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Beta-lactoglobulin (Beta-LG) (allergen Bos d 5)

 LACB_BOVIN              Reviewed;         178 AA.
P02754; Q32P89;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 3.
23-MAY-2018, entry version 155.
RecName: Full=Beta-lactoglobulin;
Short=Beta-LG;
AltName: Allergen=Bos d 5;
Flags: Precursor;
Name=LGB;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASP-80 AND VAL-134.
TISSUE=Mammary gland;
PubMed=2701948; DOI=10.1093/nar/17.16.6739;
Alexander L.J., Hayes G., Pearse M.J., Beattie C.W., Stewart A.F.,
Willis I.M., McKinlay A.G.;
"Complete sequence of the bovine beta-lactoglobulin cDNA.";
Nucleic Acids Res. 17:6739-6739(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Sperm;
Hyttinen J.M., Korhonen V.P., Myohanen S., Janne J.;
"Bovine beta-lactoglobulin: cloning and expression in transgenic
mice.";
Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Braunschweig M.H.;
"Aberrant low expression level of bovine beta-lactoglobulin B.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
TISSUE=Pituitary;
PubMed=2349102; DOI=10.1093/nar/18.10.3051;
Silva M.C., Wong D.W.S., Batt C.A.;
"Cloning and partial nucleotide sequence of the genomic bovine beta-
lactoglobulin gene.";
Nucleic Acids Res. 18:3051-3051(1990).
[6]
PROTEIN SEQUENCE OF 17-178, AND VARIANTS ASP-80 AND VAL-134.
PubMed=4611888;
Braunitzer G., Chen R., Schrank B., Stangl A.;
"The sequence of beta-lactoglobulin.";
Hoppe-Seyler's Z. Physiol. Chem. 354:867-878(1973).
[7]
SEQUENCE REVISION TO 100; 103; 171 AND 172.
PubMed=511095;
Preaux G., Braunitzer G., Schrank B., Stangl A.;
"The amino acid sequence of goat beta-lactoglobulin.";
Hoppe-Seyler's Z. Physiol. Chem. 360:1595-1604(1979).
[8]
PROTEIN SEQUENCE OF 17-178, AND VARIANT LEU-72.
STRAIN=Murnau-Werdenfelser;
PubMed=2340107;
Godovac-Zimmermann J., Krause I., Buchberger J., Weiss G.,
Klostermeyer H.;
"Genetic variants of bovine beta-lactoglobulin. A novel wild-type
beta-lactoglobulin W and its primary sequence.";
Biol. Chem. Hoppe-Seyler 371:255-260(1990).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-178, AND VARIANTS ASP-80 AND
VAL-134.
PubMed=3443305; DOI=10.1016/0378-1119(87)90367-2;
Jamieson A.C., Vandeyar M.A., Kang Y.C., Kinsella J.E., Batt C.A.;
"Cloning and nucleotide sequence of the bovine beta-lactoglobulin
gene.";
Gene 61:85-90(1987).
[10]
PROTEIN SEQUENCE OF 59-73, AND VARIANT GLN-61.
PubMed=4737332; DOI=10.1016/0014-5793(73)80162-0;
Brignon G., Ribadeau-Dumas B.;
"Localization of the Glu-Gln substitution differentiating B and D
genetic variants in the peptide chain of bovine beta lactoglobulin.";
FEBS Lett. 33:73-76(1973).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 122-178.
PubMed=3202951;
Ivanov V.N., Judinkova E.S., Gorodetsky S.I.;
"Molecular cloning of bovine beta-lactoglobulin cDNA.";
Biol. Chem. Hoppe-Seyler 369:425-429(1988).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 125-138, AND VARIANT VAL-134.
PubMed=6897774; DOI=10.1089/dna.1982.1.375;
Willis I.M., Stewart A.F., Caputo A., Thompson A.R., McKinlay A.G.;
"Construction and identification by partial nucleotide sequence
analysis of bovine casein and beta-lactoglobulin cDNA clones.";
DNA 1:375-386(1982).
[13]
DISULFIDE BONDS.
PubMed=4569282; DOI=10.1021/bi00774a017;
McKenzie H.A., Ralston G.B., Shaw D.C.;
"Location of sulfhydryl and disulfide groups in bovine beta-
lactoglobulins and effects of urea.";
Biochemistry 11:4539-4547(1972).
[14]
VARIANT HIS-75.
Shaw D.C.;
Submitted (JAN-1973) to the PIR data bank.
[15]
COMPARISON OF X-RAY STRUCTURES.
PubMed=1623143; DOI=10.1002/bip.360320425;
Monaco H.L., Zanotti G.;
"Three-dimensional structure and active site of three hydrophobic
molecule-binding proteins with significant amino acid sequence
similarity.";
Biopolymers 32:457-465(1992).
