LACB_CAPHI
ID LACB_CAPHI Reviewed; 180 AA.
AC P02756;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Beta-lactoglobulin;
DE Short=Beta-LG;
DE Flags: Precursor;
GN Name=LGB;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Ssp. aegagrus; TISSUE=Mammary gland;
RX PubMed=8226387; DOI=10.2527/1993.71102832x;
RA Folch J.M., Coll A., Sanchez A.;
RT "Cloning and sequencing of the cDNA encoding goat beta-lactoglobulin.";
RL J. Anim. Sci. 71:2832-2832(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Kim J., Kim A., Kim J., Yu M.;
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7699130; DOI=10.3168/jds.s0022-0302(94)77290-8;
RA Folch J., Coll A., Sanchez A.;
RT "Complete sequence of the caprine beta-lactoglobulin gene.";
RL J. Dairy Sci. 77:3493-3497(1994).
RN [4]
RP PROTEIN SEQUENCE OF 19-180.
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).
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 (By similarity).
CC Interaction with LMBR1L is controversial (By similarity).
CC {ECO:0000250|UniProtKB:P02754}.
CC -!- INTERACTION:
CC P02756; P02756: LGB; NbExp=3; IntAct=EBI-9697367, EBI-9697367;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Synthesized in mammary gland and secreted in milk.
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; X58471; CAA41385.1; -; mRNA.
DR EMBL; Z19569; CAA79623.1; -; mRNA.
DR EMBL; Z19570; CAA79624.1; -; Genomic_DNA.
DR EMBL; Z33881; CAA83946.1; -; Genomic_DNA.
DR PIR; A03220; LGGT.
DR RefSeq; NP_001272468.1; NM_001285539.1.
DR RefSeq; XP_017910176.1; XM_018054687.1.
DR RefSeq; XP_017910177.1; XM_018054688.1.
DR RefSeq; XP_017910178.1; XM_018054689.1.
DR PDB; 4OMW; X-ray; 2.30 A; A/B/C/D=19-180.
DR PDB; 4OMX; X-ray; 2.30 A; A=19-180.
DR PDB; 4TLJ; X-ray; 1.17 A; A/B=19-180.
DR PDB; 4Y0S; X-ray; 1.90 A; A=19-180.
DR PDB; 7LWC; X-ray; 3.00 A; A/B=19-180.
DR PDBsum; 4OMW; -.
DR PDBsum; 4OMX; -.
DR PDBsum; 4TLJ; -.
DR PDBsum; 4Y0S; -.
DR PDBsum; 7LWC; -.
DR AlphaFoldDB; P02756; -.
DR SMR; P02756; -.
DR MINT; P02756; -.
DR STRING; 9925.ENSCHIP00000012525; -.
DR Allergome; 1256; Cap h 5.
DR PRIDE; P02756; -.
DR Ensembl; ENSCHIT00010022089; ENSCHIP00010015740; ENSCHIG00010011456.
DR GeneID; 100861187; -.
DR KEGG; chx:100861187; -.
DR CTD; 5047; -.
DR OrthoDB; 1551422at2759; -.
DR Proteomes; UP000291000; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:511095"
FT CHAIN 19..180
FT /note="Beta-lactoglobulin"
FT /id="PRO_0000017905"
FT DISULFID 84..178
FT DISULFID 124..139
FT /note="Alternate"
FT DISULFID 124..137
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:4OMW"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:4TLJ"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:7LWC"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:4TLJ"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:4TLJ"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4TLJ"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4TLJ"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:4TLJ"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:4TLJ"
SQ 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
