ADCY9_HUMAN
ID ADCY9_HUMAN Reviewed; 1353 AA.
AC O60503; A7E2V5; A7E2X2; D3DUD1; O60273; Q4ZHT9; Q4ZIR5; Q9BWT4; Q9UGP2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 4.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Adenylate cyclase type 9 {ECO:0000303|PubMed:9628827};
DE EC=4.6.1.1 {ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952, ECO:0000269|PubMed:15879435, ECO:0000269|PubMed:9628827};
DE AltName: Full=ATP pyrophosphate-lyase 9;
DE AltName: Full=Adenylate cyclase type IX {ECO:0000303|PubMed:10987815};
DE Short=ACIX {ECO:0000303|PubMed:10987815};
DE AltName: Full=Adenylyl cyclase 9;
DE Short=AC9 {ECO:0000303|PubMed:15879435};
GN Name=ADCY9; Synonyms=KIAA0520;
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 [MRNA], CATALYTIC ACTIVITY, FUNCTION, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9628827; DOI=10.1006/geno.1998.5293;
RA Hacker B.M., Tomlinson J.E., Wayman G.A., Sultana R., Chan G.,
RA Villacres E., Disteche C., Storm D.R.;
RT "Cloning, chromosomal mapping, and regulatory properties of the human type
RT 9 adenylyl cyclase (ADCY9).";
RL Genomics 50:97-104(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND VARIANT MET-772.
RX PubMed=12972952; DOI=10.1097/00008571-200309000-00002;
RA Small K.M., Brown K.M., Theiss C.T., Seman C.A., Weiss S.T., Liggett S.B.;
RT "An Ile to Met polymorphism in the catalytic domain of adenylyl cyclase
RT type 9 confers reduced beta2-adrenergic receptor stimulation.";
RL Pharmacogenetics 13:535-541(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND VARIANT MET-772.
RX PubMed=15879435; DOI=10.1093/hmg/ddi175;
RA Tantisira K.G., Small K.M., Litonjua A.A., Weiss S.T., Liggett S.B.;
RT "Molecular properties and pharmacogenetics of a polymorphism of adenylyl
RT cyclase type 9 in asthma: interaction between beta-agonist and
RT corticosteroid pathways.";
RL Hum. Mol. Genet. 14:1671-1677(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT SER-1154.
RX PubMed=10987815; DOI=10.1046/j.1471-4159.2000.0751358.x;
RA Paterson J.M., Smith S.M., Simpson J., Grace O.C., Sosunov A.A., Bell J.E.,
RA Antoni F.A.;
RT "Characterisation of human adenylyl cyclase IX reveals inhibition by
RT Ca(2+)/Calcineurin and differential mRNA plyadenylation.";
RL J. Neurochem. 75:1358-1367(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Toyota T., Yamada K., Meerabux J., Hattori E., Saito K., Yoshitsugu K.,
RA Shimizu H., Nankai M., Toru M., Detera-Wadleigh S.D., Yoshikawa T.;
RT "Mutation screening, case control study and transmission disequilibrium
RT analysis of adenylate cyclase type 9 (ADCY9) gene in functional
RT psychoses.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-1154.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [7]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [8]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Ishikawa K.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-1154.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1259, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1307, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1257 AND SER-1259, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION BY
RP 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Adenylyl cyclase that catalyzes the formation of the
CC signaling molecule cAMP in response to activation of G protein-coupled
CC receptors (PubMed:9628827, PubMed:12972952, PubMed:15879435,
CC PubMed:10987815). Contributes to signaling cascades activated by CRH
CC (corticotropin-releasing factor), corticosteroids and beta-adrenergic
CC receptors (PubMed:9628827). {ECO:0000269|PubMed:10987815,
CC ECO:0000269|PubMed:12972952, ECO:0000269|PubMed:15879435,
CC ECO:0000269|PubMed:9628827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000269|PubMed:10987815, ECO:0000269|PubMed:12972952,
CC ECO:0000269|PubMed:15879435, ECO:0000269|PubMed:9628827};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P30803};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P30803};
CC Note=Binds 2 magnesium ions per subunit. Is also active with manganese
CC (in vitro). {ECO:0000250|UniProtKB:P30803};
CC -!- ACTIVITY REGULATION: Insensitive to calcium/calmodulin, forskolin and
CC somatostatin. Stimulated by beta-adrenergic receptor activation
CC (PubMed:9628827). Activity is down-regulated by calcium/calcineurin
CC (PubMed:10987815). {ECO:0000269|PubMed:10987815,
CC ECO:0000269|PubMed:9628827}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10987815,
CC ECO:0000269|PubMed:9628827}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle, pancreas, lung, heart,
CC kidney, liver, brain and placenta (PubMed:9628827, PubMed:10987815).