[16]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=9115437; DOI=10.1016/S0969-2126(97)00205-0;
Brownlow S., Morais-Cabral J.H., Cooper R., Flower D.R., Yewdall S.J.,
Polikarpov I., North A.C.T., Sawyer L.;
"Bovine beta-lactoglobulin at 1.8-A resolution -- still an enigmatic
lipocalin.";
Structure 5:481-495(1997).
[17]
X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS).
PubMed=9760236; DOI=10.1021/bi981016t;
Qin B.Y., Bewley M.C., Creamer L.K., Baker H.M., Baker E.N.,
Jameson G.B.;
"Structural basis of the tanford transition of bovine beta-
lactoglobulin.";
Biochemistry 37:14014-14023(1998).
[18]
STRUCTURE BY NMR.
PubMed=8601463; DOI=10.1016/0014-5793(96)00100-7;
Molinari H., Ragona L., Varani L., Musco G., Consonni R., Zetta L.,
Monaco H.L.;
"Partially folded structure of monomeric bovine beta-lactoglobulin.";
FEBS Lett. 381:237-243(1996).
[19]
STRUCTURE BY NMR OF VARIANT A.
PubMed=10595563; DOI=10.1110/ps.8.11.2541;
Kuwata K., Hoshino M., Forge V., Era S., Batt C.A., Goto Y.;
"Solution structure and dynamics of bovine beta-lactoglobulin A.";
Protein Sci. 8:2541-2545(1999).
-!- FUNCTION: Primary component of whey, it binds retinol and is
probably involved in the transport of that molecule.
-!- SUBUNIT: Under physiological conditions beta-lactoglobulin exists
as an equilibrium mixture of monomeric and dimeric forms.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-9697387, EBI-9697387;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Synthesized in mammary gland and secreted in
milk.
-!- PTM: Alternate disulfide bonds occur in equal amounts in all
variants examined.
-!- ALLERGEN: Causes an allergic reaction in human. Is one of the
causes of cow's milk allergy.
-!- MISCELLANEOUS: The B variant sequence is shown.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X14712; CAA32835.1; -; mRNA.
EMBL; Z48305; CAA88303.1; -; Genomic_DNA.
EMBL; DQ489319; ABF48380.1; -; Genomic_DNA.
EMBL; BC108213; AAI08214.1; -; mRNA.
EMBL; X52581; CAA36812.1; -; Genomic_DNA.
EMBL; M19088; AAA30411.1; -; Genomic_DNA.
EMBL; M27732; AAA30412.1; -; mRNA.
EMBL; K01086; AAA30413.1; -; mRNA.
PIR; S10179; LGBO.
RefSeq; NP_776354.2; NM_173929.3.
UniGene; Bt.385; -.
PDB; 1B0O; X-ray; 2.50 A; A=17-178.
PDB; 1B8E; X-ray; 1.95 A; A=17-178.
PDB; 1BEB; X-ray; 1.80 A; A/B=17-178.
PDB; 1BSO; X-ray; 2.23 A; A=17-178.
PDB; 1BSQ; X-ray; 2.22 A; A=17-178.
PDB; 1BSY; X-ray; 2.24 A; A=17-178.
PDB; 1CJ5; NMR; -; A=19-178.
PDB; 1DV9; NMR; -; A=17-178.
PDB; 1GX8; X-ray; 2.40 A; A=17-178.
PDB; 1GX9; X-ray; 2.34 A; A=17-178.
PDB; 1GXA; X-ray; 2.35 A; A=17-178.
PDB; 1QG5; X-ray; 2.00 A; A=17-178.
PDB; 1UZ2; X-ray; 1.95 A; X=17-178.
PDB; 1YUP; X-ray; 2.10 A; D=18-176.
PDB; 2AKQ; X-ray; 3.00 A; A/B/C/D=17-178.
PDB; 2BLG; X-ray; 2.46 A; A=17-178.
PDB; 2GJ5; X-ray; 2.40 A; A=17-178.
PDB; 2Q2M; X-ray; 2.10 A; A=17-178.
PDB; 2Q2P; X-ray; 2.96 A; A=17-178.
PDB; 2Q39; X-ray; 2.50 A; A/B=17-178.
PDB; 2R56; X-ray; 2.80 A; A/B=17-178.
PDB; 3BLG; X-ray; 2.56 A; A=17-178.
PDB; 3KZA; X-ray; 2.00 A; A/B=33-169.
PDB; 3NPO; X-ray; 2.20 A; A=17-178.
PDB; 3NQ3; X-ray; 1.90 A; A=17-178.
PDB; 3NQ9; X-ray; 1.90 A; A=17-178.
PDB; 3PH5; X-ray; 2.40 A; A/B=18-178.
