "Bovine beta-lactoglobulin: cloning and expression in transgenic mice."
      Hyttinen J.M., Korhonen V.P., Myohanen S., Janne J.
      Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Sperm.
    3. "Aberrant low expression level of bovine beta-lactoglobulin B."
      Braunschweig M.H.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. NIH - Mammalian Gene Collection (MGC) project
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Liver.
    5. "Cloning and partial nucleotide sequence of the genomic bovine beta-lactoglobulin gene."
      Silva M.C., Wong D.W.S., Batt C.A.
      Nucleic Acids Res. 18:3051-3051(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
      Tissue: Pituitary.
    6. "The sequence of beta-lactoglobulin."
      Braunitzer G., Chen R., Schrank B., Stangl A.
      Hoppe-Seyler's Z. Physiol. Chem. 354:867-878(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-178, VARIANTS ASP-80 AND VAL-134.
    7. "The amino acid sequence of goat beta-lactoglobulin."
      Preaux G., Braunitzer G., Schrank B., Stangl A.
      Hoppe-Seyler's Z. Physiol. Chem. 360:1595-1604(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION TO 100; 103; 171 AND 172.
    8. "Genetic variants of bovine beta-lactoglobulin. A novel wild-type beta-lactoglobulin W and its primary sequence."
      Godovac-Zimmermann J., Krause I., Buchberger J., Weiss G., Klostermeyer H.
      Biol. Chem. Hoppe-Seyler 371:255-260(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-178, VARIANT LEU-72.
      Strain: Murnau-Werdenfelser.
    9. "Cloning and nucleotide sequence of the bovine beta-lactoglobulin gene."
      Jamieson A.C., Vandeyar M.A., Kang Y.C., Kinsella J.E., Batt C.A.
      Gene 61:85-90(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-178, VARIANTS ASP-80 AND VAL-134.
    10. "Localization of the Glu-Gln substitution differentiating B and D genetic variants in the peptide chain of bovine beta lactoglobulin."
      Brignon G., Ribadeau-Dumas B.
      FEBS Lett. 33:73-76(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 59-73, VARIANT GLN-61.
    11. "Molecular cloning of bovine beta-lactoglobulin cDNA."
      Ivanov V.N., Judinkova E.S., Gorodetsky S.I.
      Biol. Chem. Hoppe-Seyler 369:425-429(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-178.
    12. "Construction and identification by partial nucleotide sequence analysis of bovine casein and beta-lactoglobulin cDNA clones."
      Willis I.M., Stewart A.F., Caputo A., Thompson A.R., McKinlay A.G.
      DNA 1:375-386(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 125-138, VARIANT VAL-134.
    13. "Location of sulfhydryl and disulfide groups in bovine beta-lactoglobulins and effects of urea."
      McKenzie H.A., Ralston G.B., Shaw D.C.
      Biochemistry 11:4539-4547(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    14. Shaw D.C.
      Submitted (JAN-1973) to the PIR data bank
      Cited for: VARIANT HIS-75.
    15. "Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity."
      Monaco H.L., Zanotti G.
      Biopolymers 32:457-465(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPARISON OF X-RAY STRUCTURES.
    16. "Bovine beta-lactoglobulin at 1.8-A resolution -- still an enigmatic lipocalin."
      Brownlow S., Morais-Cabral J.H., Cooper R., Flower D.R., Yewdall S.J., Polikarpov I., North A.C.T., Sawyer L.
      Structure 5:481-495(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    17. "Structural basis of the tanford transition of bovine beta-lactoglobulin."
      Qin B.Y., Bewley M.C., Creamer L.K., Baker H.M., Baker E.N., Jameson G.B.
      Biochemistry 37:14014-14023(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS).
    18. "Partially folded structure of monomeric bovine beta-lactoglobulin."
      Molinari H., Ragona L., Varani L., Musco G., Consonni R., Zetta L., Monaco H.L.
      FEBS Lett. 381:237-243(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    19. "Solution structure and dynamics of bovine beta-lactoglobulin A."
      Kuwata K., Hoshino M., Forge V., Era S., Batt C.A., Goto Y.
      Protein Sci. 8:2541-2545(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF VARIANT A.

    Entry informationi

    Entry nameiLACB_BOVIN
    AccessioniPrimary (citable) accession number: P02754
    Secondary accession number(s): Q32P89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The B variant sequence is shown.

    Keywords - Technical termi

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

    Documents

    1. Allergens
      Nomenclature of allergens and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3