ID G3U608_LOXAF Unreviewed; 662 AA.
AC G3U608;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Cyclic nucleotide-gated olfactory channel {ECO:0000256|ARBA:ARBA00040598};
DE AltName: Full=Cyclic nucleotide-gated cation channel 2 {ECO:0000256|ARBA:ARBA00042767};
DE AltName: Full=Cyclic nucleotide-gated channel alpha-2 {ECO:0000256|ARBA:ARBA00043150};
GN Name=CNGA2 {ECO:0000313|Ensembl:ENSLAFP00000023266.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000023266.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000023266.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023266.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000023266.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023266.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Odorant signal transduction is probably mediated by a G-
CC protein coupled cascade using cAMP as second messenger. The olfactory
CC channel can be shown to be activated by cyclic nucleotides which leads
CC to a depolarization of olfactory sensory neurons.
CC {ECO:0000256|ARBA:ARBA00037084}.
CC -!- SUBUNIT: Heterotetramer composed of two subunits of CNGA2, one of CNGA4
CC and one of CNGB1b. The complex forms the cyclic nucleotide-gated (CNG)
CC channel of olfactory sensory neurons. {ECO:0000256|ARBA:ARBA00038593}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGA2 subfamily. {ECO:0000256|ARBA:ARBA00038139}.
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 AlphaFoldDB; G3U608; -.
DR STRING; 9785.ENSLAFP00000023266; -.
DR Ensembl; ENSLAFT00000029534.1; ENSLAFP00000023266.1; ENSLAFG00000026713.1.
DR eggNOG; KOG0500; Eukaryota.
DR GeneTree; ENSGT00940000155374; -.
DR HOGENOM; CLU_005746_12_0_1; -.
DR InParanoid; G3U608; -.
DR OMA; DWYYHWL; -.
DR TreeFam; TF319048; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:Ensembl.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.5.300; -; 1.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR032406; CLZ_dom.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR PANTHER; PTHR45638:SF3; CYCLIC NUCLEOTIDE-GATED OLFACTORY CHANNEL; 1.
DR Pfam; PF16526; CLZ; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Olfaction {ECO:0000256|ARBA:ARBA00022725};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 454..568
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 75996 MW; E3CB62E7C7FDEEBD CRC64;
MTEKSNGVKS SPANNHNHHV PPTIKANGKD DRRTSSRPQS AADDDTSSEL QRLAEMDAPQ
QGRGGFRRII RLVGVIREWA NKNFREEDPR PDSFLERFRG PELQTVTTQQ GDGKSDKDGE
GKGTKKKFEL FVLDPAGDWY YRWLFFIALP VLYNWCLLVA RACFSDLQKG YYLVWLVLDY
FSDMVYIADL FIRLRTGFLE QGLLVKDPKK LRDNYIHTMQ FKLDVASIIP TDLIYFAVGI
HSPELRFNRL LHFARMFEFF DRTETRTSYP NIFRISNLVL YILVIIHWNA CIYYAISKSI
GFGVDTWVYP NITDPAYGYL AREYIYCLYW STLTLTTIGE TPPPVKDEEY LFVIFDFLIG
VLIFATIVGN VGSMISNMNA TRAEFQAKID AVKHYMQFRK VSKEMEAKVI KWFDYLWTNK
KTVDEREVLK NLPAKLRAEI AINVHLSTLK KVRIFQDCEA GLLVELVLKL RPQVFSPGDY
ICRKGDIGKE MYIIKEGKLA VVADDGVTQY ALLSAGSCFG EISILNIKGS KMGNRRTANI
RSLGYSDLFC LSKDDLMEAV TEYPDAKKVL EERGREILMK EGLLDENEVA ATMEVDVQEK
LEQLETNMET LYTRFGRLLA EYTGAQQKLK QRITVLETKM KQNNEEDYLS DGINSPEPAA
VE
//
