ID A0A3Q7UTP8_VULVU Unreviewed; 782 AA.
AC A0A3Q7UTP8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cyclic nucleotide-gated cation channel beta-3 {ECO:0000313|RefSeq:XP_025870650.1};
GN Name=CNGB3 {ECO:0000313|RefSeq:XP_025870650.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025870650.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025870650.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025870650.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025870650.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_025870650.1; XM_026014865.1.
DR AlphaFoldDB; A0A3Q7UTP8; -.
DR STRING; 9627.ENSVVUP00000002217; -.
DR Ensembl; ENSVVUT00000003133; ENSVVUP00000002217; ENSVVUG00000001785.
DR KEGG; vvp:112932010; -.
DR OrthoDB; 74296at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:1902495; C:transmembrane transporter complex; IEA:Ensembl.
DR GO; GO:0030553; F:cGMP binding; IEA:Ensembl.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IEA:Ensembl.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
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:SF8; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL BETA-3; 1.
DR PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 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 4: Predicted;
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:UP000286640};
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 213..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 519..623
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 89364 MW; BB4C85A80B176758 CRC64;
MFKSLTIKSN KVKPREENDE NKQGPDASNQ PQQSTRQGEN KSENKSLQTK MTPVTFEESH
AKIQDKISEK NSLRDLTTNP NHQHPTESKG AMPEQKEMET GKEGLVSPKS KPLGVPVINE
YADAQLHNLV RRMRQRTMLY KKKLAEGDIS SPEASPQTAK PTAIPSTQES NAKLKEEHYY
HILCFKFQKM PLTEYLKRIR LPGSIDSYTD RLYLLWLLLV TIAYNWNCWL IPLRLVFPYQ
TPDNTHYWFI TDITCDIIYL CDMLLIQPRL QFIKGGDIMV DSNELKRHYR SSTKFQLDVA
SVMPFDVFYL FFGFNPVFRM NRILKYTSFF EFNHHLESIM DKAYIYRVIR TTGYLLYTLH
INACIYYWAS DYEGIGSTKW VYNGEGNKYL RCYYWAVRTL ITIGGLPEPQ TSFEIVFQLL
NFFSGVFVFS SLIGQMQDVI GAATANQNNF RISMDHTISY MNTYSIPKNV QNRVRTWYEY
TWDSQRMLDE SDLLCTLPVT MQLALTVDVN LSIISKVELF KGCDTQMIYD MLLRLKSTVY
LPGDFVCKKG EIGKEMYIIK QGEVQVLGGS DGAQVLVTLK AGAVFGEISL LAGRGGNRRT
ANVIAHGFAN LLTLDKKTLQ EILVHYPDSE KLLMKKASVL LKKKAPATET TPPRKGLAFL
FPPKQETPKI FKALLGGTGK AGLTRLLKLK REQTIQKTSE NSEEGEGKRR EYEDKEREPS
KKILDSSECR ANCIIAEEMP QSIRRAALPR GTTHQSLIIS MAPSAEAGEE VLTIEVKEKA
KQ
//
