ID   PBP2_EPIPO              Reviewed;         164 AA.
AC   Q95VF0;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Pheromone-binding protein 2;
DE            Short=PBP 2;
DE   Flags: Precursor;
GN   Name=PBP;
OS   Epiphyas postvittana (Light brown apple moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tortricoidea;
OC   Tortricidae; Tortricinae; Epiphyas.
OX   NCBI_TaxID=65032 {ECO:0000312|EMBL:AAL09026.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-35, SUBUNIT,
RP   TISSUE SPECIFICITY, MASS SPECTROMETRY, AND POLYMORPHISM.
RC   TISSUE=Antenna;
RX   PubMed=12530222; DOI=10.1016/s0965-1748(02)00075-9;
RA   Newcomb R.D., Sirey T.M., Rassam M., Greenwood D.R.;
RT   "Pheromone binding proteins of Epiphyas postvittana (Lepidoptera:
RT   Tortricidae) are encoded at a single locus.";
RL   Insect Biochem. Mol. Biol. 32:1543-1554(2002).
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. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer and disulfide-linked dimers.
CC       {ECO:0000269|PubMed:12530222}.
CC   -!- TISSUE SPECIFICITY: Antenna. {ECO:0000269|PubMed:12530222}.
CC   -!- MASS SPECTROMETRY: Mass=15684; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12530222};
CC   -!- POLYMORPHISM: 2 electrophoretic alleles are known: fast and slow. The
CC       isoform shown here is the fast form. {ECO:0000250|UniProtKB:P34174}.
CC   -!- SIMILARITY: Belongs to the PBP/GOBP family. {ECO:0000305}.
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DR   EMBL; AF416587; AAL09026.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q95VF0; -.
DR   SMR; Q95VF0; -.
DR   GO; GO:0005550; F:pheromone binding; TAS:UniProtKB.
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   Direct protein sequencing; Disulfide bond; Pheromone response;
KW   Pheromone-binding; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:12530222"
FT   CHAIN           24..164
FT                   /note="Pheromone-binding protein 2"
FT                   /id="PRO_0000012561"
FT   DISULFID        42..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        73..130
FT                   /evidence="ECO:0000250"
FT   DISULFID        119..139
FT                   /evidence="ECO:0000250"
FT   VARIANT         54
FT                   /note="S -> A"
FT                   /evidence="ECO:0000269|PubMed:12530222"
FT   VARIANT         87
FT                   /note="D -> E"
FT                   /evidence="ECO:0000269|PubMed:12530222"
FT   VARIANT         122
FT                   /note="A -> T"
FT                   /evidence="ECO:0000269|PubMed:12530222"
SQ   SEQUENCE   164 AA;  18315 MW;  199F9C7F710C42E9 CRC64;
     MMNHKELVLF AVVCLSLYQA VEPSQDVVKD MSLNFRKGLD ACKKELNLPD TINSDFNRFW
     NDDHVVTNRD TGCAIMCLSS KLELVSDTGL HHGNTLEYAK QHGADDTVAQ QIVDLLHSCA
     QAVPDLEDPC LKVLEWAKCF KAEIHKLNWA PSAEVMAAEM LAEV