ID KGP2_HUMAN Reviewed; 762 AA. AC Q13237; B4DMX3; E7EPE6; O00125; O60916; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JUN-2018, entry version 168. DE RecName: Full=cGMP-dependent protein kinase 2; DE Short=cGK 2; DE Short=cGK2; DE EC=2.7.11.12; DE AltName: Full=cGMP-dependent protein kinase II; DE Short=cGKII; GN Name=PRKG2; Synonyms=PRKGR2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8607838; DOI=10.1006/bbrc.1996.0477; RA Orstavik S., Solberg R., Taskn K., Nordahl M., Altherr M.R., RA Hansson V., Jahnsen T., Sandberg M.; RT "Molecular cloning, cDNA structure, and chromosomal localization of RT the human type II cGMP-dependent protein kinase."; RL Biochem. Biophys. Res. Commun. 220:759-765(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7498513; DOI=10.1016/0014-5793(95)01223-2; RA Fujii M., Ogata T., Takahashi E., Yamada K., Nakabayashi K., Oishi M., RA Ayusawa D.; RT "Expression of the human cGMP-dependent protein kinase II gene is lost RT upon introduction of SV40 T antigen or immortalization in human RT cells."; RL FEBS Lett. 375:263-267(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Heart; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-734. RX PubMed=9535793; DOI=10.1006/bbrc.1998.8399; RA Witczak O., Orstavik S., Natarajan V., Frengen E., Jahnsen T., RA Sandberg M.; RT "Characterization of the gene encoding the human type II cGMP- RT dependent protein kinase."; RL Biochem. Biophys. Res. Commun. 245:113-119(1998). RN [6] RP MYRISTOYLATION AT GLY-2, AND SUBCELLULAR LOCATION. RX PubMed=8636133; DOI=10.1074/jbc.271.12.7025; RA Vaandrager A.B., Ehlert E.M., Jarchau T., Lohmann S.M., de Jonge H.R.; RT "N-terminal myristoylation is required for membrane localization of RT cGMP-dependent protein kinase type II."; RL J. Biol. Chem. 271:7025-7029(1996). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP VARIANTS [LARGE SCALE ANALYSIS] ARG-106 AND ARG-716. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 137-418 IN COMPLEX WITH CAMP RP AND CGMP, ENZYME REGULATION, AND MUTAGENESIS OF ASP-412 AND ARG-415. RX PubMed=26769964; DOI=10.1074/jbc.M115.691303; RA Campbell J.C., Kim J.J., Li K.Y., Huang G.Y., Reger A.S., Matsuda S., RA Sankaran B., Link T.M., Yuasa K., Ladbury J.E., Casteel D.E., Kim C.; RT "Structural basis of cyclic nucleotide selectivity in cGMP-dependent RT protein kinase II."; RL J. Biol. Chem. 291:5623-5633(2016). CC -!- FUNCTION: Crucial regulator of intestinal secretion and bone CC growth (By similarity). Phosphorylates and activates CFTR on the CC plasma membrane. Plays a key role in intestinal secretion by CC regulating cGMP-dependent translocation of CFTR in jejunum (By CC similarity). Acts downstream of NMDAR to activate the plasma CC membrane accumulation of GRIA1/GLUR1 in synapse and increase CC synaptic plasticity. Phosphorylates GRIA1/GLUR1 at Ser-863 (By CC similarity). Acts as regulator of gene expression and activator of CC the extracellular signal-regulated kinases MAPK3/ERK1 and CC MAPK1/ERK2 in mechanically stimulated osteoblasts. Under fluid CC shear stress, mediates ERK activation and subsequent induction of CC FOS, FOSL1/FRA1, FOSL2/FRA2 and FOSB that play a key role in the CC osteoblast anabolic response to mechanical stimulation (By CC similarity). {ECO:0000250|UniProtKB:Q61410, CC ECO:0000250|UniProtKB:Q64595}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Binding of cGMP results in enzyme activation. CC {ECO:0000269|PubMed:26769964}. CC -!