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P02754

- LACB_BOVIN

UniProt

P02754 - LACB_BOVIN

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Protein

Beta-lactoglobulin

Gene

LGB

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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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[»]
4LZUX-ray2.40A17-178[»]
4LZVX-ray2.44A17-178[»]
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

        10         20         30         40         50
MKCLLLALAL TCGAQALIVT QTMKGLDIQK VAGTWYSLAM AASDISLLDA
60 70 80 90 100
QSAPLRVYVE ELKPTPEGDL EILLQKWENG ECAQKKIIAE KTKIPAVFKI
110 120 130 140 150
DALNENKVLV LDTDYKKYLL FCMENSAEPE QSLACQCLVR TPEVDDEALE
160 170
KFDKALKALP MHIRLSFNPT QLEEQCHI
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 [» ]
4LZU X-ray 2.40 A 17-178 [» ]
4LZV X-ray 2.44 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

« Hide 'large scale' publications
  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 29, 2014
This is version 133 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