PDB; 3PH6; X-ray; 2.53 A; A/B=18-178.
PDB; 3UEU; X-ray; 2.10 A; A=17-178.
PDB; 3UEV; X-ray; 1.90 A; A=17-178.
PDB; 3UEW; X-ray; 2.00 A; A=17-178.
PDB; 3UEX; X-ray; 2.10 A; A=17-178.
PDB; 4DQ3; X-ray; 1.95 A; A=17-178.
PDB; 4DQ4; X-ray; 1.90 A; A=17-178.
PDB; 4GNY; X-ray; 1.64 A; A=17-178.
PDB; 4IB6; X-ray; 2.20 A; A=17-178.
PDB; 4IB7; X-ray; 2.20 A; A=17-178.
PDB; 4IB8; X-ray; 2.30 A; A=17-178.
PDB; 4IB9; X-ray; 2.20 A; A=17-178.
PDB; 4IBA; X-ray; 2.30 A; A=17-178.
PDB; 4KII; X-ray; 1.85 A; A=17-178.
PDB; 4LZU; X-ray; 2.40 A; A=17-178.
PDB; 4LZV; X-ray; 2.44 A; A=17-178.
PDB; 4Y0P; X-ray; 2.20 A; A=17-178.
PDB; 4Y0Q; X-ray; 2.00 A; A=17-178.
PDB; 4Y0R; X-ray; 2.30 A; A=17-178.
PDB; 5EEE; X-ray; 1.95 A; A=17-178.
PDB; 5HTD; X-ray; 2.50 A; A=17-178.
PDB; 5HTE; X-ray; 2.40 A; A=17-178.
PDB; 5IO5; X-ray; 2.85 A; A=17-178.
PDB; 5IO7; X-ray; 2.85 A; A=17-178.
PDB; 5K06; X-ray; 2.50 A; A=17-178.
PDB; 5LKE; X-ray; 2.80 A; A=17-178.
PDB; 5LKF; X-ray; 2.50 A; A=17-178.
PDB; 5NUJ; X-ray; 2.60 A; A=17-178.
PDB; 5NUK; X-ray; 1.70 A; A=17-178.
PDB; 5NUM; X-ray; 2.30 A; A=17-178.
PDB; 5NUN; X-ray; 1.95 A; A=17-178.
PDBsum; 1B0O; -.
PDBsum; 1B8E; -.
PDBsum; 1BEB; -.
PDBsum; 1BSO; -.
PDBsum; 1BSQ; -.
PDBsum; 1BSY; -.
PDBsum; 1CJ5; -.
PDBsum; 1DV9; -.
PDBsum; 1GX8; -.
PDBsum; 1GX9; -.
PDBsum; 1GXA; -.
PDBsum; 1QG5; -.
PDBsum; 1UZ2; -.
PDBsum; 1YUP; -.
PDBsum; 2AKQ; -.
PDBsum; 2BLG; -.
PDBsum; 2GJ5; -.
PDBsum; 2Q2M; -.
PDBsum; 2Q2P; -.
PDBsum; 2Q39; -.
PDBsum; 2R56; -.
PDBsum; 3BLG; -.
PDBsum; 3KZA; -.
PDBsum; 3NPO; -.
PDBsum; 3NQ3; -.
PDBsum; 3NQ9; -.
PDBsum; 3PH5; -.
PDBsum; 3PH6; -.
PDBsum; 3UEU; -.
PDBsum; 3UEV; -.
PDBsum; 3UEW; -.
PDBsum; 3UEX; -.
PDBsum; 4DQ3; -.
PDBsum; 4DQ4; -.
PDBsum; 4GNY; -.
PDBsum; 4IB6; -.
PDBsum; 4IB7; -.
PDBsum; 4IB8; -.
PDBsum; 4IB9; -.
PDBsum; 4IBA; -.
PDBsum; 4KII; -.
PDBsum; 4LZU; -.
PDBsum; 4LZV; -.
PDBsum; 4Y0P; -.
PDBsum; 4Y0Q; -.
PDBsum; 4Y0R; -.
PDBsum; 5EEE; -.
PDBsum; 5HTD; -.
PDBsum; 5HTE; -.
PDBsum; 5IO5; -.
PDBsum; 5IO7; -.
PDBsum; 5K06; -.
PDBsum; 5LKE; -.
PDBsum; 5LKF; -.
PDBsum; 5NUJ; -.
PDBsum; 5NUK; -.
PDBsum; 5NUM; -.
PDBsum; 5NUN; -.
DisProt; DP00193; -.
ProteinModelPortal; P02754; -.
SMR; P02754; -.
DIP; DIP-29525N; -.
MINT; P02754; -.
STRING; 9913.ENSBTAP00000019538; -.
BindingDB; P02754; -.
