ID LACB_BOVIN Reviewed; 178 AA. AC P02754; Q32P89; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 3. DT 27-MAR-2024, entry version 191. DE RecName: Full=Beta-lactoglobulin; DE Short=Beta-LG; DE AltName: Allergen=Bos d 5; DE Flags: Precursor; GN Name=LGB; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASP-80 AND VAL-134. RC TISSUE=Mammary gland; RX PubMed=2701948; DOI=10.1093/nar/17.16.6739; RA Alexander L.J., Hayes G., Pearse M.J., Beattie C.W., Stewart A.F., RA Willis I.M., McKinlay A.G.; RT "Complete sequence of the bovine beta-lactoglobulin cDNA."; RL Nucleic Acids Res. 17:6739-6739(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Sperm; RA Hyttinen J.M., Korhonen V.P., Myohanen S., Janne J.; RT "Bovine beta-lactoglobulin: cloning and expression in transgenic mice."; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Braunschweig M.H.; RT "Aberrant low expression level of bovine beta-lactoglobulin B."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. RC TISSUE=Pituitary; RX PubMed=2349102; DOI=10.1093/nar/18.10.3051; RA Silva M.C., Wong D.W.S., Batt C.A.; RT "Cloning and partial nucleotide sequence of the genomic bovine beta- RT lactoglobulin gene."; RL Nucleic Acids Res. 18:3051-3051(1990). RN [6] RP PROTEIN SEQUENCE OF 17-178, AND VARIANTS ASP-80 AND VAL-134. RX PubMed=4611888; RA Braunitzer G., Chen R., Schrank B., Stangl A.; RT "The sequence of beta-lactoglobulin."; RL Hoppe-Seyler's Z. Physiol. Chem. 354:867-878(1973). RN [7] RP SEQUENCE REVISION TO 100; 103; 171 AND 172. RX PubMed=511095; DOI=10.1515/bchm2.1979.360.2.1595; RA Preaux G., Braunitzer G., Schrank B., Stangl A.; RT "The amino acid sequence of goat beta-lactoglobulin."; RL Hoppe-Seyler's Z. Physiol. Chem. 360:1595-1604(1979). RN [8] RP PROTEIN SEQUENCE OF 17-178, AND VARIANT LEU-72. RC STRAIN=Murnau-Werdenfelser; RX PubMed=2340107; RA Godovac-Zimmermann J., Krause I., Buchberger J., Weiss G., Klostermeyer H.; RT "Genetic variants of bovine beta-lactoglobulin. A novel wild-type beta- RT lactoglobulin W and its primary sequence."; RL Biol. Chem. Hoppe-Seyler 371:255-260(1990). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-178, AND VARIANTS ASP-80 AND RP VAL-134. RX PubMed=3443305; DOI=10.1016/0378-1119(87)90367-2; RA Jamieson A.C., Vandeyar M.A., Kang Y.C., Kinsella J.E., Batt C.A.; RT "Cloning and nucleotide sequence of the bovine beta-lactoglobulin gene."; RL Gene 61:85-90(1987). RN [10] RP PROTEIN SEQUENCE OF 59-73, AND VARIANT GLN-61. RX PubMed=4737332; DOI=10.1016/0014-5793(73)80162-0; RA Brignon G., Ribadeau-Dumas B.; RT "Localization of the Glu-Gln substitution differentiating B and D genetic RT variants in the peptide chain of bovine beta lactoglobulin."; RL FEBS Lett. 33:73-76(1973). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 122-178. RX PubMed=3202951; DOI=10.1515/bchm3.1988.369.1.425; RA Ivanov V.N., Judinkova E.S., Gorodetsky S.I.; RT "Molecular cloning of bovine beta-lactoglobulin cDNA."; RL Biol. Chem. Hoppe-Seyler 369:425-429(1988). