ID   SNMP2_HELVI             Reviewed;         520 AA.
AC   B2RFN2;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Sensory neuron membrane protein 2 {ECO:0000303|PubMed:18209018, ECO:0000312|EMBL:CAP19028.1};
DE            Short=HvirSNMP-2 {ECO:0000303|PubMed:18209018};
GN   Name=snmp2 {ECO:0000312|EMBL:CAP19028.1};
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:0000305, ECO:0000312|EMBL:CAP19028.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Antenna {ECO:0000312|EMBL:CAP19028.1};
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 (By similarity). May play a role in the elimination of
CC       lipophilic components from the sensillum lymph.
CC       {ECO:0000250|UniProtKB:O02351, ECO:0000269|PubMed:18209018}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O02351};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:O02351}.
CC   -!- TISSUE SPECIFICITY: Localizes to cells surrounding the sensory neurons
CC       in the antenna. Associate in a ratio of 2:1 with the neurons expressing
CC       the other subtype SNMP1. {ECO:0000269|PubMed:18209018}.
CC   -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000255}.
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DR   EMBL; AM905328; CAP19028.1; -; mRNA.
DR   AlphaFoldDB; B2RFN2; -.
DR   SMR; B2RFN2; -.
DR   TCDB; 9.B.39.1.12; 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: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..520
FT                   /note="Sensory neuron membrane protein 2"
FT                   /id="PRO_0000413630"
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..468
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        490..520
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        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        267..337
FT                   /evidence="ECO:0000250|UniProtKB:P26201"
FT   DISULFID        298..361
FT                   /evidence="ECO:0000250|UniProtKB:P26201"
FT   DISULFID        339..350
FT                   /evidence="ECO:0000250|UniProtKB:P26201"
SQ   SEQUENCE   520 AA;  58629 MW;  B43A23F7BBCAD039 CRC64;
     MLGKHSKIFF GVSLIFLVIA IVLASWGFQK IVNKQIQKNV QLANDSKMFE RWVKLPMPLD
     FKVYVFNVTN VEEVNQGGKP ILQEIGPYVY KQYREKTILG YGDNDTIKYM LKKHFEFDPE
     ASGSLTEDDE LTVVHFSYLA ALLTVHDMMP SLVTVVNKAL EQLFPSLEDA FLRVKVRDLF
     FDGIYLSCDG DNSALGLVCG KIRAEMPPTM RKAEGSNGFY FSMFSHMNRS ESGPYEMIRG
     RDNVYELGNI VSYKGQENMP MWGDKYCGQI NGSDSSIFPP IKEDDVPKKI YTFEPDICRS
     VYADLVDKRE LFNISTYYYE ISETAFAAKS ANPNNRCFCK KNWSANHDGC LLMGLLNLTP
     CQGAPAIASL PHFYLGSEEL LDYFQSGVQP DKEKHNTYVY IDPVTGVVLS GVKRLQFNIE
     MRQINNIPQL KSVPTGLFPM LWLEEGATIP ESIQQELRDS HKLLGYVEVA KWFLLTIAII
     SVIASAVAVA RANALLSWPR NSNSVSFILG PSVTQVNKGN