CC Expressed in multiple cells of the lung, with expression highest in
CC airway smooth muscle (PubMed:12972952). {ECO:0000269|PubMed:10987815,
CC ECO:0000269|PubMed:12972952, ECO:0000269|PubMed:9628827}.
CC -!- DOMAIN: The protein contains two modules with six transmembrane helices
CC each; both are required for catalytic activity. Isolated N-terminal or
CC C-terminal guanylate cyclase domains have no catalytic activity, but
CC when they are brought together, enzyme activity is restored. The active
CC site is at the interface of the two domains. Both contribute substrate-
CC binding residues, but the catalytic metal ions are bound exclusively
CC via the N-terminal guanylate cyclase domain.
CC {ECO:0000250|UniProtKB:P26769}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24201.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA25446.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF036927; AAC24201.1; ALT_FRAME; mRNA.
DR EMBL; DQ008441; AAY27880.1; -; mRNA.
DR EMBL; DQ005545; AAY21237.1; -; mRNA.
DR EMBL; AJ133123; CAB65084.1; -; mRNA.
DR EMBL; AY028959; AAK29464.1; -; Genomic_DNA.
DR EMBL; AY028949; AAK29464.1; JOINED; Genomic_DNA.
DR EMBL; AY028950; AAK29464.1; JOINED; Genomic_DNA.
DR EMBL; AY028951; AAK29464.1; JOINED; Genomic_DNA.
DR EMBL; AY028952; AAK29464.1; JOINED; Genomic_DNA.
DR EMBL; AY028953; AAK29464.1; JOINED; Genomic_DNA.
DR EMBL; AY028954; AAK29464.1; JOINED; Genomic_DNA.
DR EMBL; AY028955; AAK29464.1; JOINED; Genomic_DNA.
DR EMBL; AY028956; AAK29464.1; JOINED; Genomic_DNA.
DR EMBL; AY028957; AAK29464.1; JOINED; Genomic_DNA.
DR EMBL; AB011092; BAA25446.3; ALT_INIT; mRNA.
DR EMBL; CH471112; EAW85331.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85332.1; -; Genomic_DNA.
DR EMBL; BC136657; AAI36658.1; -; mRNA.
DR EMBL; BC136658; AAI36659.1; -; mRNA.
DR EMBL; BC151207; AAI51208.1; -; mRNA.
DR EMBL; BC151229; AAI51230.1; -; mRNA.
DR CCDS; CCDS32382.1; -.
DR RefSeq; NP_001107.2; NM_001116.3.
DR AlphaFoldDB; O60503; -.
DR SMR; O60503; -.
DR BioGRID; 106628; 152.
DR IntAct; O60503; 23.
DR MINT; O60503; -.
DR STRING; 9606.ENSP00000294016; -.
DR BindingDB; O60503; -.
DR ChEMBL; CHEMBL2655; -.
DR GlyGen; O60503; 3 sites.
DR iPTMnet; O60503; -.
DR PhosphoSitePlus; O60503; -.
DR BioMuta; ADCY9; -.
DR CPTAC; CPTAC-1229; -.
DR CPTAC; CPTAC-1230; -.
