LACB2_HORSE
ID LACB2_HORSE Reviewed; 181 AA.
AC P07380; Q28395; Q549K0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Beta-lactoglobulin-2;
DE Short=Beta-LG-2;
DE AltName: Full=Beta-lactoglobulin II;
DE Short=BLGII;
DE AltName: Full=Minor monomeric beta-lactoglobulin;
DE Flags: Precursor;
GN Name=LGB2;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Masel A.M., Bell K.T.;
RT "Comparison of the equine I and II beta-lactoglobulin genes.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Masel A.M., Brandon R.B., Bell T.K.;
RT "Nucleotide sequence of the equine beta-lactoglobulin gene.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 19-181.
RX PubMed=4040766; DOI=10.1515/bchm3.1985.366.1.601;
RA Godovac-Zimmermann J., Conti A., Liberatori J., Braunitzer G.;
RT "The amino-acid sequence of beta-lactoglobulin II from horse colostrum
RT (Equus caballus, Perissodactyla): beta-lactoglobulins are retinol-binding
RT proteins.";
RL Biol. Chem. Hoppe-Seyler 366:601-608(1985).
RN [4]
RP SEQUENCE REVISION TO 96-140.
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).
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: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; U60978; AAB03622.1; -; mRNA.
DR EMBL; AF107201; AAC95385.1; -; Genomic_DNA.
DR PIR; A24654; LGHO2.
DR PIR; S14720; S14720.
DR RefSeq; NP_001075963.1; NM_001082494.1.
DR AlphaFoldDB; P07380; -.
DR SMR; P07380; -.
DR STRING; 9796.ENSECAP00000010660; -.
DR Allergome; 1499; Equ c BLG.
DR PaxDb; P07380; -.
DR PeptideAtlas; P07380; -.
DR GeneID; 100034194; -.
DR KEGG; ecb:100034194; -.
DR CTD; 100034194; -.
DR InParanoid; P07380; -.
DR OrthoDB; 1551422at2759; -.
DR Proteomes; UP000002281; Unplaced.
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 Direct protein sequencing; Disulfide bond; Milk protein;
KW Reference proteome; Retinol-binding; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:4040766"
FT CHAIN 19..181
FT /note="Beta-lactoglobulin-2"
FT /id="PRO_0000017907"
FT DISULFID 84..179
FT /evidence="ECO:0000250"
FT DISULFID 124..138
FT /evidence="ECO:0000250"
FT CONFLICT 54..55
FT /note="SV -> EA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 20123 MW; 88EF51971A4A644A CRC64;
MKCLLLALGL SLMCGNQATD IPQTMQDLDL QEVAGRWHSV AMVASDISLL DSESVPLRVY
VEELRPTPEG NLEIILREGA NHACVERNIV AQKTEDPAVF TVNYQGERKI SVLDTDYAHY
MFFCVGPPLP SAEHGMVCQY LARTQKVDEE VMEKFSRALQ PLPGRVQIVQ DPSGGQERCG
F
