CNGB1_HUMAN
ID CNGB1_HUMAN Reviewed; 1251 AA.
AC Q14028; H3BN09; O43636; Q13059; Q14029; Q9UMG2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Cyclic nucleotide-gated cation channel beta-1;
DE AltName: Full=Cyclic nucleotide-gated cation channel 4;
DE Short=CNG channel 4;
DE Short=CNG-4;
DE Short=CNG4;
DE AltName: Full=Cyclic nucleotide-gated cation channel gamma;
DE AltName: Full=Cyclic nucleotide-gated cation channel modulatory subunit;
DE AltName: Full=Cyclic nucleotide-gated channel beta-1;
DE Short=CNG channel beta-1;
DE AltName: Full=Glutamic acid-rich protein;
DE Short=GARP;
GN Name=CNGB1; Synonyms=CNCG2, CNCG3L, CNCG4, RCNC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS RCNC2A AND RCNC2B).
RC TISSUE=Retina;
RX PubMed=7682292; DOI=10.1038/362764a0;
RA Chen T.-Y., Peng Y.-W., Dhallan R.S., Ahamed B., Reed R.R., Yau K.-W.;
RT "A new subunit of the cyclic nucleotide-gated cation channel in retinal
RT rods.";
RL Nature 362:764-767(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GARP2), AND VARIANT HIS-100.
RC TISSUE=Retina;
RX PubMed=7590744; DOI=10.1006/geno.1995.1102;
RA Ardell M.D., Makhija A.K., Oliveira L., Miniou P., Viegas-Pequignot E.,
RA Pittler S.J.;
RT "cDNA, gene structure, and chromosomal localization of human GAR1 (CNCG3L),
RT a homolog of the third subunit of bovine photoreceptor cGMP-gated
RT channel.";
RL Genomics 28:32-38(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RCNC2B), AND VARIANT HIS-100.
RC TISSUE=Retina;
RX PubMed=8766832; DOI=10.1016/0014-5793(96)00588-1;
RA Ardell M.D., Aragon I., Oliveira L., Porche G.E., Burke E., Pittler S.J.;
RT "The beta subunit of human rod photoreceptor cGMP-gated cation channel is
RT generated from a complex transcription unit.";
RL FEBS Lett. 389:213-218(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RCNC2B), FUNCTION, AND VARIANT HIS-100.
RC TISSUE=Retina;
RX PubMed=9535905; DOI=10.1074/jbc.273.15.9148;
RA Grunwald M.E., Yu W.P., Yu H.H., Yau K.W.;
RT "Identification of a domain on the beta-subunit of the rod cGMP-gated
RT cation channel that mediates inhibition by calcium-calmodulin.";
RL J. Biol. Chem. 273:9148-9157(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP ALTERNATIVE SPLICING.
RX PubMed=10717482; DOI=10.1016/s0378-1119(00)00023-8;
RA Ardell M.D., Bedsole D.L., Schoborg R.V., Pittler S.J.;
RT "Genomic organization of the human rod photoreceptor cGMP-gated cation
RT channel beta-subunit gene.";
RL Gene 245:311-318(2000).
RN [8]
RP MUTAGENESIS OF LEU-568.
RX PubMed=15195096; DOI=10.1038/nn1266;
RA Bradley J., Boenigk W., Yau K.-W., Frings S.;
RT "Calmodulin permanently associates with rat olfactory CNG channels under
RT native conditions.";
RL Nat. Neurosci. 7:705-710(2004).
RN [9]
RP ALTERNATIVE SPLICING (ISOFORM GARP2), AND FUNCTION.
RX PubMed=16407240; DOI=10.1074/jbc.m507488200;
RA Pentia D.C., Hosier S., Cote R.H.;
RT "The glutamic acid-rich protein-2 (GARP2) is a high affinity rod
RT photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its
RT catalytic properties.";
RL J. Biol. Chem. 281:5500-5505(2006).
RN [10]
RP CHARACTERIZATION OF THE GARPS PROTEINS.