DR EPD; O60503; -.
DR jPOST; O60503; -.
DR MassIVE; O60503; -.
DR MaxQB; O60503; -.
DR PaxDb; O60503; -.
DR PeptideAtlas; O60503; -.
DR PRIDE; O60503; -.
DR ProteomicsDB; 49441; -.
DR Antibodypedia; 55436; 238 antibodies from 31 providers.
DR DNASU; 115; -.
DR Ensembl; ENST00000294016.8; ENSP00000294016.3; ENSG00000162104.10.
DR GeneID; 115; -.
DR KEGG; hsa:115; -.
DR MANE-Select; ENST00000294016.8; ENSP00000294016.3; NM_001116.4; NP_001107.2.
DR UCSC; uc002cvx.4; human.
DR CTD; 115; -.
DR DisGeNET; 115; -.
DR GeneCards; ADCY9; -.
DR HGNC; HGNC:240; ADCY9.
DR HPA; ENSG00000162104; Tissue enhanced (skeletal).
DR MIM; 603302; gene.
DR neXtProt; NX_O60503; -.
DR OpenTargets; ENSG00000162104; -.
DR PharmGKB; PA30; -.
DR VEuPathDB; HostDB:ENSG00000162104; -.
DR eggNOG; KOG3618; Eukaryota.
DR GeneTree; ENSGT00940000155577; -.
DR HOGENOM; CLU_001072_12_0_1; -.
DR InParanoid; O60503; -.
DR OMA; PYIQTYL; -.
DR OrthoDB; 430975at2759; -.
DR PhylomeDB; O60503; -.
DR TreeFam; TF313845; -.
DR PathwayCommons; O60503; -.
DR Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
DR Reactome; R-HSA-163615; PKA activation.
DR Reactome; R-HSA-164378; PKA activation in glucagon signalling.
DR Reactome; R-HSA-170660; Adenylate cyclase activating pathway.
DR Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-9634597; GPER1 signaling.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR SignaLink; O60503; -.
DR SIGNOR; O60503; -.
DR BioGRID-ORCS; 115; 16 hits in 1069 CRISPR screens.
DR ChiTaRS; ADCY9; human.
DR GeneWiki; ADCY9; -.
DR GenomeRNAi; 115; -.
DR Pharos; O60503; Tbio.
DR PRO; PR:O60503; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O60503; protein.
DR Bgee; ENSG00000162104; Expressed in secondary oocyte and 199 other tissues.
DR ExpressionAtlas; O60503; baseline and differential.
DR Genevisible; O60503; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004016; F:adenylate cyclase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd07302; CHD; 2.
DR Gene3D; 3.30.70.1230; -; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 2.
DR SUPFAM; SSF55073; SSF55073; 2.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; cAMP biosynthesis; Cell membrane; Glycoprotein; Lyase;
KW Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1353
FT /note="Adenylate cyclase type 9"
FT /id="PRO_0000195708"
FT TOPO_DOM 1..117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..818
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 819..839
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 840..867
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 868..888
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 889..891
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 892..912
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 913..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 921..941
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 942..975
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 976..996
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 997..1353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 394..521
FT /note="Guanylate cyclase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT DOMAIN 1058..1198
FT /note="Guanylate cyclase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 399..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 399
