ID   PBP_ANTPO               Reviewed;         163 AA.
AC   P20797;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Pheromone-binding protein;
DE            Short=PBP;
DE   Flags: Precursor;
OS   Antheraea polyphemus (Polyphemus moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Saturniidae; Saturniinae; Saturniini; Antheraea.
OX   NCBI_TaxID=7120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2806547; DOI=10.1016/0014-5793(89)81751-x;
RA   Raming K., Krieger J., Breer H.;
RT   "Molecular cloning of an insect pheromone-binding protein.";
RL   FEBS Lett. 256:215-218(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-56.
RX   PubMed=2010751; DOI=10.1002/neu.480220108;
RA   Vogt R.G., Prestwich G.D., Lerner M.R.;
RT   "Odorant-binding-protein subfamilies associate with distinct classes of
RT   olfactory receptor neurons in insects.";
RL   J. Neurobiol. 22:74-84(1991).
RN   [3]
RP   STRUCTURE BY NMR OF 22-163, AND DISULFIDE BONDS.
RX   PubMed=15003458; DOI=10.1016/j.jmb.2004.01.009;
RA   Mohanty S., Zubkov S., Gronenborn A.M.;
RT   "The solution NMR structure of Antheraea polyphemus PBP provides new
RT   insight into pheromone recognition by pheromone-binding proteins.";
RL   J. Mol. Biol. 337:443-451(2004).
RN   [4]
RP   STRUCTURE BY NMR OF 22-163, AND DISULFIDE BONDS.
RX   PubMed=17884092; DOI=10.1016/j.jmb.2007.07.078;
RA   Damberger F.F., Ishida Y., Leal W.S., Wuthrich K.;
RT   "Structural basis of ligand binding and release in insect pheromone-binding
RT   proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5.";
RL   J. Mol. Biol. 373:811-819(2007).
RN   [5]
RP   STRUCTURE BY NMR OF 22-163, AND DISULFIDE BONDS.
RX   PubMed=16289114; DOI=10.1016/j.jmb.2005.10.015;
RA   Zubkov S., Gronenborn A.M., Byeon I.J., Mohanty S.;
RT   "Structural consequences of the pH-induced conformational switch in
RT   A.polyphemus pheromone-binding protein: mechanisms of ligand release.";
RL   J. Mol. Biol. 354:1081-1090(2005).
CC   -!- FUNCTION: This major soluble protein in olfactory sensilla of male
CC       moths might serve to solubilize the extremely hydrophobic pheromone
CC       molecules and to transport pheromone through the aqueous lymph to
CC       receptors located on olfactory cilia.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Antenna.
CC   -!- DEVELOPMENTAL STAGE: Its synthesis occurs around the time of eclosion.
CC   -!- SIMILARITY: Belongs to the PBP/GOBP family. {ECO:0000305}.
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DR   EMBL; X17559; CAA35592.1; -; mRNA.
DR   PIR; S06152; S06152.
DR   PDB; 1QWV; NMR; -; A=22-163.
DR   PDB; 1TWO; NMR; -; A=22-163.
DR   PDB; 2JPO; NMR; -; A=22-163.
DR   PDBsum; 1QWV; -.
DR   PDBsum; 1TWO; -.
DR   PDBsum; 2JPO; -.
DR   AlphaFoldDB; P20797; -.
DR   BMRB; P20797; -.
DR   SMR; P20797; -.
DR   EvolutionaryTrace; P20797; -.
DR   GO; GO:0005550; F:pheromone binding; IEA:UniProtKB-KW.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.238.20; -; 1.
DR   InterPro; IPR006072; Odorant/phero-bd_Lep.
DR   InterPro; IPR006170; PBP/GOBP.
DR   InterPro; IPR036728; PBP_GOBP_sf.
DR   Pfam; PF01395; PBP_GOBP; 1.
DR   PIRSF; PIRSF015604; Odorant/phero_bd; 1.
DR   PRINTS; PR00484; PBPGOBP.
DR   SMART; SM00708; PhBP; 1.
DR   SUPFAM; SSF47565; SSF47565; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Pheromone response; Pheromone-binding; Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:2010751"
FT   CHAIN           22..163
FT                   /note="Pheromone-binding protein"
FT                   /id="PRO_0000012558"
FT   DISULFID        40..75
FT   DISULFID        71..129
FT   DISULFID        118..138
FT   CONFLICT        40
FT                   /note="C -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           23..26
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   HELIX           29..33
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   HELIX           37..44
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   HELIX           48..54
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   TURN            58..61
FT                   /evidence="ECO:0007829|PDB:2JPO"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:1TWO"
FT   HELIX           67..73
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   HELIX           76..80
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   HELIX           92..100
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   HELIX           105..120
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   TURN            128..130
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   HELIX           131..146
FT                   /evidence="ECO:0007829|PDB:1QWV"
FT   STRAND          155..158
FT                   /evidence="ECO:0007829|PDB:1TWO"
SQ   SEQUENCE   163 AA;  18142 MW;  B997CB8BF4C08859 CRC64;
     MLRKISLLLL PVFVAINLVH SSPEIMKNLS NNFGKAMDQC KDELSLPDSV VADLYNFWKD
     DYVMTDRLAG CAINCLATKL DVVDPDGNLH HGNAKDFAMK HGADETMAQQ LVDIIHGCEK
     SAPPNDDKCM KTIDVAMCFK KEIHKLNWVP NMDLVIGEVL AEV