- SUBUNIT: Interacts with GRIA1/GLUR1. CC {ECO:0000250|UniProtKB:Q64595}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:8636133}; Lipid-anchor CC {ECO:0000269|PubMed:8636133}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13237-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13237-2; Sequence=VSP_055121; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Highly concentrated in brain, lung and CC intestinal mucosa. CC -!- PTM: Myristoylation mediates membrane localization. CC {ECO:0000269|PubMed:8636133}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. cGMP subfamily. {ECO:0000305}. 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; X94612; CAA64318.1; -; mRNA. DR EMBL; D70899; BAA18934.1; -; mRNA. DR EMBL; AK297673; BAG60035.1; -; mRNA. DR EMBL; AC098819; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC139722; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Y16106; CAA76073.1; -; Genomic_DNA. DR EMBL; Y16107; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16108; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16109; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16110; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16111; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16112; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16113; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16114; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16115; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16116; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16117; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16118; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16119; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16120; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16121; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16122; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16123; CAA76073.1; JOINED; Genomic_DNA. DR CCDS; CCDS3589.1; -. [Q13237-1] DR CCDS; CCDS64005.1; -. [Q13237-2] DR PIR; S68217; S68217. DR RefSeq; NP_001269409.1; NM_001282480.1. DR RefSeq; NP_001269410.1; NM_001282481.1. DR RefSeq; NP_001269411.1; NM_001282482.1. DR RefSeq; NP_001269412.1; NM_001282483.1. DR RefSeq; NP_001269414.1; NM_001282485.1. [Q13237-2] DR RefSeq; NP_006250.1; NM_006259.2. [Q13237-1] DR RefSeq; XP_005263183.1; XM_005263126.3. [Q13237-1] DR UniGene; Hs.232044; -. DR UniGene; Hs.570833; -. DR UniGene; Hs.739943; -. DR PDB; 5BV6; X-ray; 1.94 A; A=269-418. DR PDB; 5C6C; X-ray; 2.05 A; A/B=137-277. DR PDB; 5C8W; X-ray; 1.80 A; A/B/C/D/E/F=137-277. DR PDB; 5JIX; X-ray; 1.47 A; A=269-418. DR PDB; 5JIZ; X-ray; 1.50 A; A=269-418. DR PDB; 6BQ8; Other; 2.00 A; A=269-418. DR PDBsum; 5BV6; -. DR PDBsum; 5C6C; -. DR PDBsum; 5C8W; -. DR PDBsum; 5JIX; -. DR PDBsum; 5JIZ; -. DR PDBsum; 6BQ8; -. DR ProteinModelPortal; Q13237; -. DR SMR; Q13237; -. DR BioGrid; 111579; 9. DR IntAct; Q13237; 3. DR STRING; 9606.ENSP00000264399; -. DR BindingDB; Q13237; -. DR ChEMBL; CHEMBL2896; -. DR GuidetoPHARMACOLOGY; 1493; -. DR iPTMnet; Q13237; -. DR PhosphoSitePlus; Q13237; -. DR DMDM; 6226833; -. DR PaxDb; Q13237; -. DR PeptideAtlas; Q13237; -. DR PRIDE; Q13237; -. DR ProteomicsDB; 59241; -. DR DNASU; 5593; -. DR Ensembl; ENST00000264399; ENSP00000264399; ENSG00000138669. [Q13237-1] DR Ensembl; ENST00000395578; ENSP00000378945; ENSG00000138669. [Q13237-1] DR Ensembl; ENST00000628926; ENSP00000486129; ENSG00000138669. [Q13237-2] DR GeneID; 5593; -. DR KEGG; hsa:5593; -. DR UCSC; uc003hmh.3; human. [Q13237-1] DR CTD; 