ID   SNMP1_HELVI             Reviewed;         523 AA.
AC   Q9U1G3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Sensory neuron membrane protein 1;
DE            Short=SNMP1-Hvir {ECO:0000303|PubMed:11536197};
GN   Name=snmp1 {ECO:0000312|EMBL:CAB65739.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102;
RN   [1] {ECO:0000312|EMBL:CAB65739.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Antenna {ECO:0000312|EMBL:CAB65739.1};
RX   PubMed=11536197; DOI=10.1002/neu.1065;
RA   Rogers M.E., Krieger J., Vogt R.G.;
RT   "Antennal SNMPs (sensory neuron membrane proteins) of Lepidoptera define a
RT   unique family of invertebrate CD36-like proteins.";
RL   J. Neurobiol. 49:47-61(2001).
RN   [2] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RC   TISSUE=Antenna {ECO:0000269|PubMed:18209018};
RX   PubMed=18209018; DOI=10.1093/chemse/bjm087;
RA   Forstner M., Gohl T., Gondesen I., Raming K., Breer H., Krieger J.;
RT   "Differential expression of SNMP-1 and SNMP-2 proteins in pheromone-
RT   sensitive hairs of moths.";
RL   Chem. Senses 33:291-299(2008).
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 sensory neurons in the antenna.
CC       {ECO:0000269|PubMed:18209018}.
CC   -!- SIMILARITY: Belongs to the CD36 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; AJ251959; CAB65739.1; -; mRNA.
DR   AlphaFoldDB; Q9U1G3; -.
DR   SMR; Q9U1G3; -.
DR   TCDB; 9.B.39.1.11; the long chain fatty acid translocase (lcfat) family.
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:0005186; F:pheromone activity; 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;
KW   Pheromone; Receptor; Sensory transduction; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..523
FT                   /note="Sensory neuron membrane protein 1"
FT                   /id="PRO_0000408250"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..458
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        459..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        480..523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        268..333
FT                   /evidence="ECO:0000250|UniProtKB:P26201"
FT   DISULFID        297..352
FT                   /evidence="ECO:0000250|UniProtKB:P26201"
FT   DISULFID        335..341
FT                   /evidence="ECO:0000250|UniProtKB:P26201"
SQ   SEQUENCE   523 AA;  59108 MW;  C9D3F92135AA87D2 CRC64;
     MQLPKELKYA AIAGGVALFG LIFGWVLFPT ILKSQLKKEM ALSKKTDVRK MWEKIPFALD
     FKVYIFNFTN AEEVQKGATP ILKEIGPYHF DEWKEKVEVE DHEEDDTITY KKRDVFYFNP
     EMSGPGLTGE EIVVIPHIFM LGMALTVARD KPAMLNMVGK AMNGIFDDPP DIFLRVKALD
     ILFRGMIINC ARTEFAPKAT CTALKKEAVS GLVLEPNNQF RFSIFGTRNN TIDPHVITVK
     RGIKNVMDVG QVVAVDGKLE QTIWRDTCNE YQGTDGTVFP PFVPETERIQ SFSTDLCRTF
     KPWYQKKTSY RGIKTNRYVA NIGDFANDPE LNCFCPKPDS CPPKGLMDLA PCMKAPMYAS
     MPHFLDSDPE LLTKVKGLNP DVTQHGIEID YEPITGTPMV AKQRIQFNIQ LLKTDKLDLF
     KDLSGDIVPL FWIDEGLALN KTFVNMLKHQ LFIPKRVVGV LRWWVVSFGS LGAVIGIVFH
     FRDHIMRLAV SGDTKVSKVT PEEPEQKDIS VIGQAQEPAK VNI