ChEMBL; CHEMBL1075053; -.
Allergome; 164; Bos d 5.
Allergome; 2739; Bos d 5.0101.
CarbonylDB; P02754; -.
GlyConnect; 70; -.
UniCarbKB; P02754; -.
PaxDb; P02754; -.
PeptideAtlas; P02754; -.
PRIDE; P02754; -.
GeneID; 280838; -.
KEGG; bta:280838; -.
CTD; 5047; -.
eggNOG; ENOG410JCG3; Eukaryota.
eggNOG; ENOG4111386; LUCA.
HOGENOM; HOG000113272; -.
HOVERGEN; HBG104361; -.
InParanoid; P02754; -.
EvolutionaryTrace; P02754; -.
PRO; PR:P02754; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0036041; F:long-chain fatty acid binding; IDA:CAFA.
GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR002447; Blactoglobulin.
InterPro; IPR012674; Calycin.
InterPro; IPR002345; Lipocalin.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11430; PTHR11430; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR01172; BLCTOGLOBULN.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Allergen; Complete proteome; Direct protein sequencing;
Disulfide bond; Milk protein; Polymorphism; Reference proteome;
Retinol-binding; Secreted; Signal; Transport.
SIGNAL 1 16 {ECO:0000269|PubMed:2340107,
ECO:0000269|PubMed:4611888}.
CHAIN 17 178 Beta-lactoglobulin.
/FTId=PRO_0000017903.
DISULFID 82 176 {ECO:0000269|PubMed:10595563,
ECO:0000269|PubMed:4569282}.
DISULFID 122 137 Alternate. {ECO:0000269|PubMed:4569282}.
DISULFID 122 135 {ECO:0000269|PubMed:10595563,
ECO:0000269|PubMed:4569282}.
VARIANT 61 61 E -> Q (in variant D).
{ECO:0000269|PubMed:4737332}.
VARIANT 72 72 I -> L (in variant W).
{ECO:0000269|PubMed:2340107}.
VARIANT 75 75 Q -> H (in variant C; found only in the
Jersey breed). {ECO:0000269|Ref.14}.
VARIANT 80 80 G -> D (in variant A).
{ECO:0000269|PubMed:2701948,
ECO:0000269|PubMed:3443305,
ECO:0000269|PubMed:4611888}.
VARIANT 134 134 A -> V (in variant A).
{ECO:0000269|PubMed:2701948,
ECO:0000269|PubMed:3443305,
ECO:0000269|PubMed:4611888,
ECO:0000269|PubMed:6897774}.
CONFLICT 121 121 F -> V (in Ref. 1; CAA32835).
{ECO:0000305}.
CONFLICT 136 136 Q -> E (in Ref. 12). {ECO:0000305}.
HELIX 19 21 {ECO:0000244|PDB:1B8E}.
HELIX 28 31 {ECO:0000244|PDB:4GNY}.
STRAND 36 44 {ECO:0000244|PDB:4GNY}.
HELIX 45 47 {ECO:0000244|PDB:4GNY}.
STRAND 48 50 {ECO:0000244|PDB:1UZ2}.
STRAND 57 64 {ECO:0000244|PDB:4GNY}.
STRAND 66 68 {ECO:0000244|PDB:5LKF}.
STRAND 70 78 {ECO:0000244|PDB:4GNY}.
STRAND 81 91 {ECO:0000244|PDB:4GNY}.
STRAND 97 100 {ECO:0000244|PDB:4GNY}.
STRAND 102 104 {ECO:0000244|PDB:4KII}.
STRAND 107 113 {ECO:0000244|PDB:4GNY}.
STRAND 115 124 {ECO:0000244|PDB:4GNY}.
STRAND 126 128 {ECO:0000244|PDB:3PH6}.
HELIX 129 131 {ECO:0000244|PDB:1BEB}.
STRAND 133 143 {ECO:0000244|PDB:4GNY}.
HELIX 146 156 {ECO:0000244|PDB:4GNY}.
STRAND 157 159 {ECO:0000244|PDB:3UEX}.
STRAND 163 166 {ECO:0000244|PDB:4GNY}.
HELIX 169 172 {ECO:0000244|PDB:4GNY}.
HELIX 175 177 {ECO:0000244|PDB:4GNY}.
SEQUENCE 178 AA; 19883 MW; 225F10A78C63A6B2 CRC64;
MKCLLLALAL TCGAQALIVT QTMKGLDIQK VAGTWYSLAM AASDISLLDA QSAPLRVYVE
ELKPTPEGDL EILLQKWENG ECAQKKIIAE KTKIPAVFKI DALNENKVLV LDTDYKKYLL
FCMENSAEPE QSLACQCLVR TPEVDDEALE KFDKALKALP MHIRLSFNPT QLEEQCHI


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