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OBP1_BOMMO
ID   OBP1_BOMMO              Reviewed;         164 AA.
AC   P34171; Q17225;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=General odorant-binding protein 1;
DE            Short=GOBP1;
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 19-164.
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).
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: Antenna. {ECO:0000269|PubMed:8900598}.
CC   -!- SIMILARITY: Belongs to the PBP/GOBP family. {ECO:0000305}.
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DR   EMBL; X94988; CAA64444.1; -; mRNA.
DR   RefSeq; NP_001037496.1; NM_001044031.1.
DR   AlphaFoldDB; P34171; -.
DR   SMR; P34171; -.
DR   STRING; 7091.BGIBMGA012611-TA; -.
DR   GeneID; 693051; -.
DR   KEGG; bmor:693051; -.
DR   CTD; 693051; -.
DR   eggNOG; ENOG502TBNR; Eukaryota.
DR   HOGENOM; CLU_1827210_0_0_1; -.
DR   OrthoDB; 1372438at2759; -.
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   Direct protein sequencing; Disulfide bond; Olfaction; Reference proteome;
KW   Sensory transduction; Signal; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:2010751"
FT   CHAIN           19..164
FT                   /note="General odorant-binding protein 1"
FT                   /id="PRO_0000012567"
FT   DISULFID        37..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..126
FT                   /evidence="ECO:0000250"
FT   DISULFID        115..135
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   164 AA;  19150 MW;  EF11A87F727E517B CRC64;
     MWKLVVVLTV NLLQGALTDV YVMKDVTLGF GQALEQCREE SQLTEEKMEE FFHFWNDDFK
     FEHRELGCAI QCMSRHFNLL TDSSRMHHEN TDKFIKSFPN GEILSQKMID MIHTCEKTFD
     SEPDHCWRIL RVAECFKDAC NKSGLAPSME LILAEFIMES EADK
 
 
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