ID A0A2K6BXM6_MACNE Unreviewed; 672 AA.
AC A0A2K6BXM6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=cGMP-gated cation channel alpha-1 {ECO:0000256|ARBA:ARBA00021373};
DE AltName: Full=Cyclic nucleotide-gated cation channel 1 {ECO:0000256|ARBA:ARBA00031628};
DE AltName: Full=Cyclic nucleotide-gated channel alpha-1 {ECO:0000256|ARBA:ARBA00033061};
DE AltName: Full=Cyclic nucleotide-gated channel, photoreceptor {ECO:0000256|ARBA:ARBA00032867};
DE AltName: Full=Rod photoreceptor cGMP-gated channel subunit alpha {ECO:0000256|ARBA:ARBA00030411};
GN Name=CNGA1 {ECO:0000313|Ensembl:ENSMNEP00000016168.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000016168.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000016168.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Subunit of the rod cyclic GMP-gated cation channel, which is
CC involved in the final stage of the phototransduction pathway. When
CC light hits rod photoreceptors, cGMP concentrations decrease causing
CC rapid closure of CNGA1/CNGB1 channels and, therefore, hyperpolarization
CC of the membrane potential. {ECO:0000256|ARBA:ARBA00002301}.
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. CNGA1 subfamily. {ECO:0000256|ARBA:ARBA00010530}.
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DR AlphaFoldDB; A0A2K6BXM6; -.
DR Ensembl; ENSMNET00000040382.1; ENSMNEP00000016168.1; ENSMNEG00000032099.1.
DR GeneTree; ENSGT00940000156074; -.
DR OMA; IYYNWLF; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000032099; Expressed in pituitary gland.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
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; 1.20.5.170; -; 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:SF9; CYCLIC NUCLEOTIDE-GATED CHANNEL ROD PHOTORECEPTOR SUBUNIT ALPHA; 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 Reference proteome {ECO:0000313|Proteomes:UP000233120};
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};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT TRANSMEM 285..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..567
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 31..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 77500 MW; D942DAF8FC8DA1A3 CRC64;
MKKNIVNTQQ SFVNMPNVIV PDIEKEIRKM ENGACSSFSE DDDSASVSEE SENENHHARG
SFSYKSHRKG GPSQREQYLP GAIALFNVNN SSNKDHKSDD KNENKKDLEK KKKKKDKEKK
KKEEKSKDKK EEEKKEVVVI DPSGNTYYNW LFCITLPVMY NWTMVIARSC FDELQSDYLE
YWLILDYVSD IVYLIDMFVR TRTGYLEQGL LVKEELKLIN KYKSNLQFKL DVLSLIPTDL
LYFKLGWNYP EIRLNRLLRI SRMFEFFQRT ETRTNYPNIF RISNLVMYIV IIIHWNACVY
YSISKAIGFG NDTWVYPDTN DPEFGRLARK YVYSLYWSTL TLTTIGETPP PVRDSEYVFV
VVDFLIGVLI FATIVGNIGS MISNMNAARA EFQARIDAIK QYMHFRNVSK DMEKRVIKWF
DYLWTNKKTV DEKEVLKYLP DKLRAEIAIN VHLDTLKKVR IFADCEAGLL VELVLKLQPQ
VYSPGDYICK KGDIGREMYI IKEGKLAVVA DDGVTQFVVL SDGSYFGEIS ILNIKGSKAG
NRRTANIKSI GYSDLFCLSK DDLMEALTEY PDAKTMLEEK GKQILMKDGL LDLNIANAGS
DPKDLEEKVT RMEGSVDLLQ TRFARILAEY ESMQQKLKQR LTKVEKFLKP LIDTEFSSIE
GPGVESGPID ST
//
