LACB_SHEEP
ID LACB_SHEEP Reviewed; 180 AA.
AC P67976; P02757;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Beta-lactoglobulin-1/B;
DE Short=Beta-LG;
DE Flags: Precursor;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (BLG 1 AND 2).
RX PubMed=3351935; DOI=10.1016/0022-2836(88)90614-6;
RA Ali S., Clark A.J.;
RT "Characterization of the gene encoding ovine beta-lactoglobulin. Similarity
RT to the genes for retinol binding protein and other secretory proteins.";
RL J. Mol. Biol. 199:415-426(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (BLG 1).
RX PubMed=3096387; DOI=10.1016/s0300-9084(86)80184-5;
RA Gaye P., Hue-Delahaie D., Mercier J.-C., Soulier S., Vilotte J.-L.,
RA Furet J.-P.;
RT "Ovine beta-lactoglobulin messenger RNA: nucleotide sequence and mRNA
RT levels during functional differentiation of the mammary gland.";
RL Biochimie 68:1097-1107(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (BLG 1).
RX PubMed=3194215; DOI=10.1093/nar/16.21.10379;
RA Harris S., Ali S., Anderson S., Archibald A.L., Clark A.J.;
RT "Complete nucleotide sequence of the genomic ovine beta-lactoglobulin
RT gene.";
RL Nucleic Acids Res. 16:10379-10380(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (BLG 1 AND 2).
RX PubMed=1976573; DOI=10.1016/0378-1119(90)90089-a;
RA Ali S., McClenaghan M., Simons J.P., Clark A.J.;
RT "Characterisation of the alleles encoding ovine beta-lactoglobulins A and
RT B.";
RL Gene 91:201-207(1990).
RN [5]
RP PROTEIN SEQUENCE OF 19-180 (BLG 2).
RX PubMed=6155855;
RA Preaux G., Braunitzer G., Kolde H.-J.;
RT "Primary structure of ovine beta-lactoglobulin.";
RL Arch. Int. Physiol. Biochim. 88:B45-B46(1980).
RN [6]
RP PROTEIN SEQUENCE OF 19-180 (BLG 3).
RX PubMed=2775495; DOI=10.1515/bchm3.1989.370.2.757;
RA Erhardt G., Godovac-Zimmermann J., Conti A.;
RT "Isolation and complete primary sequence of a new ovine wild-type beta-
RT lactoglobulin C.";
RL Biol. Chem. Hoppe-Seyler 370:757-762(1989).
CC -!- FUNCTION: Lactoglobulin is the primary component of whey, it binds
CC retinol and is probably 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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Alternate disulfide bonds occur in equal amounts.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; X04520; CAA28204.1; -; mRNA.
DR EMBL; X12817; CAA31305.1; -; Genomic_DNA.
DR EMBL; X07004; CAA30059.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X07005; CAA30059.1; JOINED; Genomic_DNA.
DR EMBL; X07006; CAA30059.1; JOINED; Genomic_DNA.
DR EMBL; X07007; CAA30059.1; JOINED; Genomic_DNA.
DR EMBL; X07008; CAA30059.1; JOINED; Genomic_DNA.
DR EMBL; X07009; CAA30059.1; JOINED; Genomic_DNA.
DR EMBL; M32236; AAA31510.1; -; Genomic_DNA.
DR EMBL; M32233; AAA31510.1; JOINED; Genomic_DNA.
DR EMBL; M32232; AAA31510.1; JOINED; Genomic_DNA.
DR EMBL; M32235; AAA31510.1; JOINED; Genomic_DNA.
DR PIR; JQ0749; LGSH.
DR RefSeq; NP_001009366.1; NM_001009366.1.
DR PDB; 4CK4; X-ray; 1.12 A; A/B=19-180.
DR PDB; 4NLI; X-ray; 1.90 A; A=19-180.
DR PDB; 4NLJ; X-ray; 1.40 A; A/B=19-180.
DR PDB; 6T44; X-ray; 2.00 A; AAA/BBB=19-180.
DR PDBsum; 4CK4; -.
DR PDBsum; 4NLI; -.
DR PDBsum; 4NLJ; -.
DR PDBsum; 6T44; -.
DR AlphaFoldDB; P67976; -.
DR SMR; P67976; -.
DR STRING; 9940.ENSOARP00000005471; -.
DR Allergome; 1257; Ovi a 5.
DR Ensembl; ENSOART00020007400; ENSOARP00020006122; ENSOARG00020004839.
DR GeneID; 443385; -.
DR KEGG; oas:443385; -.
DR CTD; 5047; -.
DR eggNOG; ENOG502T0EI; Eukaryota.
DR OrthoDB; 1551422at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019841; F:retinol binding; IEA:UniProtKB-KW.
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; Direct protein sequencing; Disulfide bond; Milk protein;
KW Reference proteome; Retinol-binding; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2775495,
FT ECO:0000269|PubMed:6155855"
FT CHAIN 19..180
FT /note="Beta-lactoglobulin-1/B"
FT /id="PRO_0000017910"
FT DISULFID 84..178
FT DISULFID 124..139
FT /note="Alternate"
FT DISULFID 124..137
FT VARIANT 38
FT /note="H -> Y (in lactoglobulin 2=A and 3=C)"
FT VARIANT 166
FT /note="R -> Q (in lactoglobulin 3=C)"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:4NLJ"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:4NLJ"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4NLJ"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4NLJ"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:4NLJ"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:4NLJ"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:4NLJ"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:4NLJ"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:4NLJ"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4NLJ"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:4NLJ"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:4NLJ"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4NLJ"
FT HELIX 171..174
FT /evidence="ECO:0007829|PDB:4NLJ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:4NLJ"
SQ SEQUENCE 180 AA; 19921 MW; BABC82E89E757333 CRC64;
MKCLLLALGL ALACGVQAII VTQTMKGLDI QKVAGTWHSL AMAASDISLL DAQSAPLRVY
VEELKPTPEG NLEILLQKWE NGECAQKKII AEKTKIPAVF KIDALNENKV LVLDTDYKKY
LLFCMENSAE PEQSLACQCL VRTPEVDNEA LEKFDKALKA LPMHIRLAFN PTQLEGQCHV
