PBP_BOMMO
ID PBP_BOMMO Reviewed; 164 AA.
AC P34174; Q17235;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Pheromone-binding protein;
DE Short=PBP;
DE Flags: Precursor;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Antenna;
RX PubMed=8900598; DOI=10.1016/0965-1748(95)00096-8;
RA Krieger J., von Nickisch-Rosenegk E., Mameli M., Pelosi P., Breer H.;
RT "Binding proteins from the antennae of Bombyx mori.";
RL Insect Biochem. Mol. Biol. 26:297-307(1996).
RN [2]
RP PROTEIN SEQUENCE OF 23-57.
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 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=10662696; DOI=10.1016/s1074-5521(00)00078-8;
RA Sandler B.H., Nikonova L., Leal W.S., Clardy J.;
RT "Sexual attraction in the silkworm moth: structure of the pheromone-
RT binding-protein-bombykol complex.";
RL Chem. Biol. 7:143-151(2000).
CC -!- FUNCTION: This major soluble protein in olfactory sensilla of male
CC moths serves to solubilize the extremely hydrophobic pheromone
CC molecules such as bombykol and to transport pheromone through the
CC aqueous lymph to receptors located on olfactory cilia.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Antenna.
CC -!- SIMILARITY: Belongs to the PBP/GOBP family. {ECO:0000305}.
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DR EMBL; X94987; CAA64443.1; -; mRNA.
DR RefSeq; NP_001037494.1; NM_001044029.1.
DR PDB; 1DQE; X-ray; 1.80 A; A/B=23-159.
DR PDB; 1GM0; NMR; -; A=23-164.
DR PDB; 1LS8; NMR; -; A=23-164.
DR PDB; 1XFR; NMR; -; A=23-150.
DR PDB; 2FJY; X-ray; 2.30 A; A/B=23-164.
DR PDB; 2P70; X-ray; 2.10 A; A=23-154.
DR PDB; 2P71; X-ray; 2.01 A; A=23-154.
DR PDBsum; 1DQE; -.
DR PDBsum; 1GM0; -.
DR PDBsum; 1LS8; -.
DR PDBsum; 1XFR; -.
DR PDBsum; 2FJY; -.
DR PDBsum; 2P70; -.
DR PDBsum; 2P71; -.
DR AlphaFoldDB; P34174; -.
DR BMRB; P34174; -.
DR SMR; P34174; -.
DR STRING; 7091.BGIBMGA012615-TA; -.
DR GeneID; 693050; -.
DR KEGG; bmor:693050; -.
DR CTD; 693050; -.
DR eggNOG; ENOG502TBQP; Eukaryota.
DR HOGENOM; CLU_1827210_0_0_1; -.
DR OrthoDB; 1467045at2759; -.
DR EvolutionaryTrace; P34174; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:2010751"
FT CHAIN 23..164
FT /note="Pheromone-binding protein"
FT /id="PRO_0000012559"
FT DISULFID 41..76
FT DISULFID 72..130
FT DISULFID 119..139
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:1DQE"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:1DQE"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1DQE"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1DQE"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1LS8"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1DQE"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2FJY"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1DQE"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:1DQE"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:1DQE"
FT HELIX 129..146
FT /evidence="ECO:0007829|PDB:1DQE"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1GM0"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:2FJY"
SQ SEQUENCE 164 AA; 18086 MW; 57591C4C98C0F553 CRC64;
MSIQGQIALA LMVNMAVGSV DASQEVMKNL SLNFGKALDE CKKEMTLTDA INEDFYNFWK
EGYEIKNRET GCAIMCLSTK LNMLDPEGNL HHGNAMEFAK KHGADETMAQ QLIDIVHGCE
KSTPANDDKC IWTLGVATCF KAEIHKLNWA PSMDVAVGEI LAEV