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-138, AND VARIANT VAL-134. RX PubMed=6897774; DOI=10.1089/dna.1982.1.375; RA Willis I.M., Stewart A.F., Caputo A., Thompson A.R., McKinlay A.G.; RT "Construction and identification by partial nucleotide sequence analysis of RT bovine casein and beta-lactoglobulin cDNA clones."; RL DNA 1:375-386(1982). RN [13] RP DISULFIDE BONDS. RX PubMed=4569282; DOI=10.1021/bi00774a017; RA McKenzie H.A., Ralston G.B., Shaw D.C.; RT "Location of sulfhydryl and disulfide groups in bovine beta-lactoglobulins RT and effects of urea."; RL Biochemistry 11:4539-4547(1972). RN [14] RP INTERACTION WITH LGB. RX PubMed=17991420; DOI=10.1016/j.bbamem.2007.10.010; RA Fluckinger M., Merschak P., Hermann M., Haertle T., Redl B.; RT "Lipocalin-interacting-membrane-receptor (LIMR) mediates cellular RT internalization of beta-lactoglobulin."; RL Biochim. Biophys. Acta 1778:342-347(2008). RN [15] RP ABSENCE OF INTERACTION WITH LMBR1L. RX PubMed=23964685; DOI=10.3109/09687688.2013.823018; RA Hesselink R.W., Findlay J.B.; RT "Expression, characterization and ligand specificity of lipocalin-1 RT interacting membrane receptor (LIMR)."; RL Mol. Membr. Biol. 30:327-337(2013). RN [16] RP VARIANT HIS-75. RA Shaw D.C.; RL Submitted (JAN-1973) to the PIR data bank. RN [17] RP COMPARISON OF X-RAY STRUCTURES. RX PubMed=1623143; DOI=10.1002/bip.360320425; RA Monaco H.L., Zanotti G.; RT "Three-dimensional structure and active site of three hydrophobic molecule- RT binding proteins with significant amino acid sequence similarity."; RL Biopolymers 32:457-465(1992). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND SUBUNIT. RX PubMed=9115437; DOI=10.1016/s0969-2126(97)00205-0; RA Brownlow S., Morais-Cabral J.H., Cooper R., Flower D.R., Yewdall S.J., RA Polikarpov I., North A.C.T., Sawyer L.; RT "Bovine beta-lactoglobulin at 1.8-A resolution -- still an enigmatic RT lipocalin."; RL Structure 5:481-495(1997). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS), AND SUBUNIT. RX PubMed=9760236; DOI=10.1021/bi981016t; RA Qin B.Y., Bewley M.C., Creamer L.K., Baker H.M., Baker E.N., Jameson G.B.; RT "Structural basis of the tanford transition of bovine beta-lactoglobulin."; RL Biochemistry 37:14014-14023(1998). RN [20] RP STRUCTURE BY NMR, AND SUBUNIT. RX PubMed=8601463; DOI=10.1016/0014-5793(96)00100-7; RA Molinari H., Ragona L., Varani L., Musco G., Consonni R., Zetta L., RA Monaco H.L.; RT "Partially folded structure of monomeric bovine beta-lactoglobulin."; RL FEBS Lett. 381:237-243(1996). RN [21] RP STRUCTURE BY NMR OF VARIANT A, AND SUBUNIT. RX PubMed=10595563; DOI=10.1110/ps.8.11.2541; RA Kuwata K., Hoshino M., Forge V., Era S., Batt C.A., Goto Y.; RT "Solution structure and dynamics of bovine beta-lactoglobulin A."; RL Protein Sci. 8:2541-2545(1999). CC -!