ID   CNGA3_BOVIN             Reviewed;         706 AA.
AC   Q29441;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Cyclic nucleotide-gated cation channel alpha-3;
DE   AltName: Full=Cone photoreceptor cGMP-gated channel subunit alpha;
DE   AltName: Full=Cyclic nucleotide-gated channel alpha-3;
DE            Short=CNG channel alpha-3;
DE            Short=CNG-3;
DE            Short=CNG3;
GN   Name=CNGA3; Synonyms=CNCG3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=7512693; DOI=10.1038/368859a0;
RA   Weyand I., Godde M., Frings S., Weiner J., Mueller F., Altenhofen W.,
RA   Hatt H., Kaupp U.B.;
RT   "Cloning and functional expression of a cyclic-nucleotide-gated channel
RT   from mammalian sperm.";
RL   Nature 368:859-863(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=8170936; DOI=10.1073/pnas.91.9.3505;
RA   Biel M., Zong X., Distler M., Bosse E., Klugbauer N., Murakami M.,
RA   Flockerzi V., Hofmann F.;
RT   "Another member of the cyclic nucleotide-gated channel family, expressed in
RT   testis, kidney, and heart.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:3505-3509(1994).
CC   -!- FUNCTION: Visual signal transduction is mediated by a G-protein coupled
CC       cascade using cGMP as second messenger. This protein can be activated
CC       by cyclic GMP which leads to an opening of the cation channel and
CC       thereby causing a depolarization of cone photoreceptors. Essential for
CC       the generation of light-evoked electrical responses in the red-,
CC       green- and blue sensitive cones Induced a flickering channel gating,
CC       weakened the outward rectification in the presence of extracellular
CC       calcium, increased sensitivity for L-cis diltiazem and enhanced the
CC       cAMP efficacy of the channel when coexpressed with CNGB3 (By
CC       similarity). Could be responsible for cGMP-induced calcium entry in
CC       cells other than sensory cells. Might be involved in chemotaxis of
CC       sperm. {ECO:0000250}.
CC   -!- SUBUNIT: Tetramer formed of three CNGA3 and one CNGB3 modulatory
CC       subunits (By similarity). Forms functional heterooligomeric channels
CC       with CNG4 in vitro. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Testis, kidney, retinal cone and heart.
CC   -!- DOMAIN: The C-terminal coiled-coil domain mediates homotrimerization of
CC       CNGA subunits. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
CC       (TC 1.A.1.5) family. CNGA3 subfamily. {ECO:0000305}.
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DR   EMBL; X89600; CAA61759.1; -; mRNA.
DR   EMBL; X76485; CAA54023.1; -; mRNA.
DR   PIR; A55251; A55251.
DR   RefSeq; NP_776704.1; NM_174279.2.
DR   AlphaFoldDB; Q29441; -.
DR   SMR; Q29441; -.
DR   STRING; 9913.ENSBTAP00000062580; -.
DR   PaxDb; 9913-ENSBTAP00000052464; -.
DR   GeneID; 281701; -.
DR   KEGG; bta:281701; -.
DR   CTD; 1261; -.
DR   eggNOG; KOG0500; Eukaryota.
DR   HOGENOM; CLU_005746_12_0_1; -.
DR   InParanoid; Q29441; -.
DR   OrthoDB; 74296at2759; -.
DR   TreeFam; TF319048; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030553; F:cGMP binding; IBA:GO_Central.
DR   GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; IBA:GO_Central.
DR   GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR   GO; GO:0098655; P:monoatomic cation transmembrane transport; IBA:GO_Central.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; 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:SF6; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL ALPHA-3; 1.
DR   PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 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   2: Evidence at transcript level;
KW   cGMP; cGMP-binding; Coiled coil; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Nucleotide-binding; Reference proteome;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Transport;
KW   Vision.
FT   CHAIN           1..706
FT                   /note="Cyclic nucleotide-gated cation channel alpha-3"
FT                   /id="PRO_0000219316"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          113..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          645..688
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        145..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         501..624
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT   BINDING         568
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000255"
FT   BINDING         583
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   706 AA;  81132 MW;  F4990DCD29B56239 CRC64;
     MAKISTQYSH PTRTHPSVRT MDRDLDCIEN GLSRTHLPCE ETSSELQEGI AMETRGLAES
     RQSSFTSQGP TRLSRLIISL RAWSARHLHQ EDQRPDSFLE RFRGAELQEV SSRESHVQFN
     VGSQEPPDRG RSAWPLARNN TNTCNNSEKD DKAKKEEKEK KEEKKENPKK EEKKKDSVVM
     DPSSNMYYHW LTVIAVPVFY NWCLLVCRAC FDELQSEHLM LWLVLDYSAD ILYGMDMLVR
     ARTGFLEQGL MVMDASRLWK HYTQTLHFKL DVLSLVPTDL AYFKLGMNYP ELRFNRLLKL
     ARLFEFFDRT ETRTNYPNMF RIGNLVLYIL IIIHWNACIY FAISKFIGFG TDSWVYPNVS
     NPEYGRLSRK YIYSLYWSTL TLTTIGETPP PVKDEEYLFV VIDFLVGVLI FATIVGNVGS
     MISNMNASRA EFQAKIDSIK QYMQFRKVTK DLETRVIRWF DYLWANKKTV DEKEVLKSLP
     DKLKAEIAIN VHLDTLRKVR IFQDCEAGLL VELVLKLRPA VFSPGDYICK KGDIGREMYI
     IKEGKLAVVA EDGITQFVVL GDGSYFGEIS ILNIKGSKSG NRRTANIRSI GYSDLFCLSK
     DDLMEALTEY PEAKKALEEK GRQILMKDNL IDEELAKAGA DPKDIEEKVE HLETSLDSLQ
     TRFARLLAEY NATQMKVKQR LSQLESQVKM GLPPDGDAPQ TEASQP
//