OBP2_BOMMO
ID OBP2_BOMMO Reviewed; 160 AA.
AC P34170; Q17226;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=General odorant-binding protein 2;
DE Short=GOBP2;
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], AND TISSUE SPECIFICITY.
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 21-41.
RC TISSUE=Antenna;
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 (1.4 ANGSTROMS) OF 20-160 IN COMPLEXES WITH BOMBYKOL;
RP BOMBYKAL AND SYNTHETIC ANALOGS, AND TISSUE SPECIFICITY.
RX PubMed=19371749; DOI=10.1016/j.jmb.2009.04.015;
RA Zhou J.J., Robertson G., He X., Dufour S., Hooper A.M., Pickett J.A.,
RA Keep N.H., Field L.M.;
RT "Characterisation of Bombyx mori odorant-binding proteins reveals that a
RT general odorant-binding protein discriminates between sex pheromone
RT components.";
RL J. Mol. Biol. 389:529-545(2009).
CC -!- FUNCTION: Present in the aqueous fluid surrounding olfactory sensory
CC dendrites and are thought to aid in the capture and transport of
CC hydrophobic odorants into and through this fluid.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in antenna (at protein level). Expressed
CC at high levels in antenna. {ECO:0000269|PubMed:19371749,
CC ECO:0000269|PubMed:8900598}.
CC -!- SIMILARITY: Belongs to the PBP/GOBP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X94989; CAA64445.1; -; mRNA.
DR RefSeq; NP_001037498.1; NM_001044033.1.
DR PDB; 2WC5; X-ray; 1.90 A; A=20-160.
DR PDB; 2WC6; X-ray; 1.90 A; A=20-160.
DR PDB; 2WCH; X-ray; 1.70 A; A=20-160.
DR PDB; 2WCJ; X-ray; 1.40 A; A=20-160.
DR PDB; 2WCK; X-ray; 1.61 A; A=20-160.
DR PDB; 2WCL; X-ray; 1.61 A; A=20-160.
DR PDB; 2WCM; X-ray; 1.50 A; A=20-160.
DR PDBsum; 2WC5; -.
DR PDBsum; 2WC6; -.
DR PDBsum; 2WCH; -.
DR PDBsum; 2WCJ; -.
DR PDBsum; 2WCK; -.
DR PDBsum; 2WCL; -.
DR PDBsum; 2WCM; -.
DR AlphaFoldDB; P34170; -.
DR SMR; P34170; -.
DR STRING; 7091.BGIBMGA012614-TA; -.
DR EnsemblMetazoa; BGIBMGA012614-RA; BGIBMGA012614-TA; BGIBMGA012614.
DR GeneID; 693052; -.
DR KEGG; bmor:693052; -.
DR CTD; 693052; -.
DR eggNOG; ENOG502TKYM; Eukaryota.
DR HOGENOM; CLU_1827210_0_0_1; -.
DR InParanoid; P34170; -.
DR OMA; LIHNCEK; -.
DR OrthoDB; 1372438at2759; -.
DR EvolutionaryTrace; P34170; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005549; F:odorant binding; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; 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; Olfaction;
KW Reference proteome; Sensory transduction; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:2010751"
FT CHAIN 21..160
FT /note="General odorant-binding protein 2"
FT /id="PRO_0000012566"
FT DISULFID 38..73
FT /evidence="ECO:0000250"
FT DISULFID 69..127
FT /evidence="ECO:0000250"
FT DISULFID 116..136
FT /evidence="ECO:0000250"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:2WCJ"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2WCJ"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:2WCJ"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2WCJ"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:2WCJ"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:2WCJ"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2WCJ"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:2WCJ"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2WCJ"
FT HELIX 103..119
FT /evidence="ECO:0007829|PDB:2WCJ"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2WCJ"
FT HELIX 126..143
FT /evidence="ECO:0007829|PDB:2WCJ"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:2WCJ"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2WCJ"
SQ SEQUENCE 160 AA; 18145 MW; 2DC95D3FD284C81A CRC64;
MFSFLILVFV ASVADSVIGT AEVMSHVTAH FGKTLEECRE ESGLSVDILD EFKHFWSDDF
DVVHRELGCA IICMSNKFSL MDDDVRMHHV NMDEYIKGFP NGQVLAEKMV KLIHNCEKQF
DTETDDCTRV VKVAACFKKD SRKEGIAPEV AMIEAVIEKY