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 399
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 400
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 441..443
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 443
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 1108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1185..1187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1192..1196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51830"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51830"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51830"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51830"
FT MOD_RES 1307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 955
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 964
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 772
FT /note="I -> M (found in 37.5% of the Asian population, in
FT 30% of the Caucasian population and in 16.3% of the
FT African-American population; reduced adenylyl cyclase
FT activity in response to stimulation of the beta-adregnergic
FT receptor by Mn(2+) agonists isoproteronol and NaF;
FT increased albuterol-stimulated adenylyl cyclase activity in
FT the presence of corticosteroid; dbSNP:rs2230739)"
FT /evidence="ECO:0000269|PubMed:12972952,
FT ECO:0000269|PubMed:15879435"
FT /id="VAR_023750"
FT VARIANT 1154
FT /note="N -> S (in dbSNP:rs61731445)"
FT /evidence="ECO:0000269|PubMed:10987815,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9628581"
FT /id="VAR_070887"
FT CONFLICT 493
FT /note="G -> R (in Ref. 4; CAB65084)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="V -> A (in Ref. 4; CAB65084)"
FT /evidence="ECO:0000305"
FT CONFLICT 1308
FT /note="P -> R (in Ref. 4; CAB65084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1353 AA; 150701 MW; 4CBF051EA49B5B7B CRC64;
MASPPHQQLL HHHSTEVSCD SSGDSNSVRV KINPKQLSSN SHPKHCKYSI SSSCSSSGDS
GGVPRRVGGG GRLRRQKKLP QLFERASSRW WDPKFDSVNL EEACLERCFP QTQRRFRYAL
FYIGFACLLW SIYFAVHMRS RLIVMVAPAL CFLLVCVGFF LFTFTKLYAR HYAWTSLALT
LLVFALTLAA QFQVLTPVSG RGDSSNLTAT ARPTDTCLSQ VGSFSMCIEV LFLLYTVMHL
PLYLSLCLGV AYSVLFETFG YHFRDEACFP SPGAGALHWE LLSRGLLHGC IHAIGVHLFV
MSQVRSRSTF LKVGQSIMHG KDLEVEKALK ERMIHSVMPR IIADDLMKQG DEESENSVKR
HATSSPKNRK KKSSIQKAPI AFRPFKMQQI EEVSILFADI VGFTKMSANK SAHALVGLLN
DLFGRFDRLC EETKCEKIST LGDCYYCVAG CPEPRADHAY CCIEMGLGMI KAIEQFCQEK
KEMVNMRVGV HTGTVLCGIL GMRRFKFDVW SNDVNLANLM EQLGVAGKVH ISEATAKYLD
DRYEMEDGKV IERLGQSVVA DQLKGLKTYL ISGQRAKESR CSCAEALLSG FEVIDGSQVS
SGPRGQGTAS SGNVSDLAQT VKTFDNLKTC PSCGITFAPK SEAGAEGGAP QNGCQDEHKN
STKASGGPNP KTQNGLLSPP QEEKLTNSQT SLCEILQEKG RWAGVSLDQS ALLPLRFKNI
REKTDAHFVD VIKEDSLMKD YFFKPPINQF SLNFLDQELE RSYRTSYQEE VIKNSPVKTF
ASPTFSSLLD VFLSTTVFLT LSTTCFLKYE AATVPPPPAA LAVFSAALLL EVLSLAVSIR
MVFFLEDVMA CTKRLLEWIA GWLPRHCIGA ILVSLPALAV YSHVTSEYET NIHFPVFTGS
AALIAVVHYC NFCQLSSWMR SSLATVVGAG PLLLLYVSLC PDSSVLTSPL DAVQNFSSER
NPCNSSVPRD LRRPASLIGQ EVVLVFFLLL LLVWFLNREF EVSYRLHYHG DVEADLHRTK
IQSMRDQADW LLRNIIPYHV AEQLKVSQTY SKNHDSGGVI FASIVNFSEF YEENYEGGKE
CYRVLNELIG DFDELLSKPD YSSIEKIKTI GATYMAASGL NTAQAQDGSH PQEHLQILFE
FAKEMMRVVD DFNNNMLWFN FKLRVGFNHG PLTAGVIGTT KLLYDIWGDT VNIASRMDTT
GVECRIQVSE ESYRVLSKMG YDFDYRGTVN VKGKGQMKTY LYPKCTDHRV IPQHQLSISP
DIRVQVDGSI GRSPTDEIAN LVPSVQYVDK TSLGSDSSTQ AKDAHLSPKR PWKEPVKAEE
RGRFGKAIEK DDCDETGIEE ANELTKLNVS KSV