- FUNCTION: Primary component of whey, it binds retinol and is probably CC involved in the transport of that molecule. CC -!- SUBUNIT: Under physiological conditions beta-lactoglobulin exists as an CC equilibrium mixture of monomeric and dimeric forms (PubMed:9115437, CC PubMed:9760236, PubMed:8601463, PubMed:10595563). Interaction with CC LMBR1L which mediates the endocytosis of LGB has been observed in CC PubMed:17991420, but not in PubMed:23964685 (PubMed:17991420, CC PubMed:23964685). {ECO:0000269|PubMed:10595563, CC ECO:0000269|PubMed:17991420, ECO:0000269|PubMed:23964685, CC ECO:0000269|PubMed:8601463, ECO:0000269|PubMed:9115437, CC ECO:0000269|PubMed:9760236}. CC -!- INTERACTION: CC P02754; P02754: LGB; NbExp=2; IntAct=EBI-9697387, EBI-9697387; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Synthesized in mammary gland and secreted in milk. CC -!- PTM: Alternate disulfide bonds occur in equal amounts in all variants CC examined. CC -!- ALLERGEN: Causes an allergic reaction in human. Is one of the causes of CC cow's milk allergy. CC -!- MISCELLANEOUS: The B variant sequence is shown. CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X14712; CAA32835.1; -; mRNA. DR EMBL; Z48305; CAA88303.1; -; Genomic_DNA. DR EMBL; DQ489319; ABF48380.1; -; Genomic_DNA. DR EMBL; BC108213; AAI08214.1; -; mRNA. DR EMBL; X52581; CAA36812.1; -; Genomic_DNA. DR EMBL; M19088; AAA30411.1; -; Genomic_DNA. DR EMBL; M27732; AAA30412.1; -; mRNA. DR EMBL; K01086; AAA30413.1; -; mRNA. DR PIR; S10179; LGBO. DR RefSeq; NP_776354.2; NM_173929.3. DR PDB; 1B0O; X-ray; 2.50 A; A=17-178. DR PDB; 1B8E; X-ray; 1.95 A; A=17-178. DR PDB; 1BEB; X-ray; 1.80 A; A/B=17-178. DR PDB; 1BSO; X-ray; 2.23 A; A=17-178. DR PDB; 1BSQ; X-ray; 2.22 A; A=17-178. DR PDB; 1BSY; X-ray; 2.24 A; A=17-178. DR PDB; 1CJ5; NMR; -; A=19-178. DR PDB; 1DV9; NMR; -; A=17-178. DR PDB; 1GX8; X-ray; 2.40 A; A=17-178. DR PDB; 1GX9; X-ray; 2.34 A; A=17-178. DR PDB; 1GXA; X-ray; 2.35 A; A=17-178. DR PDB; 1QG5; X-ray; 2.00 A; A=17-178. DR PDB; 1UZ2; X-ray; 1.95 A; X=17-178. DR PDB; 1YUP; X-ray; 2.10 A; D=18-176. DR PDB; 2AKQ; X-ray; 3.00 A; A/B/C/D=17-178. DR PDB; 2BLG; X-ray; 2.46 A; A=17-178. DR PDB; 2GJ5; X-ray; 2.40 A; A=17-178. DR PDB; 2Q2M; X-ray; 2.10 A; A=17-178. DR PDB; 2Q2P; X-ray; 2.96 A; A=17-178. DR PDB; 2Q39; X-ray; 2.50 A; A/B=17-178. DR PDB; 2R56; X-ray; 2.80 A; A/B=17-178. DR PDB; 3BLG; X-ray; 2.56 A; A=17-178. DR PDB; 3KZA; X-ray; 2.00 A; A/B=33-169. DR PDB; 3NPO; X-ray; 2.20 A; A=17-178. DR PDB; 3NQ3; X-ray; 1.90 A; A=17-178. DR PDB; 3NQ9; X-ray; 1.90 A; A=17-178. DR PDB; 3PH5; X-ray; 2.40 A; A/B=18-178. DR PDB; 3PH6; X-ray; 2.53 A; A/B=18-178. DR PDB; 3UEU; X-ray; 2.10 A; A=17-178. DR PDB; 3UEV; X-ray; 1.90 A; A=17-178. DR PDB; 3UEW; X-ray; 2.00 A; A=17-178. DR PDB; 3UEX; X-ray; 2.10 A; A=17-178. DR PDB; 4DQ3; X-ray; 1.95 A; A=17-178. DR PDB; 4DQ4; X-ray; 1.90 A; A=17-178. DR PDB; 4GNY; X-ray; 1.64 A; A=17-178. DR PDB; 4IB6; X-ray; 2.20 A; A=17-178. DR PDB; 4IB7; X-ray; 2.20 