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Beta-lactoglobulin (Beta-LG)

 LACB_CAPHI              Reviewed;         180 AA.
P02756;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 2.
12-APR-2017, entry version 100.
RecName: Full=Beta-lactoglobulin;
Short=Beta-LG;
Flags: Precursor;
Name=LGB;
Capra hircus (Goat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Capra.
NCBI_TaxID=9925;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Ssp. aegagrus; TISSUE=Mammary gland;
PubMed=8226387;
Folch J.M., Coll A., Sanchez A.;
"Cloning and sequencing of the cDNA encoding goat beta-
lactoglobulin.";
J. Anim. Sci. 71:2832-2832(1993).
[2]
NUCLEOTIDE SEQUENCE.
Kim J., Kim A., Kim J., Yu M.;
Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=7699130; DOI=10.3168/jds.S0022-0302(94)77290-8;
Folch J., Coll A., Sanchez A.;
"Complete sequence of the caprine beta-lactoglobulin gene.";
J. Dairy Sci. 77:3493-3497(1994).
[4]
PROTEIN SEQUENCE OF 19-180.
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).
-!- 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=3; IntAct=EBI-9697367, EBI-9697367;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Synthesized in mammary gland and secreted in
milk.
-!- PTM: Alternate disulfide bonds occur in equal amounts.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
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EMBL; X58471; CAA41385.1; -; mRNA.
EMBL; Z19569; CAA79623.1; -; mRNA.
EMBL; Z19570; CAA79624.1; -; Genomic_DNA.
EMBL; Z33881; CAA83946.1; -; Genomic_DNA.
PIR; A03220; LGGT.
RefSeq; NP_001272468.1; NM_001285539.1.
RefSeq; XP_017910176.1; XM_018054687.1.
RefSeq; XP_017910177.1; XM_018054688.1.
RefSeq; XP_017910178.1; XM_018054689.1.
UniGene; Chi.595; -.
PDB; 4OMW; X-ray; 2.30 A; A/B/C/D=19-180.
PDB; 4OMX; X-ray; 2.30 A; A=19-180.
PDB; 4TLJ; X-ray; 1.17 A; A/B=19-180.
PDB; 4Y0S; X-ray; 1.90 A; A=19-180.
PDBsum; 4OMW; -.
PDBsum; 4OMX; -.
PDBsum; 4TLJ; -.
PDBsum; 4Y0S; -.
ProteinModelPortal; P02756; -.
SMR; P02756; -.
Allergome; 1256; Cap h 5.
PRIDE; P02756; -.
GeneID; 100861187; -.
KEGG; chx:100861187; -.
CTD; 5047; -.
HOVERGEN; HBG104361; -.
OrthoDB; EOG091G0M2T; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
GO; GO:0006810; P:transport; 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.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR01172; BLCTOGLOBULN.
PRINTS; PR00179; LIPOCALIN.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond; Milk protein;
Retinol-binding; Secreted; Signal; Transport.
SIGNAL 1 18 {ECO:0000269|PubMed:511095}.
CHAIN 19 180 Beta-lactoglobulin.
/FTId=PRO_0000017905.
DISULFID 84 178
DISULFID 124 139 Alternate.
DISULFID 124 137
HELIX 23 26 {ECO:0000244|PDB:4OMW}.
HELIX 30 33 {ECO:0000244|PDB:4TLJ}.
STRAND 38 46 {ECO:0000244|PDB:4TLJ}.
HELIX 47 49 {ECO:0000244|PDB:4TLJ}.
STRAND 59 66 {ECO:0000244|PDB:4TLJ}.
STRAND 72 80 {ECO:0000244|PDB:4TLJ}.
STRAND 83 93 {ECO:0000244|PDB:4TLJ}.
STRAND 99 104 {ECO:0000244|PDB:4TLJ}.
STRAND 107 115 {ECO:0000244|PDB:4TLJ}.
STRAND 117 126 {ECO:0000244|PDB:4TLJ}.
HELIX 131 134 {ECO:0000244|PDB:4TLJ}.
STRAND 136 145 {ECO:0000244|PDB:4TLJ}.
HELIX 148 157 {ECO:0000244|PDB:4TLJ}.
TURN 158 160 {ECO:0000244|PDB:4TLJ}.
STRAND 165 168 {ECO:0000244|PDB:4TLJ}.
HELIX 171 175 {ECO:0000244|PDB:4TLJ}.
HELIX 177 179 {ECO:0000244|PDB:4TLJ}.
SEQUENCE 180 AA; 19976 MW; C2449BB02A1A80F1 CRC64;
MKCLLLALGL ALACGIQAII VTQTMKGLDI QKVAGTWYSL AMAASDISLL DAQSAPLRVY
VEELKPTPEG NLEILLQKWE NGECAQKKII AEKTKIPAVF KIDALNENKV LVLDTDYKKY
LLFCMENSAE PEQSLACQCL VRTPEVDKEA LEKFDKALKA LPMHIRLAFN PTQLEGQCHV


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