ID   ICYA_MANSE              Reviewed;         189 AA.
AC   P00305;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Insecticyanin-A;
DE            Short=INS-a;
DE   AltName: Full=Blue biliprotein;
GN   Name=INSA;
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   PROTEIN SEQUENCE.
RC   TISSUE=Fifth instar larvae;
RX   PubMed=6386809; DOI=10.1016/s0021-9258(18)90671-x;
RA   Riley C.T., Barbeau B.K., Keim P.S., Kezdy F.J., Heinrikson R.L., Law J.H.;
RT   "The covalent protein structure of insecticyanin, a blue biliprotein from
RT   the hemolymph of the tobacco hornworm, Manduca sexta L.";
RL   J. Biol. Chem. 259:13159-13165(1984).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=3608987; DOI=10.1002/j.1460-2075.1987.tb02401.x;
RA   Holden H.M., Rypniewski W.R., Law J.H., Rayment I.;
RT   "The molecular structure of insecticyanin from the tobacco hornworm Manduca
RT   sexta L. at 2.6-A resolution.";
RL   EMBO J. 6:1565-1570(1987).
RN   [3]
RP   IDENTIFICATION OF CHROMOPHORE.
RX   PubMed=4096898; DOI=10.1021/bi00326a017;
RA   Goodman W.G., Adams B., Trost J.T.;
RT   "Purification and characterization of a biliverdin-associated protein from
RT   the hemolymph of Manduca sexta.";
RL   Biochemistry 24:1168-1175(1985).
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   PIR; A03225; CUWOI.
DR   PDB; 1Z24; X-ray; 2.60 A; A=1-189.
DR   PDBsum; 1Z24; -.
DR   AlphaFoldDB; P00305; -.
DR   SMR; P00305; -.
DR   EvolutionaryTrace; P00305; -.
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.
FT   CHAIN           1..189
FT                   /note="Insecticyanin-A"
FT                   /id="PRO_0000201012"
FT   DISULFID        9..119
FT                   /evidence="ECO:0000269|PubMed:6386809"
FT   DISULFID        43..175
FT                   /evidence="ECO:0000269|PubMed:6386809"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          25..32
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          42..50
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          55..63
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          66..76
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          86..94
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          110..121
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   TURN            123..125
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          126..140
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   HELIX           144..154
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   TURN            155..159
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   HELIX           162..164
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:1Z24"
FT   STRAND          178..187
FT                   /evidence="ECO:0007829|PDB:1Z24"
SQ   SEQUENCE   189 AA;  21379 MW;  4907E45DEB72873D CRC64;
     GDIFYPGYCP DVKPVNDFDL SAFAGAWHEI AKLPLENENQ GKCTIAEYKY DGKKASVYNS
     FVSNGVKEYM EGDLEIAPDA KYTKQGKYVM TFKFGQRVVN LVPWVLATDY KNYAINYNCD
     YHPDKKAHSI HAWILSKSKV LEGNTKEVVD NVLKTFSHLI DASKFISNDF SEAACQYSTT
     YSLTGPDRH