A; A=17-178. DR PDB; 4IB8; X-ray; 2.30 A; A=17-178. DR PDB; 4IB9; X-ray; 2.20 A; A=17-178. DR PDB; 4IBA; X-ray; 2.30 A; A=17-178. DR PDB; 4KII; X-ray; 1.85 A; A=17-178. DR PDB; 4LZU; X-ray; 2.40 A; A=17-178. DR PDB; 4LZV; X-ray; 2.44 A; A=17-178. DR PDB; 4Y0P; X-ray; 2.20 A; A=17-178. DR PDB; 4Y0Q; X-ray; 2.00 A; A=17-178. DR PDB; 4Y0R; X-ray; 2.30 A; A=17-178. DR PDB; 5HTD; X-ray; 2.50 A; A=17-178. DR PDB; 5HTE; X-ray; 2.40 A; A=17-178. DR PDB; 5IO5; X-ray; 2.85 A; A=17-178. DR PDB; 5IO7; X-ray; 2.85 A; A=17-178. DR PDB; 5K06; X-ray; 2.50 A; A=17-178. DR PDB; 5LKE; X-ray; 2.80 A; A=17-178. DR PDB; 5LKF; X-ray; 2.50 A; A=17-178. DR PDB; 5NUJ; X-ray; 2.60 A; A=17-178. DR PDB; 5NUK; X-ray; 1.70 A; A=17-178. DR PDB; 5NUM; X-ray; 2.30 A; A=17-178. DR PDB; 5NUN; X-ray; 1.95 A; A=17-178. DR PDB; 5Y5C; X-ray; 2.61 A; A/B=17-178. DR PDB; 6FXB; X-ray; 2.00 A; A/B/C/D=17-178. DR PDB; 6GE7; X-ray; 2.30 A; A=17-178. DR PDB; 6GF9; X-ray; 2.10 A; A=17-178. DR PDB; 6GFS; X-ray; 2.00 A; A=17-178. DR PDB; 6GHH; X-ray; 1.90 A; A=17-178. DR PDB; 6NKQ; X-ray; 2.30 A; A/B/C/D/E/F=1-178. DR PDB; 6QI6; X-ray; 2.00 A; A=17-178. DR PDB; 6QI7; X-ray; 2.50 A; A=17-178. DR PDB; 6QPD; X-ray; 2.00 A; A=17-178. DR PDB; 6QPE; X-ray; 2.20 A; A=17-178. DR PDB; 6RWP; X-ray; 2.10 A; A=17-178. DR PDB; 6RWQ; X-ray; 2.05 A; A=17-178. DR PDB; 6RWR; X-ray; 2.10 A; A=17-178. DR PDB; 6RYT; X-ray; 2.10 A; A/B=17-178. DR PDB; 6T42; X-ray; 1.95 A; AAA=17-178. DR PDB; 6XVE; X-ray; 2.15 A; A=17-178. DR PDB; 6ZSQ; X-ray; 2.00 A; AAA/BBB=17-178. DR PDB; 6ZSR; X-ray; 2.00 A; AAA/BBB=17-178. DR PDB; 7BF7; X-ray; 2.10 A; AAA=17-178. DR PDB; 7BF8; X-ray; 1.80 A; AAA/BBB=17-178. DR PDB; 7BF9; X-ray; 1.80 A; AAA=17-178. DR PDB; 7BGA; X-ray; 1.90 A; AAA=17-178. DR PDB; 7BGX; X-ray; 2.00 A; AAA=17-178. DR PDB; 7BGZ; X-ray; 2.40 A; AAA=17-178. DR PDB; 7BH0; X-ray; 2.10 A; AAA=17-178. DR PDB; 7ER3; X-ray; 2.60 A; A/B/C/D=17-178. DR PDB; 7KOT; X-ray; 1.74 A; A=17-178. DR PDB; 7KP5; X-ray; 2.40 A; AA1/BA1=17-178. DR PDB; 7NQB; X-ray; 2.01 A; AAA/BBB=17-178. DR PDB; 7Q17; X-ray; 1.80 A; AAA=17-178. DR PDB; 7Q18; X-ray; 1.80 A; AAA/BBB=17-178. DR PDB; 7Q19; X-ray; 1.55 A; AAA=17-178. DR PDB; 7Q2N; X-ray; 1.70 A; AAA/BBB=17-178. DR PDB; 7Q2O; X-ray; 1.80 A; AAA/BBB=17-178. DR PDB; 7Q2P; X-ray; 1.69 A; AAA/BBB=17-178. DR PDB; 7WQL; X-ray; 2.00 A; A/B=17-178. DR PDB; 7Z9Z; X-ray; 2.50 A; AAA=19-178. DR PDB; 7ZA0; X-ray; 2.10 A; AAA=17-178. DR PDB; 7ZCD; X-ray; 2.10 A; AAA=19-178. DR PDB; 7ZLF; X-ray; 2.10 A; AAA=19-178. DR PDBsum; 1B0O; -. DR PDBsum; 1B8E; -. DR PDBsum; 1BEB; -. DR PDBsum; 1BSO; -. DR PDBsum; 1BSQ; -. DR PDBsum; 1BSY; -. DR PDBsum; 1CJ5; -. DR PDBsum; 1DV9; -. DR PDBsum; 1GX8; -. DR PDBsum; 1GX9; -. DR PDBsum; 1GXA; -. DR PDBsum; 1QG5; -. DR PDBsum; 1UZ2; -. DR PDBsum; 1YUP; -. DR PDBsum; 2AKQ; -. DR PDBsum; 2BLG; -. DR PDBsum; 2GJ5; -. DR PDBsum; 2Q2M; -. DR PDBsum; 2Q2P; -. DR PDBsum; 2Q39; -. DR PDBsum; 2R56; -. DR PDBsum; 3BLG; -. DR