ID   SNMP2_OSTFU             Reviewed;         522 AA.
AC   E5EZX0;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 22.
DE   RecName: Full=Sensory neuron membrane protein 2 {ECO:0000312|EMBL:ADQ73891.1};
GN   Name=Snmp2 {ECO:0000312|EMBL:ADQ73891.1};
OS   Ostrinia furnacalis (Asian corn borer).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC   Crambidae; Pyraustinae; Ostrinia.
OX   NCBI_TaxID=93504;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ADQ73891.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=21056664; DOI=10.1016/j.ibmb.2010.10.005;
RA   Allen J.E., Wanner K.W.;
RT   "Asian corn borer pheromone binding protein 3, a candidate for evolving
RT   specificity to the 12-tetradecenyl acetate sex pheromone.";
RL   Insect Biochem. Mol. Biol. 41:141-149(2011).
CC   -!- FUNCTION: Plays an olfactory role that is not restricted to pheromone
CC       sensitivity. {ECO:0000250|UniProtKB:O02351}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O02351};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:O02351}.
CC   -!- TISSUE SPECIFICITY: Detected in both male and female antennal tissues.
CC       Expression is two to three fold higher in male compared to female
CC       antenna. Detected at low levels in all body tissues except the female
CC       abdomen. {ECO:0000269|PubMed:21056664}.
CC   -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000255}.
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DR   EMBL; HM044393; ADQ73891.1; -; mRNA.
DR   AlphaFoldDB; E5EZX0; -.
DR   SMR; E5EZX0; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR   InterPro; IPR002159; CD36_fam.
DR   PANTHER; PTHR11923; PTHR11923; 1.
DR   Pfam; PF01130; CD36; 1.
DR   PRINTS; PR01609; CD36FAMILY.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Membrane; Olfaction; Receptor;
KW   Sensory transduction; Transmembrane; Transmembrane helix.
FT   CHAIN           1..522
FT                   /note="Sensory neuron membrane protein 2"
FT                   /id="PRO_0000413632"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..469
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        491..522
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        314
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        268..338
FT                   /evidence="ECO:0000250|UniProtKB:P26201"
FT   DISULFID        299..362
FT                   /evidence="ECO:0000250|UniProtKB:P26201"
FT   DISULFID        340..351
FT                   /evidence="ECO:0000250|UniProtKB:P26201"
SQ   SEQUENCE   522 AA;  58173 MW;  56CDBF2BD4B4EBB8 CRC64;
     MLGKHTKLFF GVSLVALIVS VILAAWGFPK IVSKQIQKNI QIDNSSVMFE KWRKIPMPLT
     FNVYVFNVTN VEDVNNGAKP RLQQIGPYAY KEYRERTVLG YGDNDTVSYT LKKTFIFDQE
     ASGLLSEDDE VTVIHFSYMA AILTVNDMMP SITGVVNGAL EQFFTNLTDP FLRVKVKDLF
     FDGVYVNCAG NHSALGLVCG KLKADAPQTM RPAGDGNGFY FSMFSHMNRT ESGPYEMIRG
     RENIKELGHI ISYKGKSFMK NWGNDMYCGQ LNGSDASIFP PIDENNVPEK LYTFEPEVCR
     SLYASLVGKS SIFNMSAYYY EISSDALASK SANPGNKCYC KKNWSANHDG CLIMGILNLM
     PCQDAPAIAS LPHFYLASEE LLEYFDGGIS PDKEKHNTYI YLEPVTGVVL KGLRRLQFNI
     ELRNIPMVPQ LAKVPTGLFP LLWIEEGAEL PDSIIQELRQ SHTLLGYVEA VRWALLAIAI
     VATAISAIAV ARSGLIPVWP RNANSVSFIL SPHPNSDVNK VH