LACB_BOVIN
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 03-AUG-2022, entry version 183.
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}.
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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 RefSeq; XP_015329083.1; XM_015473597.1.
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; 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 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; 7KOT; -.
DR PDBsum; 7KP5; -.
DR PDBsum; 7NQB; -.
DR AlphaFoldDB; P02754; -.
DR BMRB; P02754; -.
DR PCDDB; P02754; -.
DR SMR; P02754; -.
DR DIP; DIP-29525N; -.
DR MINT; P02754; -.
DR STRING; 9913.ENSBTAP00000019538; -.
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 PaxDb; P02754; -.
DR PeptideAtlas; P02754; -.
DR PRIDE; P02754; -.
DR ABCD; P02754; 1 sequenced antibody.
DR Ensembl; ENSBTAT00000019538; ENSBTAP00000019538; ENSBTAG00000014678.
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 OrthoDB; 1551422at2759; -.
DR EvolutionaryTrace; P02754; -.
DR PRO; PR:P02754; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000014678; Expressed in milk and 28 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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 DisProt; DP00193; -.
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; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01172; BLCTOGLOBULN.
DR SUPFAM; SSF50814; SSF50814; 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