RX PubMed=16280326; DOI=10.1074/jbc.m505012200;
RA Batra-Safferling R., Abarca-Heidemann K., Korschen H.G., Tziatzios C.,
RA Stoldt M., Budyak I., Willbold D., Schwalbe H., Klein-Seetharaman J.,
RA Kaupp U.B.;
RT "Glutamic acid-rich proteins of rod photoreceptors are natively unfolded.";
RL J. Biol. Chem. 281:1449-1460(2006).
RN [11]
RP ALTERNATIVE SPLICING (ISOFORM GARP2).
RA Cote R.H.;
RL Unpublished observations (MAY-2009).
RN [12]
RP VARIANT RP45 VAL-993.
RX PubMed=11379879; DOI=10.1007/s004390100496;
RA Bareil C., Hamel C.P., Delague V., Arnaud B., Demaille J., Claustres M.;
RT "Segregation of a mutation in CNGB1 encoding the beta-subunit of the rod
RT cGMP-gated channel in a family with autosomal recessive retinitis
RT pigmentosa.";
RL Hum. Genet. 108:328-334(2001).
CC -!- FUNCTION: Subunit of cyclic nucleotide-gated (CNG) channels,
CC nonselective cation channels, which play important roles in both visual
CC and olfactory signal transduction. When associated with CNGA1, it is
CC involved in the regulation of ion flow into the rod photoreceptor outer
CC segment (ROS), in response to light-induced alteration of the levels of
CC intracellular cGMP.
CC -!- FUNCTION: Isoform GARP2 is a high affinity rod photoreceptor
CC phosphodiesterase (PDE6)-binding protein that modulates its catalytic
CC properties: it is a regulator of spontaneous activation of rod PDE6,
CC thereby serving to lower rod photoreceptor 'dark noise' and allowing
CC these sensory cells to operate at the single photon detection limit.
CC -!- SUBUNIT: Tetramer formed of three CNGA1 and one CNGB1 modulatory
CC subunits. {ECO:0000250}.
CC -!- INTERACTION:
CC Q14028; Q5ICW4: GRB14; Xeno; NbExp=2; IntAct=EBI-7959609, EBI-7639273;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=There is no evidence for an ortholog to bovine GARP1 in the
CC human genome.;
CC Name=RCNC2B;
CC IsoId=Q14028-1; Sequence=Displayed;
CC Name=RCNC2A;
CC IsoId=Q14028-2; Sequence=VSP_001110;
CC Name=GARP2; Synonyms=GARP;
CC IsoId=Q14028-3; Sequence=VSP_037921, VSP_037922;
CC Name=4;
CC IsoId=Q14028-4; Sequence=VSP_053421;
CC -!- DISEASE: Retinitis pigmentosa 45 (RP45) [MIM:613767]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:11379879}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: [Isoform GARP2]: In the rod cells, the CNGB1 locus
CC encodes the cyclic nucleotide-gated cation channel beta-1 subunit and
CC several glutamic-acid-rich proteins (GARPs). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC 1.A.1.5) family. CNGB1 subfamily. {ECO:0000305}.
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DR EMBL; L15296; AAA65620.1; -; Genomic_DNA.
DR EMBL; L15297; AAA65619.1; -; Genomic_DNA.
DR EMBL; U18945; AAA91633.1; -; mRNA.
DR EMBL; U58837; AAB63387.1; -; mRNA.
DR EMBL; AF042498; AAC04830.1; -; mRNA.
DR EMBL; AC010543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW82957.1; -; Genomic_DNA.
DR CCDS; CCDS42169.1; -. [Q14028-1]
DR CCDS; CCDS45495.1; -. [Q14028-3]
DR CCDS; CCDS67042.1; -. [Q14028-4]
DR PIR; A57652; A57652.
DR PIR; S32538; S32538.
DR PIR; S69275; S69275.
DR RefSeq; NP_001129111.1; NM_001135639.1. [Q14028-3]
DR RefSeq; NP_001273059.1; NM_001286130.1. [Q14028-4]
DR RefSeq; NP_001288.3; NM_001297.4. [Q14028-1]
DR PDB; 7RH9; EM; 2.61 A; B=454-1251.
DR PDB; 7RHG; EM; 2.88 A; B=454-1251.
DR PDB; 7RHH; EM; 3.31 A; B=454-1251.
DR PDB; 7RHI; EM; 3.31 A; B=454-1251.