PDBsum; 3KZA; -. DR PDBsum; 3NPO; -. DR PDBsum; 3NQ3; -. DR PDBsum; 3NQ9; -. DR PDBsum; 3PH5; -. DR PDBsum; 3PH6; -. DR PDBsum; 3UEU; -. DR PDBsum; 3UEV; -. DR PDBsum; 3UEW; -. DR PDBsum; 3UEX; -. DR PDBsum; 4DQ3; -. DR PDBsum; 4DQ4; -. DR PDBsum; 4GNY; -. DR PDBsum; 4IB6; -. DR PDBsum; 4IB7; -. DR PDBsum; 4IB8; -. DR PDBsum; 4IB9; -. DR PDBsum; 4IBA; -. DR PDBsum; 4KII; -. DR PDBsum; 4LZU; -. DR PDBsum; 4LZV; -. DR PDBsum; 4Y0P; -. DR PDBsum; 4Y0Q; -. DR PDBsum; 4Y0R; -. DR PDBsum; 5HTD; -. DR PDBsum; 5HTE; -. DR PDBsum; 5IO5; -. DR PDBsum; 5IO7; -. DR PDBsum; 5K06; -. DR PDBsum; 5LKE; -. DR PDBsum; 5LKF; -. DR PDBsum; 5NUJ; -. DR PDBsum; 5NUK; -. DR PDBsum; 5NUM; -. DR PDBsum; 5NUN; -. DR PDBsum; 5Y5C; -. DR PDBsum; 6FXB; -. DR PDBsum; 6GE7; -. DR PDBsum; 6GF9; -. DR PDBsum; 6GFS; -. DR PDBsum; 6GHH; -. DR PDBsum; 6NKQ; -. DR PDBsum; 6QI6; -. DR PDBsum; 6QI7; -. DR PDBsum; 6QPD; -. DR PDBsum; 6QPE; -. DR PDBsum; 6RWP; -. DR PDBsum; 6RWQ; -. DR PDBsum; 6RWR; -. DR PDBsum; 6RYT; -. DR PDBsum; 6T42; -. DR PDBsum; 6XVE; -. DR PDBsum; 6ZSQ; -. DR PDBsum; 6ZSR; -. DR PDBsum; 7BF7; -. DR PDBsum; 7BF8; -. DR PDBsum; 7BF9; -. DR PDBsum; 7BGA; -. DR PDBsum; 7BGX; -. DR PDBsum; 7BGZ; -. DR PDBsum; 7BH0; -. DR PDBsum; 7ER3; -. DR PDBsum; 7KOT; -. DR PDBsum; 7KP5; -. DR PDBsum; 7NQB; -. DR PDBsum; 7Q17; -. DR PDBsum; 7Q18; -. DR PDBsum; 7Q19; -. DR PDBsum; 7Q2N; -. DR PDBsum; 7Q2O; -. DR PDBsum; 7Q2P; -. DR PDBsum; 7WQL; -. DR PDBsum; 7Z9Z; -. DR PDBsum; 7ZA0; -. DR PDBsum; 7ZCD; -. DR PDBsum; 7ZLF; -. DR AlphaFoldDB; P02754; -. DR BMRB; P02754; -. DR PCDDB; P02754; -. DR SMR; P02754; -. DR DIP; DIP-29525N; -. DR MINT; P02754; -. DR STRING; 9913.ENSBTAP00000062602; -. DR BindingDB; P02754; -. DR ChEMBL; CHEMBL1075053; -. DR DrugCentral; P02754; -. DR Allergome; 164; Bos d 5. DR Allergome; 2739; Bos d 5.0101. DR CarbonylDB; P02754; -. DR GlyConnect; 70; 6 N-Linked glycans. DR GlyCosmos; P02754; No site information, 7 glycans. DR PaxDb; 9913-ENSBTAP00000019538; -. DR PeptideAtlas; P02754; -. DR ABCD; P02754; 1 sequenced antibody. DR Ensembl; ENSBTAT00000019538.6; ENSBTAP00000019538.6; ENSBTAG00000014678.6. DR GeneID; 280838; -. DR KEGG; bta:280838; -. DR CTD; 5047; -. DR VEuPathDB; HostDB:ENSBTAG00000014678; -. DR eggNOG; ENOG502T0EI; Eukaryota. DR GeneTree; ENSGT01050000244868; -. DR InParanoid; P02754; -. DR EvolutionaryTrace; P02754; -. DR PRO; PR:P02754; -. DR Proteomes; UP000009136; Chromosome 11. DR Bgee; ENSBTAG00000014678; Expressed in milk and 28 other cell types or tissues. DR ExpressionAtlas; P02754; baseline. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0036041; F:long-chain fatty acid binding; IDA:CAFA. DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW. DR CDD; cd19416; lipocalin_beta-LG-like; 1. DR Gene3D; 2.40.128.20; -; 1. DR InterPro; IPR002447; Blactoglobulin. DR InterPro; IPR012674; Calycin. DR InterPro; IPR002345; Lipocalin. DR InterPro; IPR022272; Lipocalin_CS. DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom. DR PANTHER; PTHR11430:SF117; GLYCODELIN; 1. DR PANTHER; PTHR11430; LIPOCALIN; 1. DR Pfam; PF00061; Lipocalin; 1. DR PRINTS; PR01172; BLCTOGLOBULN. DR PRINTS; PR00179; LIPOCALIN. DR SUPFAM; SSF50814; Lipocalins; 1. DR PROSITE; PS00213; LIPOCALIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Direct protein sequencing; Disulfide bond; KW Milk protein; Reference proteome; Retinol-binding; Secreted; Signal; KW Transport. FT SIGNAL 1..16 FT /evidence="ECO:0000269|PubMed:2340107, FT ECO:0000269|PubMed:4611888" FT CHAIN 17..178 FT /note="Beta-lactoglobulin" FT /id="PRO_0000017903" FT DISULFID 82..176 FT /evidence="ECO:0000269|PubMed:10595563, FT ECO:0000269|PubMed:4569282" FT DISULFID 122..137 FT /note="Alternate" FT /evidence="ECO:0000269|PubMed:4569282" FT DISULFID 122..135 FT /evidence="ECO:0000269|PubMed:10595563, FT ECO:0000269|PubMed:4569282" FT VARIANT 61 FT /note="E -> Q (in variant D)" FT /evidence="ECO:0000269|PubMed:4737332" FT VARIANT 72 FT /note="I -> L (in variant W)" FT /evidence="ECO:0000269|PubMed:2340107" FT VARIANT 75 FT /note="Q -> H (in variant C; found only in the Jersey FT breed)" FT /evidence="ECO:0000269|Ref.16" FT VARIANT 80 FT /note="G -> D (in variant A)" FT /evidence="ECO:0000269|PubMed:2701948, FT ECO:0000269|PubMed:3443305, ECO:0000269|PubMed:4611888" FT VARIANT 134 FT /note="A -> V (in variant A)" FT /evidence="ECO:0000269|PubMed:2701948, FT ECO:0000269|PubMed:3443305, ECO:0000269|PubMed:4611888, FT ECO:0000269|PubMed:6897774" FT CONFLICT 121 FT /note="F -> V (in Ref. 1; CAA32835)" FT /evidence="ECO:0000305" FT CONFLICT 136 FT /note="Q -> E (in Ref. 12)" FT /evidence="ECO:0000305" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:1B8E" FT HELIX 28..31 FT /evidence="ECO:0007829|PDB:4GNY" FT STRAND 36..44 FT /evidence="ECO:0007829|PDB:4GNY" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:4GNY" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:1UZ2" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:4GNY" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:5LKF" FT STRAND 70..78 FT /evidence="ECO:0007829|PDB:4GNY" FT STRAND 81..91 FT /evidence="ECO:0007829|PDB:4GNY" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:4GNY" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:5NUK" FT STRAND 107..113 FT /evidence="ECO:0007829|PDB:4GNY" FT STRAND 115..124 FT /evidence="ECO:0007829|PDB:4GNY" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:6NKQ" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:1BEB" FT STRAND 133..143 FT /evidence="ECO:0007829|PDB:4GNY" FT HELIX 146..156 FT /evidence="ECO:0007829|PDB:4GNY" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:6GHH" FT STRAND 163..166 FT /evidence="ECO:0007829|PDB:4GNY" FT HELIX 169..172 FT /evidence="ECO:0007829|PDB:4GNY" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:4GNY" SQ 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 //