SNMP1_ANTPO
ID SNMP1_ANTPO Reviewed; 525 AA.
AC O02351;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Sensory neuron membrane protein 1;
GN Name=Snmp-1 {ECO:0000303|PubMed:9169446};
OS Antheraea polyphemus (Polyphemus moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Saturniinae; Saturniini; Antheraea.
OX NCBI_TaxID=7120;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC47540.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-30, FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Antenna {ECO:0000269|PubMed:9169446};
RX PubMed=9169446; DOI=10.1074/jbc.272.23.14792;
RA Rogers M.E., Sun M., Lerner M.R., Vogt R.G.;
RT "Snmp-1, a novel membrane protein of olfactory neurons of the silk moth
RT Antheraea polyphemus with homology to the CD36 family of membrane
RT proteins.";
RL J. Biol. Chem. 272:14792-14799(1997).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Antenna {ECO:0000269|PubMed:11320659};
RX PubMed=11320659; DOI=10.1007/s004410000305;
RA Rogers M.E., Steinbrecht R.A., Vogt R.G.;
RT "Expression of SNMP-1 in olfactory neurons and sensilla of male and female
RT antennae of the silkmoth Antheraea polyphemus.";
RL Cell Tissue Res. 303:433-446(2001).
CC -!- FUNCTION: Plays an olfactory role that is not restricted to pheromone
CC sensitivity. May be involved in the odor detection properties of the
CC olfactory receptor neurons (ORNs) rather than their differentiation and
CC growth. {ECO:0000269|PubMed:11320659, ECO:0000269|PubMed:9169446}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11320659,
CC ECO:0000269|PubMed:9169446}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11320659, ECO:0000269|PubMed:9169446}.
CC Note=Localizes to structures interpreted to be vesicles and secretory
CC granules but not in the plasma membrane of the cell body.
CC {ECO:0000269|PubMed:11320659, ECO:0000269|PubMed:9169446}.
CC -!- TISSUE SPECIFICITY: Principal component of the olfactory cilia
CC membrane. Localizes to the somata, dendritic neck and cilia of the
CC olfactory neurons (at protein level). Not detected in the axons of
CC ORNs, the cytoplasm of auxiliary cells or non-sensory structures.
CC Expression is universal among ORNs but differential between neuron and
CC sensillum types. {ECO:0000269|PubMed:11320659,
CC ECO:0000269|PubMed:9169446}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels on day 6, increases
CC gradually to day 11 and then dramatically rises well into the adult
CC stage. {ECO:0000269|PubMed:9169446}.
CC -!- SIMILARITY: Belongs to the CD36 family. {ECO:0000305}.
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DR EMBL; U95026; AAC47540.1; -; mRNA.
DR PIR; A59259; A59259.
DR AlphaFoldDB; O02351; -.
DR SMR; O02351; -.
DR PRIDE; O02351; -.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Olfaction; Receptor; Sensory transduction; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..525
FT /note="Sensory neuron membrane protein 1"
FT /id="PRO_0000408232"
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..456
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 496..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
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 525 AA; 59921 MW; 716649B293592E3A CRC64;
MLLPKPLKYA AIGGGVFVFG ILIGWVIFPV ILKSQIKKEM ALSKKTDLRQ MWEKVPFALD
FKVYIFNYTN VDEIQKGAKP IVKEIGPYYF EEWKEKVEVE DHEENDTITY KRLDVFHFRP
DLSGPGLTGE EVIIMPHLFI LAMVATINRE KPSMLNVVEK SINGIFDNPK DVFLRVKAMD
IMFRGIIINC DRTEFAPKAA CTKMKKDAVT GVIYEPNNQF RFSLFGTRNN TVNPDVVTVK
RGIKNIMDVG QVVALNGKPQ IDIWRDHCNE FQGTDGTVFP PFLTYKDRLQ SFSFDLCRSF
KAWFQKKTSY KGIKTNRYIA NVGDFANDPE LQCFCDTPDE CLPKGIMDIR KCLKVPMYVS
LPHFLETDTS VTNQVKGLTP DPNEHGIIAD FEPLSGTLMD AKQRMQYNIK LLRTDKIAIF
KDLPDSIVPC FWVHEGILLN KTFVKMLKHQ LFIPKRIVGV IRWWMVSFGL IAVLAGVMYH
FKDNIMGWAA KGESTTAKVN PEDGSNEQRG VSVIGQDREP PKVTM
