ID   BBP_PIEBR               Reviewed;         189 AA.
AC   P09464;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Bilin-binding protein;
DE            Short=BBP;
DE   Flags: Precursor;
OS   Pieris brassicae (White butterfly) (Large white butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Pieridae; Pierinae; Pieris.
OX   NCBI_TaxID=7116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8112337; DOI=10.1111/j.1432-1033.1994.tb18567.x;
RA   Schmidt F.S., Skerra A.;
RT   "The bilin-binding protein of Pieris brassicae. cDNA sequence and
RT   regulation of expression reveal distinct features of this insect pigment
RT   protein.";
RL   Eur. J. Biochem. 219:855-863(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 16-189, DISULFIDE BONDS, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=3202956; DOI=10.1515/bchm3.1988.369.1.497;
RA   Suter F., Kayser H., Zuber H.;
RT   "The complete amino-acid sequence of the bilin-binding protein from Pieris
RT   brassicae and its similarity to a family of serum transport proteins like
RT   the retinol-binding proteins.";
RL   Biol. Chem. Hoppe-Seyler 369:497-505(1988).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX   PubMed=3430616; DOI=10.1016/0022-2836(87)90296-8;
RA   Huber M., Schneider M., Mayr I., Mueller R., Deutzmann R., Suter F.,
RA   Zuber H., Falk H., Kayser H.;
RT   "Molecular structure of the bilin binding protein (BBP) from Pieris
RT   brassicae after refinement at 2.0-A resolution.";
RL   J. Mol. Biol. 198:499-513(1987).
CC   -!- FUNCTION: This protein binds the blue pigments bilins.
CC       {ECO:0000269|PubMed:3202956}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:3430616}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3202956}.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X76568; CAA54063.1; -; mRNA.
DR   PIR; S41410; S41410.
DR   PDB; 1BBP; X-ray; 2.00 A; A/B/C/D=16-188.
DR   PDB; 1KXO; X-ray; 1.80 A; A=16-189.
DR   PDB; 1LKE; X-ray; 1.90 A; A=16-189.
DR   PDB; 1LNM; X-ray; 1.90 A; A=16-189.
DR   PDB; 1N0S; X-ray; 2.00 A; A/B=16-189.
DR   PDB; 1T0V; NMR; -; A=16-189.
DR   PDBsum; 1BBP; -.
DR   PDBsum; 1KXO; -.
DR   PDBsum; 1LKE; -.
DR   PDBsum; 1LNM; -.
DR   PDBsum; 1N0S; -.
DR   PDBsum; 1T0V; -.
DR   AlphaFoldDB; P09464; -.
DR   SMR; P09464; -.
DR   EvolutionaryTrace; P09464; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031409; F:pigment binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR003057; Invtbrt_color.
DR   InterPro; IPR022271; Lipocalin_ApoD.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR   PRINTS; PR01273; INVTBRTCOLOR.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bile pigment; Chromophore; Direct protein sequencing;
KW   Disulfide bond; Pigment; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:3202956"
FT   CHAIN           16..189
FT                   /note="Bilin-binding protein"
FT                   /id="PRO_0000017880"
FT   DISULFID        23..130
FT                   /evidence="ECO:0000269|PubMed:3202956"
FT   DISULFID        57..185
FT                   /evidence="ECO:0000269|PubMed:3202956"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   STRAND          39..46
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   HELIX           48..54
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   STRAND          56..64
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   STRAND          66..77
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   STRAND          80..90
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   STRAND          98..104
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   STRAND          110..119
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   STRAND          121..131
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   TURN            134..136
FT                   /evidence="ECO:0007829|PDB:1T0V"
FT   STRAND          137..151
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   HELIX           154..163
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:1KXO"
FT   HELIX           182..185
FT                   /evidence="ECO:0007829|PDB:1BBP"
SQ   SEQUENCE   189 AA;  21306 MW;  DDC2B53072E63412 CRC64;
     MQYLIVLALV AAASANVYHD GACPEVKPVD NFDWSNYHGK WWEVAKYPNS VEKYGKCGWA
     EYTPEGKSVK VSNYHVIHGK EYFIEGTAYP VGDSKIGKIY HKLTYGGVTK ENVFNVLSTD
     NKNYIIGYYC KYDEDKKGHQ DFVWVLSRSK VLTGEAKTAV ENYLIGSPVV DSQKLVYSDF
     SEAACKVNN