LACB1_HORSE
ID LACB1_HORSE Reviewed; 180 AA.
AC P02758; Q28394;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Beta-lactoglobulin-1;
DE Short=Beta-LG-1;
DE AltName: Full=Beta-lactoglobulin I;
DE Short=BLGI;
DE Flags: Precursor;
GN Name=LGB1;
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 PROTEIN SEQUENCE OF 19-180.
RX PubMed=6526379; DOI=10.1515/bchm2.1984.365.2.1393;
RA Conti A., Godovac-Zimmermann J., Liberatori J., Braunitzer G.;
RT "The primary structure of monomeric beta-lactoglobulin I from horse
RT colostrum (Equus caballus, Perissodactyla).";
RL Hoppe-Seyler's Z. Physiol. Chem. 365:1393-1401(1984).
RN [3]
RP SEQUENCE REVISION TO 95; 99; 104 AND 112.
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; U60356; AAB03511.1; -; mRNA.
DR PIR; A03222; LGHO.
DR RefSeq; NP_001075962.1; NM_001082493.2.
DR PDB; 3KZA; X-ray; 2.00 A; A/B=19-180.
DR PDBsum; 3KZA; -.
DR AlphaFoldDB; P02758; -.
DR SMR; P02758; -.
DR STRING; 9796.ENSECAP00000007932; -.
DR Allergome; 1499; Equ c BLG.
DR PaxDb; P02758; -.
DR PeptideAtlas; P02758; -.
DR PRIDE; P02758; -.
DR GeneID; 100034193; -.
DR KEGG; ecb:100034193; -.
DR CTD; 100034193; -.
DR HOGENOM; CLU_094061_5_0_1; -.
DR InParanoid; P02758; -.
DR OMA; WEDNRCV; -.
DR OrthoDB; 1551422at2759; -.
DR TreeFam; TF342475; -.
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 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:6526379"
FT CHAIN 19..180
FT /note="Beta-lactoglobulin-1"
FT /id="PRO_0000017906"
FT DISULFID 84..178
FT DISULFID 124..137
FT CONFLICT 54
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:3KZA"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3KZA"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3KZA"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:3KZA"
SQ SEQUENCE 180 AA; 20345 MW; A57A477E9D618BFD CRC64;
MKCLLLALGL ALMCGIQATN IPQTMQDLDL QEVAGKWHSV AMAASDISLL DSESAPLRVY
IEKLRPTPED NLEIILREGE NKGCAEKKIF AEKTESPAEF KINYLDEDTV FALDTDYKNY
LFLCMKNAAT PGQSLVCQYL ARTQMVDEEI MEKFRRALQP LPGRVQIVPD LTRMAERCRI