5593; -. DR DisGeNET; 5593; -. DR EuPathDB; HostDB:ENSG00000138669.9; -. DR GeneCards; PRKG2; -. DR HGNC; HGNC:9416; PRKG2. DR HPA; CAB018739; -. DR HPA; HPA007386; -. DR MIM; 601591; gene. DR neXtProt; NX_Q13237; -. DR OpenTargets; ENSG00000138669; -. DR PharmGKB; PA33778; -. DR eggNOG; KOG0616; Eukaryota. DR eggNOG; ENOG410XPQQ; LUCA. DR GeneTree; ENSGT00810000125385; -. DR HOGENOM; HOG000233033; -. DR HOVERGEN; HBG006211; -. DR InParanoid; Q13237; -. DR KO; K19477; -. DR OMA; ELQSKCI; -. DR OrthoDB; EOG091G0S9R; -. DR PhylomeDB; Q13237; -. DR TreeFam; TF313261; -. DR BRENDA; 2.7.11.12; 2681. DR Reactome; R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation. DR Reactome; R-HSA-4086398; Ca2+ pathway. DR Reactome; R-HSA-418457; cGMP effects. DR SignaLink; Q13237; -. DR SIGNOR; Q13237; -. DR GenomeRNAi; 5593; -. DR PRO; PR:Q13237; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000138669; -. DR CleanEx; HS_PRKG2; -. DR ExpressionAtlas; Q13237; baseline and differential. DR Genevisible; Q13237; HS. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW. DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; TAS:Reactome. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc. DR GO; GO:0051186; P:cofactor metabolic process; TAS:Reactome. DR GO; GO:2001226; P:negative regulation of chloride transport; IEA:Ensembl. DR GO; GO:0036289; P:peptidyl-serine autophosphorylation; IEA:Ensembl. DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; IMP:CAFA. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd00038; CAP_ED; 2. DR CDD; cd05572; STKc_cGK; 1. DR Gene3D; 2.60.120.10; -; 2. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR002374; cGMP_dep_kinase. DR InterPro; IPR018490; cNMP-bd-like. DR InterPro; IPR018488; cNMP-bd_CS. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR InterPro; IPR035014; STKc_cGK. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00069; Pkinase; 1. DR PIRSF; PIRSF000559; cGMP-dep_kinase; 1. DR PRINTS; PR00104; CGMPKINASE. DR SMART; SM00100; cNMP; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF51206; SSF51206; 2. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; cGMP; KW cGMP-binding; Coiled coil; Complete proteome; Kinase; Lipoprotein; KW Membrane; Myristate; Nucleotide-binding; Phosphoprotein; Polymorphism; KW Reference proteome; Serine/threonine-protein kinase; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8636133}. FT CHAIN 2 762 cGMP-dependent protein kinase 2. FT /FTId=PRO_0000086123. FT DOMAIN 453 711 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT DOMAIN 712 762 AGC-kinase C-terminal. FT NP_BIND 232 235 cAMP or cGMP 1. {ECO:0000244|PDB:5C6C, FT ECO:0000244|PDB:5C8W, FT ECO:0000269|PubMed:26769964}. FT NP_BIND 242 243 cAMP or cGMP 1. {ECO:0000244|PDB:5C6C, FT ECO:0000244|PDB:5C8W, FT ECO:0000269|PubMed:26769964}. FT NP_BIND 357 359 cAMP or cGMP 2. {ECO:0000244|PDB:5BV6, FT ECO:0000269|PubMed:26769964}. FT NP_BIND 366 367 cAMP or cGMP 2. {ECO:0000244|PDB:5BV6, FT ECO:0000269|PubMed:26769964}. FT NP_BIND 459 467 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT REGION 168 283 cGMP-binding, high affinity; cAMP- FT binding, moderate affinity. FT {ECO:0000305|PubMed:26769964}. FT REGION 286 416 cGMP-binding, high affinity; cAMP- FT binding, low affinity. FT {ECO:0000305|PubMed:26769964}. FT COILED 23 85 {ECO:0000255}. FT ACT_SITE 576 576 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 347 347 cAMP or cGMP 2. FT {ECO:0000269|PubMed:26769964, FT ECO:0000312|PDB:5BV6}. FT