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P02754 (LACB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-lactoglobulin

Short name=Beta-LG
Alternative name(s):
Allergen=Bos d 5
Gene names
Name:LGB
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Secreted.

Tissue specificity

Synthesized in mammary gland and secreted in milk.

Post-translational modification

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

Allergenic properties

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

Miscellaneous

The B variant sequence is shown.

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseAllergen
   DomainSignal
   LigandRetinol-binding
   Molecular functionMilk protein
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processtransport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionretinol binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.6 Ref.8
Chain17 – 178162Beta-lactoglobulin
PRO_0000017903

Amino acid modifications

Disulfide bond82 ↔ 176 Ref.13 Ref.19
Disulfide bond122 ↔ 137Alternate Ref.13
Disulfide bond122 ↔ 135 Ref.13 Ref.19

Natural variations

Natural variant611E → Q in variant D. Ref.10
Natural variant721I → L in variant W. Ref.8
Natural variant751Q → H in variant C; found only in the Jersey breed. Ref.14
Natural variant801G → D in variant A. Ref.1 Ref.6 Ref.9
Natural variant1341A → V in variant A. Ref.1 Ref.6 Ref.9 Ref.12

Experimental info

Sequence conflict1211F → V in CAA32835. Ref.1
Sequence conflict1361Q → E Ref.12

Secondary structure

..................................... 178
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02754 [UniParc].

Last modified August 1, 1991. Version 3.
Checksum: 225F10A78C63A6B2

FASTA17819,883
        10         20         30         40         50         60 
MKCLLLALAL TCGAQALIVT QTMKGLDIQK VAGTWYSLAM AASDISLLDA QSAPLRVYVE 

        70         80         90        100        110        120 
ELKPTPEGDL EILLQKWENG ECAQKKIIAE KTKIPAVFKI DALNENKVLV LDTDYKKYLL 

       130        140        150        160        170 
FCMENSAEPE QSLACQCLVR TPEVDDEALE KFDKALKALP MHIRLSFNPT QLEEQCHI 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of the bovine beta-lactoglobulin cDNA."
Alexander L.J., Hayes G., Pearse M.J., Beattie C.W., Stewart A.F., Willis I.M., McKinlay A.G.
Nucleic Acids Res. 17:6739-6739(1989) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRLGBO. S10179.
RefSeqNP_776354.2. NM_173929.3.
UniGeneBt.385.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00193.
ProteinModelPortalP02754.
SMRP02754. Positions 17-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29525N.

Chemistry

ChEMBLCHEMBL1075053.

Protein family/group databases

Allergome164. Bos d 5.
2739. Bos d 5.0101.

PTM databases

UniCarbKBP02754.

Proteomic databases

PaxDbP02754.
PRIDEP02754.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID280838.
KEGGbta:280838.

Organism-specific databases

CTD5047.

Phylogenomic databases

eggNOGNOG73754.
HOGENOMHOG000113272.
HOVERGENHBG104361.
InParanoidP02754.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR002447. Blactoglobulin.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR01172. BLCTOGLOBULN.
PR00179. LIPOCALIN.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02754.
NextBio20804987.

Entry information

Entry nameLACB_BOVIN
AccessionPrimary (citable) accession number: P02754
Secondary accession number(s): Q32P89
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Allergens

Nomenclature of allergens and list of entries