LACB_PIG
ID LACB_PIG Reviewed; 178 AA.
AC P04119; Q53Z18;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Beta-lactoglobulin-1A/1C;
DE AltName: Full=Beta-lactoglobulin IA/IC;
DE Short=Beta-LG;
DE Flags: Precursor;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=1503260; DOI=10.1111/j.1365-2052.1992.tb00139.x;
RA Alexander L.J., Beattie C.W.;
RT "Sequence of porcine beta-lactoglobulin cDNA.";
RL Anim. Genet. 23:263-265(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RA Larsen K., Hedegaard J., Bendixen C.;
RT "Porcine beta-lactoglobulin mRNA.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 19-178.
RX PubMed=3790256; DOI=10.1515/bchm3.1986.367.2.871;
RA Conti A., Godovac-Zimmermann J., Pirchner F., Liberatori J., Braunitzer G.;
RT "Pig beta-lactoglobulin I (Sus scrofa domestica, Artiodactyla). The primary
RT structure of the major component.";
RL Biol. Chem. Hoppe-Seyler 367:871-878(1986).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=7231399; DOI=10.1007/bf02354824;
RA Bell K., McKenzie H.A., Shaw D.C.;
RT "Porcine beta-lactoglobulin A and C. Occurrence, isolation and chemical
RT properties.";
RL Mol. Cell. Biochem. 35:103-111(1981).
RN [5]
RP SEQUENCE REVISION TO 87; 128; 131; 137 AND 139.
RX PubMed=2009291; DOI=10.1016/0167-4838(91)90521-z;
RA Halliday J.A., Bell K., Shaw D.C.;
RT "The complete amino acid sequence of feline beta-lactoglobulin II and a
RT partial revision of the equine beta-lactoglobulin II sequence.";
RL Biochim. Biophys. Acta 1077:25-30(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS).
RX PubMed=11856834; DOI=10.1107/s0907444902000616;
RA Hoedemaeker F.J., Visschers R.W., Alting A.C., de Kruif K.G., Kuil M.E.,
RA Abrahams J.P.;
RT "A novel pH-dependent dimerization motif in beta-lactoglobulin from pig
RT (Sus scrofa).";
RL Acta Crystallogr. D 58:480-486(2002).
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 -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; X54976; CAA38720.1; -; mRNA.
DR EMBL; AY372187; AAQ74978.1; -; mRNA.
DR PIR; A45542; A45542.
DR RefSeq; NP_998919.1; NM_213754.2.
DR RefSeq; XP_013849407.1; XM_013993953.1.
DR PDB; 1EXS; X-ray; 2.39 A; A=19-178.
DR PDBsum; 1EXS; -.
DR AlphaFoldDB; P04119; -.
DR SMR; P04119; -.
DR STRING; 9823.ENSSSCP00000006164; -.
DR PaxDb; P04119; -.
DR PeptideAtlas; P04119; -.
DR Ensembl; ENSSSCT00025055905; ENSSSCP00025023695; ENSSSCG00025041122.
DR Ensembl; ENSSSCT00045008980; ENSSSCP00045006104; ENSSSCG00045005411.
DR Ensembl; ENSSSCT00065017180; ENSSSCP00065007039; ENSSSCG00065012892.
DR GeneID; 396596; -.
DR KEGG; ssc:396596; -.
DR CTD; 5047; -.
DR eggNOG; ENOG502T0EI; Eukaryota.
DR HOGENOM; CLU_094061_5_0_1; -.
DR InParanoid; P04119; -.
DR OMA; GRCAEQK; -.
DR OrthoDB; 1551422at2759; -.
DR TreeFam; TF342475; -.
DR EvolutionaryTrace; P04119; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P04119; SS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:3790256"
FT CHAIN 19..178
FT /note="Beta-lactoglobulin-1A/1C"
FT /id="PRO_0000017909"
FT DISULFID 84..176
FT DISULFID 124..137
FT VARIANT 27
FT /note="E -> D (in variant C)"
FT VARIANT 86
FT /note="Q -> H (in variant C)"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:1EXS"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 107..115
FT /evidence="ECO:0007829|PDB:1EXS"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1EXS"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1EXS"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1EXS"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1EXS"
SQ SEQUENCE 178 AA; 19734 MW; 180062EB6CDCBD8D CRC64;
MRCLLLTLGL ALLCGVQAVE VTPIMTELDT QKVAGTWHTV AMAVSDVSLL DAKSSPLKAY
VEGLKPTPEG DLEILLQKRE NDKCAQEVLL AKKTDIPAVF KINALDENQL FLLDTDYDSH
LLLCMENSAS PEHSLVCQSL ARTLEVDDQI REKFEDALKT LSVPMRILPA QLEEQCRV