DR PDB; 7RHJ; EM; 2.88 A; B=454-1251.
DR PDB; 7RHK; EM; 3.27 A; B=454-1251.
DR PDB; 7RHL; EM; 3.03 A; B=454-1251.
DR PDBsum; 7RH9; -.
DR PDBsum; 7RHG; -.
DR PDBsum; 7RHH; -.
DR PDBsum; 7RHI; -.
DR PDBsum; 7RHJ; -.
DR PDBsum; 7RHK; -.
DR PDBsum; 7RHL; -.
DR AlphaFoldDB; Q14028; -.
DR SMR; Q14028; -.
DR BioGRID; 107658; 4.
DR IntAct; Q14028; 2.
DR MINT; Q14028; -.
DR STRING; 9606.ENSP00000251102; -.
DR TCDB; 1.A.1.5.3; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q14028; -.
DR PhosphoSitePlus; Q14028; -.
DR BioMuta; CNGB1; -.
DR DMDM; 257051004; -.
DR EPD; Q14028; -.
DR MassIVE; Q14028; -.
DR PaxDb; Q14028; -.
DR PeptideAtlas; Q14028; -.
DR PRIDE; Q14028; -.
DR ProteomicsDB; 41062; -.
DR ProteomicsDB; 59797; -. [Q14028-1]
DR ProteomicsDB; 59798; -. [Q14028-2]
DR ProteomicsDB; 59799; -. [Q14028-3]
DR Antibodypedia; 48567; 121 antibodies from 21 providers.
DR DNASU; 1258; -.
DR Ensembl; ENST00000251102.13; ENSP00000251102.8; ENSG00000070729.14. [Q14028-1]
DR Ensembl; ENST00000311183.8; ENSP00000311670.4; ENSG00000070729.14. [Q14028-3]
DR Ensembl; ENST00000564448.5; ENSP00000454633.1; ENSG00000070729.14. [Q14028-4]
DR GeneID; 1258; -.
DR KEGG; hsa:1258; -.
DR MANE-Select; ENST00000251102.13; ENSP00000251102.8; NM_001297.5; NP_001288.3.
DR UCSC; uc002emt.3; human. [Q14028-1]
DR CTD; 1258; -.
DR DisGeNET; 1258; -.
DR GeneCards; CNGB1; -.
DR GeneReviews; CNGB1; -.
DR HGNC; HGNC:2151; CNGB1.
DR HPA; ENSG00000070729; Tissue enriched (retina).
DR MalaCards; CNGB1; -.
DR MIM; 600724; gene.
DR MIM; 613767; phenotype.
DR neXtProt; NX_Q14028; -.
DR OpenTargets; ENSG00000070729; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA26662; -.
DR VEuPathDB; HostDB:ENSG00000070729; -.
DR eggNOG; KOG0499; Eukaryota.
DR GeneTree; ENSGT00940000154824; -.
DR HOGENOM; CLU_005746_11_0_1; -.
DR InParanoid; Q14028; -.
DR OMA; EEVEPHW; -.
DR OrthoDB; 1073751at2759; -.
DR PhylomeDB; Q14028; -.
DR TreeFam; TF318250; -.
DR PathwayCommons; Q14028; -.
DR Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-HSA-381753; Olfactory Signaling Pathway. [Q14028-3]
DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium.
DR SignaLink; Q14028; -.
DR BioGRID-ORCS; 1258; 15 hits in 1062 CRISPR screens.
DR ChiTaRS; CNGB1; human.
DR GeneWiki; CNGB1; -.
DR GenomeRNAi; 1258; -.
DR Pharos; Q14028; Tbio.
DR PRO; PR:Q14028; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q14028; protein.
DR Bgee; ENSG00000070729; Expressed in buccal mucosa cell and 135 other tissues.
DR ExpressionAtlas; Q14028; baseline and differential.
DR Genevisible; Q14028; HS.
DR GO; GO:0060170; C:ciliary membrane; TAS:Reactome.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; TAS:Reactome.
DR GO; GO:0017071; C:intracellular cyclic nucleotide activated cation channel complex; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1902495; C:transmembrane transporter complex; IDA:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; TAS:ProtInc.
