ID H2PX32_PONAB Unreviewed; 664 AA.
AC H2PX32; A0A2J8S401; A0A6D2XSY6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
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:ENSPPYP00000023309.1};
GN ORFNames=CR201_G0046470 {ECO:0000313|EMBL:PNJ15497.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000023309.1, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000023309.1, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ15497.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ15497.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000023309.1}
RP IDENTIFICATION.
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}.
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DR EMBL; NDHI03003613; PNJ15497.1; -; Genomic_DNA.
DR RefSeq; XP_009233650.1; XM_009235375.1.
DR STRING; 9601.ENSPPYP00000023309; -.
DR Ensembl; ENSPPYT00000024285.2; ENSPPYP00000023309.1; ENSPPYG00000020824.2.
DR GeneID; 100449041; -.
DR KEGG; pon:100449041; -.
DR CTD; 1260; -.
DR eggNOG; KOG0500; Eukaryota.
DR GeneTree; ENSGT00940000155374; -.
DR HOGENOM; CLU_005746_12_0_1; -.
DR OMA; DWYYHWL; -.
DR OrthoDB; 74296at2759; -.
DR TreeFam; TF319048; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
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 PRINTS; PR01463; EAGCHANLFMLY.
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:UP000001595};
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..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 76130 MW; BFEF91B7184BF1DA CRC64;
MTEKTNGVKS SPANNHNHHA PPAIKANGKD DHRISSRPHS AADDDTSSEL QRLADVDAPQ
QGRSGFRRIV RLVGIIREWA NKNFREEEPR PDSFLERFRG PELQTVTTQQ GDGKGDKDGE
DKGTKKKFEL FVLDPAGDWY YCWLFVIAMP VLYNWCLLVA RACFSDLQKG YYLVWLVLDY
VSDVVYIVDL FIRLRTGFLE QGLLVKDTKK LRDNYIHTLQ FKLDVASIIP TDLIYFAVDI
HSPEVRFNRL LHFARMFEFF DRTETRTSYP NIFRISNLVL YILVIIHWNA CIYYAISKSI
GFGVDTWVYP NITDPEYGYL AREYIYCLYW STLTLTTIGE TPPPVKDEEY LFVIFDFLIG
VLIFATIVGN VGSMISNMNA TRAEFQAKID AVKHYMQFRK VSKEMEAKVI RWFDYLWTNK
KTVDEREILK NLPAKLRAEI AINVHLSTLK KVRIFHDCEA GLLVELVLKL RPQVFSPGDY
ICHKGDIGKE MYIIKEGKLA VVADDGVTQY ALLSAGSCFG EISILNIKGS KMGNRRTANI
RSLGYSDLFC LSKDDLMEAV TEYPDAKKVL EERGREILMK EGLLDENEVA TSMEVDMQEK
LGQLETNMET LYTRFGRLLA EYTGAQQKLK QRITVLETKM KQNNEDDYLS DGMNSPELAA
ADNP
//
