ID   ICYB_MANSE              Reviewed;         206 AA.
AC   Q00630;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Insecticyanin-B;
DE            Short=INS-b;
DE   AltName: Full=Blue biliprotein;
DE   Flags: Precursor;
GN   Name=INSB;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1572353; DOI=10.1111/j.1432-1033.1992.tb16805.x;
RA   Li W., Riddiford L.M.;
RT   "Two distinct genes encode two major isoelectric forms of insecticyanin in
RT   the tobacco hornworm, Manduca sexta.";
RL   Eur. J. Biochem. 205:491-499(1992).
CC   -!- FUNCTION: This protein binds a chromophore: biliverdin IX, isomer
CC       gamma. Mixed with lipoprotein-bound carotenes, this blue protein
CC       provides hornworms with their green cryptic coloration which serves a
CC       camouflage.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized only in the caterpillars, apparently by
CC       the epidermis and secreted into the hemolymph. The protein is passed
CC       over from the larval hemolymph to that of pupae and adults and is
CC       sequestered in the eggs.
CC   -!- DOMAIN: The molecule consist primarily of eight antiparallel beta-
CC       pleated strands, which enclose a hydrophobic pocket, and an alpha-
CC       helix.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; X64715; CAA45970.1; -; Genomic_DNA.
DR   PIR; S22401; S22401.
DR   AlphaFoldDB; Q00630; -.
DR   SMR; Q00630; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Pigment; Secreted; Signal.
FT   SIGNAL          1..17
FT   CHAIN           18..206
FT                   /note="Insecticyanin-B"
FT                   /id="PRO_0000017902"
FT   DISULFID        26..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        60..192
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   206 AA;  23182 MW;  501DAC047B54E8B8 CRC64;
     MQRFLVFTIV AVATAAAGDI FYPGYCPDVK PVDDFDLSAF AGAWHEIAKL PLENENQGKC
     TIAEYKYDGK KASVYNSFVV NGVKEYMEGD LEIAPDAKYT KQGKYVMTFK FGQRVVNLVP
     WVLATDYKNY AINYNCNYHP DKKAHSIHAW ILSKSKVLEG NTKEVVDNVL KTFSHLIDAS
     KFISNDFSEA ACQYSTTYSL TGPDRH