DR GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0006812; P:cation transport; IDA:UniProtKB.
DR GO; GO:0050911; P:detection of chemical stimulus involved in sensory perception of smell; ISS:ARUK-UCL.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProtKB.
DR GO; GO:0099105; P:ion channel modulating, G protein-coupled receptor signaling pathway; ISS:ARUK-UCL.
DR GO; GO:0051899; P:membrane depolarization; ISS:ARUK-UCL.
DR GO; GO:0021630; P:olfactory nerve maturation; ISS:ARUK-UCL.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR GO; GO:0007602; P:phototransduction; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0033365; P:protein localization to organelle; IEA:Ensembl.
DR GO; GO:1990834; P:response to odorant; ISS:ARUK-UCL.
DR GO; GO:0001895; P:retina homeostasis; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR032944; CNGB1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45638:SF16; PTHR45638:SF16; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; cAMP; cAMP-binding; Disease variant;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Nucleotide-binding; Olfaction; Reference proteome; Retinitis pigmentosa;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport;
KW Vision.
FT CHAIN 1..1251
FT /note="Cyclic nucleotide-gated cation channel beta-1"
FT /id="PRO_0000219323"
FT TOPO_DOM 343..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..675
FT /note="Helical; Name=H1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..689
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 690..708
FT /note="Helical; Name=H2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..753
FT /note="Helical; Name=H3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..790
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..813
FT /note="Helical; Name=H4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 814..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 858..877
FT /note="Helical; Name=H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 878..961
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 962..982
FT /note="Helical; Name=H6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 983..1251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 568..578
FT /note="IQ-like"
FT COMPBIAS 26..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..375
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 970..1109
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250"
FT BINDING 1030
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000255"
FT BINDING 1042
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..628
FT /note="Missing (in isoform RCNC2A)"
FT /evidence="ECO:0000305"
FT /id="VSP_001110"
FT VAR_SEQ 189..194
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_053421"
FT VAR_SEQ 292..299
FT /note="ISILPGGQ -> RVMGAGGL (in isoform GARP2)"
FT /evidence="ECO:0000303|PubMed:7590744"
FT /id="VSP_037921"
FT VAR_SEQ 300..1251
FT /note="Missing (in isoform GARP2)"
FT /evidence="ECO:0000303|PubMed:7590744"
FT /id="VSP_037922"
FT VARIANT 100
FT /note="R -> H (in dbSNP:rs13336595)"
FT /evidence="ECO:0000269|PubMed:7590744,
FT ECO:0000269|PubMed:8766832, ECO:0000269|PubMed:9535905"
FT /id="VAR_058691"
FT VARIANT 479
FT /note="L -> I (in dbSNP:rs2303783)"
FT /id="VAR_059225"
FT VARIANT 535
FT /note="V -> A (in dbSNP:rs12927214)"
FT /id="VAR_059226"
FT VARIANT 731
FT /note="N -> K (in dbSNP:rs376270)"
FT /id="VAR_059227"
FT VARIANT 745
FT /note="L -> I (in dbSNP:rs10459809)"
FT /id="VAR_059228"
FT VARIANT 911
FT /note="K -> R (in dbSNP:rs2303785)"
FT /id="VAR_059229"
FT VARIANT 961
FT /note="A -> S (in dbSNP:rs16942445)"
FT /id="VAR_059230"
FT VARIANT 993
FT /note="G -> V (in RP45; dbSNP:rs121918532)"
FT /evidence="ECO:0000269|PubMed:11379879"
FT /id="VAR_060491"
FT MUTAGEN 568
FT /note="L->E: Loss of calcium/calmodulin modulation."