BINDING 412 412 cAMP or cGMP 2. FT {ECO:0000269|PubMed:26769964, FT ECO:0000312|PDB:5BV6}. FT BINDING 415 415 cAMP or cGMP 2. FT {ECO:0000269|PubMed:26769964, FT ECO:0000312|PDB:5BV6}. FT BINDING 482 482 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 110 110 Phosphoserine. FT {ECO:0000250|UniProtKB:Q64595}. FT MOD_RES 117 117 Phosphoserine. FT {ECO:0000250|UniProtKB:Q64595}. FT MOD_RES 431 431 Phosphoserine. FT {ECO:0000250|UniProtKB:Q64595}. FT MOD_RES 609 609 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q61410}. FT LIPID 2 2 N-myristoyl glycine. FT {ECO:0000269|PubMed:8636133}. FT VAR_SEQ 441 469 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055121. FT VARIANT 22 22 T -> S (in dbSNP:rs34956759). FT /FTId=VAR_051633. FT VARIANT 106 106 H -> R (in dbSNP:rs34616910). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_040608. FT VARIANT 716 716 W -> R (in a colorectal adenocarcinoma FT sample; somatic mutation). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_040609. FT MUTAGEN 412 412 D->A: Reduces cGMP binding affinity; when FT associated with A-415. FT {ECO:0000269|PubMed:26769964}. FT MUTAGEN 415 415 R->A: Reduces cGMP binding affinity; when FT associated with A-412. FT {ECO:0000269|PubMed:26769964}. FT CONFLICT 57 58 QL -> HG (in Ref. 2; BAA18934). FT {ECO:0000305}. FT CONFLICT 154 154 S -> I (in Ref. 5; CAA76073). FT {ECO:0000305}. FT CONFLICT 388 388 N -> D (in Ref. 3; BAG60035). FT {ECO:0000305}. FT CONFLICT 460 460 G -> A (in Ref. 2; BAA18934). FT {ECO:0000305}. FT HELIX 153 164 {ECO:0000244|PDB:5C8W}. FT HELIX 169 171 {ECO:0000244|PDB:5C8W}. FT HELIX 174 183 {ECO:0000244|PDB:5C8W}. FT STRAND 185 189 {ECO:0000244|PDB:5C8W}. FT STRAND 194 196 {ECO:0000244|PDB:5C8W}. FT STRAND 204 211 {ECO:0000244|PDB:5C8W}. FT STRAND 213 217 {ECO:0000244|PDB:5C8W}. FT STRAND 220 224 {ECO:0000244|PDB:5C8W}. FT STRAND 230 232 {ECO:0000244|PDB:5C8W}. FT HELIX 233 238 {ECO:0000244|PDB:5C8W}. FT STRAND 243 250 {ECO:0000244|PDB:5C8W}. FT STRAND 252 258 {ECO:0000244|PDB:5C8W}. FT HELIX 259 266 {ECO:0000244|PDB:5C8W}. FT HELIX 270 282 {ECO:0000244|PDB:5JIX}. FT HELIX 285 287 {ECO:0000244|PDB:5JIX}. FT HELIX 292 301 {ECO:0000244|PDB:5JIX}. FT STRAND 303 307 {ECO:0000244|PDB:5JIX}. FT STRAND 312 314 {ECO:0000244|PDB:5JIX}. FT STRAND 323 335 {ECO:0000244|PDB:5JIX}. FT STRAND 344 350 {ECO:0000244|PDB:5JIX}. FT HELIX 357 362 {ECO:0000244|PDB:5JIX}. FT STRAND 368 372 {ECO:0000244|PDB:5JIX}. FT STRAND 377 382 {ECO:0000244|PDB:5JIX}. FT HELIX 384 389 {ECO:0000244|PDB:5JIX}. FT HELIX 391 393 {ECO:0000244|PDB:5JIX}. FT HELIX 395 414 {ECO:0000244|PDB:5JIX}. SQ SEQUENCE 762 AA; 87432 MW; FA7BA149906B5996 CRC64; MGNGSVKPKH SKHPDGHSGN LTTDALRNKV TELERELRRK DAEIQEREYH LKELREQLSK QTVAIAELTE ELQNKCIQLN KLQDVVHMQG GSPLQASPDK VPLEVHRKTS GLVSLHSRRG AKAGVSAEPT TRTYDLNKPP EFSFEKARVR KDSSEKKLIT DALNKNQFLK RLDPQQIKDM VECMYGRNYQ QGSYIIKQGE PGNHIFVLAE GRLEVFQGEK LLSSIPMWTT FGELAILYNC TRTASVKAIT NVKTWALDRE VFQNIMRRTA QARDEQYRNF LRSVSLLKNL PEDKLTKIID CLEVEYYDKG DYIIREGEEG STFFILAKGK VKVTQSTEGH DQPQLIKTLQ KGEYFGEKAL ISDDVRSANI IAEENDVACL VIDRETFNQT VGTFEELQKY LEGYVANLNR DDEKRHAKRS MSNWKLSKAL SLEMIQLKEK VARFSSSSPF QNLEIIATLG VGGFGRVELV KVKNENVAFA MKCIRKKHIV DTKQQEHVYS EKRILEELCS PFIVKLYRTF KDNKYVYMLL EACLGGELWS ILRDRGSFDE PTSKFCVACV TEAFDYLHRL GIIYRDLKPE NLILDAEGYL KLVDFGFAKK IGSGQKTWTF CGTPEYVAPE VILNKGHDFS VDFWSLGILV YELLTGNPPF SGVDQMMTYN LILKGIEKMD FPRKITRRPE DLIRRLCRQN PTERLGNLKN GINDIKKHRW LNGFNWEGLK ARSLPSPLQR ELKGPIDHSY FDKYPPEKGM PPDELSGWDK DF //