ID Q80XL8_MOUSE Unreviewed; 866 AA. AC Q80XL8; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 130. DE SubName: Full=Cngb1 protein {ECO:0000313|EMBL:AAH45114.1}; DE Flags: Fragment; GN Name=Cngb1 {ECO:0000313|EMBL:AAH45114.1, ECO:0000313|MGI:MGI:2664102}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH45114.1}; RN [1] {ECO:0000313|EMBL:AAH45114.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye {ECO:0000313|EMBL:AAH45114.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. 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 EMBL; BC045114; AAH45114.1; -; mRNA. DR RefSeq; NP_001182342.1; NM_001195413.1. DR AlphaFoldDB; Q80XL8; -. DR ELM; Q80XL8; -. DR TCDB; 1.A.1.5.4; the voltage-gated ion channel (vic) superfamily. DR iPTMnet; Q80XL8; -. DR PhosphoSitePlus; Q80XL8; -. DR DNASU; 333329; -. DR GeneID; 333329; -. DR KEGG; mmu:333329; -. DR AGR; MGI:2664102; -. DR CTD; 1258; -. DR MGI; MGI:2664102; Cngb1. DR OrthoDB; 74296at2759; -. DR BioGRID-ORCS; 333329; 5 hits in 79 CRISPR screens. DR ChiTaRS; Cngb1; mouse. DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0043195; C:terminal bouton; ISO:MGI. DR GO; GO:1902495; C:transmembrane transporter complex; ISO:MGI. DR GO; GO:0030553; F:cGMP binding; ISO:MGI. DR GO; GO:0043855; F:cyclic nucleotide-activated monoatomic ion channel activity; IMP:MGI. DR GO; GO:0005222; F:intracellular cAMP-activated cation channel activity; ISO:MGI. DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISO:MGI. DR GO; GO:0098655; P:monoatomic cation transmembrane transport; IBA:GO_Central. DR GO; GO:0006812; P:monoatomic cation transport; ISO:MGI. DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI. DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:MGI. DR GO; GO:0007602; P:phototransduction; IMP:MGI. DR GO; GO:0033365; P:protein localization to organelle; IMP:MGI. DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:0001895; P:retina homeostasis; ISO:MGI. DR GO; GO:0007608; P:sensory perception of smell; IMP:MGI. 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; IPR014710; RmlC-like_jellyroll. DR PANTHER; PTHR45638:SF16; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL BETA-1; 1. DR PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1. DR Pfam; PF00027; cNMP_binding; 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. DR Genevisible; Q80XL8; MM. PE 2: Evidence at transcript level; 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|SAM:Phobius}; KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 268..286 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 306..326 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 579..683 FT /note="Cyclic nucleotide-binding" FT /evidence="ECO:0000259|PROSITE:PS50042" FT REGION 20..178 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 200..235 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 767..866 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 41..60 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 98..115 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 130..144 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 153..178 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 200..220 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 767..782 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 791..817 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAH45114.1" SQ SEQUENCE 866 AA; 97427 MW; CACC4AD8EB6DEE2A CRC64; EEEPIVLLDS CLVVQADVDE CQLERTPSEL ASIQELPEEK EEKEEEKEEE KEEEEEKKEE EVEKKEEGEA TNSTVPATKE HPELQVEDTD ADSGPLIPEE TLPPPERPPP SPVKSDTLTV PGAAAAGHRK KLPSQDDEAE ELKALSPAES PVVAWSDPTT PQEADGQDRA ASTASQNSAI INDRLQELVK MFKERTEKVK EKLIDPDVTS DEESPKPSPA KKAPEPDPAQ KPAEAEVAEE EHYCDMLCCK FKRRPLKMYR FPQSIDPLTN LMYILWLFFV VLAWNWNCWL IPVRWAFPYQ RADNIHFWLL MDYLCDFIYL LDITVFQMRL QFVKGGDIIT DKKEMRNNYL KSRRFKMDLL CLLPLDFLYL KLGINPLLRL PRCLKYMAFF EFNNRLEAIL SKAYVYRVIR TTAYLLYSLH LNSCLYYWAS AFQGIGSTHW VYDGVGNSYI RCYYWAVKTL ITIGGLPDPQ TLFEIVFQLL NYFTGVFAFS VMIGQMRDVV GAATAGQTYY RSCMDSTVKY MNFYKIPRSV QNRVKTWYEY TWHSQGMLDE SELMVQLPDK MRLDLAIDVN YSIVSKVALF QGCDRQMIFD MLKRLRSVVY LPNDYVCKKG EIGREMYIIQ AGQVQVLGGP DGKAVLVTLK AGSVFGEISL LAVGGGNRRT ANVVAHGFTN LFILDKKDLN EILVHYPESQ KLLRKKARRM LRNNNKPKEE KSVLILPPRA GTPKLFNAAL AAAGKMGPRG AKGGKLAHLR ARLKELAALE AAARQQQLLE QAKSSQEAGG EEGSGATDQP APQEPPEPKD PPKPPGPPEP SAQSSPPPAS AKPEESTGEA AGPPEPSVRI RVSPGPDPGE QTLSVEVLEE KKEGAE //