FT /evidence="ECO:0000269|PubMed:15195096"
FT CONFLICT 128
FT /note="I -> V (in Ref. 5; AC010543)"
FT /evidence="ECO:0000305"
FT CONFLICT 1148..1149
FT /note="QQ -> HE (in Ref. 2; AAB63387 and 1; AAA65619/
FT AAA65620)"
FT /evidence="ECO:0000305"
FT CONFLICT 1207..1208
FT /note="RP -> SC (in Ref. 2; AAB63387 and 1; AAA65619/
FT AAA65620)"
FT /evidence="ECO:0000305"
FT TURN 650..652
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 654..679
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 688..707
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 715..717
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 725..734
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 736..745
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 759..767
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 770..782
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 783..785
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 787..816
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 820..824
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 829..832
FT /evidence="ECO:0007829|PDB:7RHL"
FT HELIX 833..843
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 855..886
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 888..906
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 911..928
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 929..931
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 933..939
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 942..959
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 961..963
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 968..977
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 979..983
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 992..995
FT /evidence="ECO:0007829|PDB:7RHJ"
FT STRAND 998..1005
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 1007..1012
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 1017..1022
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 1027..1029
FT /evidence="ECO:0007829|PDB:7RHI"
FT HELIX 1030..1033
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 1036..1038
FT /evidence="ECO:0007829|PDB:7RH9"
FT STRAND 1046..1058
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 1059..1066
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 1070..1083
FT /evidence="ECO:0007829|PDB:7RH9"
FT HELIX 1107..1129
FT /evidence="ECO:0007829|PDB:7RHL"
SQ SEQUENCE 1251 AA; 139678 MW; 7A45CB399EB2B20C CRC64;
MLGWVQRVLP QPPGTPRKTK MQEEEEVEPE PEMEAEVEPE PNPEEAETES ESMPPEESFK
EEEVAVADPS PQETKEAALT STISLRAQGA EISEMNSPSR RVLTWLMKGV EKVIPQPVHS
ITEDPAQILG HGSTGDTGCT DEPNEALEAQ DTRPGLRLLL WLEQNLERVL PQPPKSSEVW
RDEPAVATGA ASDPAPPGRP QEMGPKLQAR ETPSLPTPIP LQPKEEPKEA PAPEPQPGSQ
AQTSSLPPTR DPARLVAWVL HRLEMALPQP VLHGKIGEQE PDSPGICDVQ TISILPGGQV
EPDLVLEEVE PPWEDAHQDV STSPQGTEVV PAYEEENKAV EKMPRELSRI EEEKEDEEEE
EEEEEEEEEE EVTEVLLDSC VVSQVGVGQS EEDGTRPQST SDQKLWEEVG EEAKKEAEEK
AKEEAEEVAE EEAEKEPQDW AETKEEPEAE AEAASSGVPA TKQHPEVQVE DTDADSCPLM
AEENPPSTVL PPPSPAKSDT LIVPSSASGT HRKKLPSEDD EAEELKALSP AESPVVAWSD
PTTPKDTDGQ DRAASTASTN SAIINDRLQE LVKLFKERTE KVKEKLIDPD VTSDEESPKP
SPAKKAPEPA PDTKPAEAEP VEEEHYCDML CCKFKHRPWK KYQFPQSIDP LTNLMYVLWL
FFVVMAWNWN CWLIPVRWAF PYQTPDNIHH WLLMDYLCDL IYFLDITVFQ TRLQFVRGGD
IITDKKDMRN NYLKSRRFKM DLLSLLPLDF LYLKVGVNPL LRLPRCLKYM AFFEFNSRLE
SILSKAYVYR VIRTTAYLLY SLHLNSCLYY WASAYQGLGS THWVYDGVGN SYIRCYYFAV
KTLITIGGLP DPKTLFEIVF QLLNYFTGVF AFSVMIGQMR DVVGAATAGQ TYYRSCMDST
VKYMNFYKIP KSVQNRVKTW YEYTWHSQGM LDESELMVQL PDKMRLDLAI DVNYNIVSKV
ALFQGCDRQM IFDMLKRLRS VVYLPNDYVC KKGEIGREMY IIQAGQVQVL GGPDGKSVLV
TLKAGSVFGE ISLLAVGGGN RRTANVVAHG FTNLFILDKK DLNEILVHYP ESQKLLRKKA
RRMLRSNNKP KEEKSVLILP PRAGTPKLFN AALAMTGKMG GKGAKGGKLA HLRARLKELA
ALEAAAKQQE LVEQAKSSQD VKGEEGSAAP DQHTHPKEAA TDPPAPRTPP EPPGSPPSSP
PPASLGRPEG EEEGPAEPEE HSVRICMSPG PEPGEQILSV KMPEEREEKA E
