ID   LACB2_EQUAS             Reviewed;         163 AA.
AC   P19647;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Beta-lactoglobulin-2;
DE            Short=Beta-LG-2;
DE   AltName: Full=Beta-lactoglobulin II, minor monomeric;
GN   Name=LGB2;
OS   Equus asinus (Donkey) (Equus africanus asinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9793;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Milk;
RX   PubMed=2291812; DOI=10.1515/bchm3.1990.371.2.871;
RA   Godovac-Zimmermann J., Conti A., Sheil M., Napolitano L.;
RT   "Covalent structure of the minor monomeric beta-lactoglobulin II component
RT   from donkey milk.";
RL   Biol. Chem. Hoppe-Seyler 371:871-879(1990).
RN   [2]
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, DISULFIDE BONDS, AND VARIANTS D
RP   PRO-110 AND ASP-162.
RC   STRAIN=Ragusana; TISSUE=Milk;
RX   PubMed=17377935; DOI=10.1002/rcm.2978;
RA   Cunsolo V., Costa A., Saletti R., Muccilli V., Foti S.;
RT   "Detection and sequence determination of a new variant beta-lactoglobulin
RT   II from donkey.";
RL   Rapid Commun. Mass Spectrom. 21:1438-1446(2007).
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   -!- MASS SPECTROMETRY: Mass=18311; Method=Electrospray; Note=Variant D.;
CC       Evidence={ECO:0000269|PubMed:17377935};
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   PIR; S11538; S11538.
DR   AlphaFoldDB; P19647; -.
DR   SMR; P19647; -.
DR   PRIDE; P19647; -.
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   Direct protein sequencing; Disulfide bond; Milk protein; Retinol-binding;
KW   Secreted; Transport.
FT   CHAIN           1..163
FT                   /note="Beta-lactoglobulin-2"
FT                   /id="PRO_0000201016"
FT   DISULFID        66..161
FT                   /evidence="ECO:0000269|PubMed:17377935"
FT   DISULFID        106..120
FT                   /evidence="ECO:0000269|PubMed:17377935"
FT   VARIANT         110
FT                   /note="C -> P (in D)"
FT                   /evidence="ECO:0000269|PubMed:17377935"
FT   VARIANT         162
FT                   /note="G -> D (in D)"
FT                   /evidence="ECO:0000269|PubMed:17377935"
SQ   SEQUENCE   163 AA;  18263 MW;  45C7A4EED1A7F690 CRC64;
     TDIPQTMQDL DLQEVAGRWH SVAMVASDIS LLDSESAPLR VYVEELRPTP EGNLEIILRE
     GANHVCVERN IVAQKTEDPA VFTVNYQGER KISVLDTDYA HYMFFCVGPC LPSAEHGMVC
     QYLARTQKVD EEVMEKFSRA LQPLPGHVQI IQDPSGGQER CGF