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   24-JAN-2024, entry version 193.
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
CC       (TC 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   PDB; 8DGH; NMR; -; B=1128-1139.
DR   PDB; 8DGK; NMR; -; B=565-576.
DR   PDBsum; 7RH9; -.
DR   PDBsum; 7RHG; -.
DR   PDBsum; 7RHH; -.
DR   PDBsum; 7RHI; -.
DR   PDBsum; 7RHJ; -.
DR   PDBsum; 7RHK; -.
DR   PDBsum; 7RHL; -.
DR   PDBsum; 8DGH; -.
DR   PDBsum; 8DGK; -.
DR   AlphaFoldDB; Q14028; -.
DR   EMDB; EMD-24458; -.
DR   EMDB; EMD-24460; -.
DR   EMDB; EMD-24461; -.
DR   EMDB; EMD-24462; -.
DR   EMDB; EMD-24463; -.
DR   EMDB; EMD-24464; -.
DR   EMDB; EMD-24465; -.
DR   SMR; Q14028; -.
DR   BioGRID; 107658; 5.
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   GlyGen; Q14028; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q14028; -.
DR   PhosphoSitePlus; Q14028; -.
DR   BioMuta; CNGB1; -.
DR   DMDM; 257051004; -.
DR   EPD; Q14028; -.
DR   MassIVE; Q14028; -.
DR   PaxDb; 9606-ENSP00000251102; -.
DR   PeptideAtlas; Q14028; -.
DR   ProteomicsDB; 41062; -.
DR   ProteomicsDB; 59797; -. [Q14028-1]
DR   ProteomicsDB; 59798; -. [Q14028-2]
DR   ProteomicsDB; 59799; -. [Q14028-3]
DR   Antibodypedia; 48567; 143 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   AGR; HGNC:2151; -.
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; YWASAFE; -.
DR   OrthoDB; 74296at2759; -.
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 1142 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 136 other cell types or tissues.
DR   ExpressionAtlas; Q14028; baseline and differential.
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:0043195; C:terminal bouton; IEA:Ensembl.
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 monoatomic ion channel activity; TAS:ProtInc.
DR   GO; GO:0044877; F:protein-containing complex binding; IBA:GO_Central.
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:0098655; P:monoatomic cation transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006812; P:monoatomic cation transport; IDA:UniProtKB.
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:0051480; P:regulation of cytosolic calcium ion concentration; 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; 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; Q14028; HS.
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;
FT                   AAA65619/AAA65620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1207..1208
FT                   /note="RP -> SC (in Ref. 2; AAB63387 and 1;
FT                   AAA65619/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
//