ADCY9_CHICK
ID ADCY9_CHICK Reviewed; 1334 AA.
AC Q9DGG6;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Adenylate cyclase type 9;
DE EC=4.6.1.1 {ECO:0000269|PubMed:11322775};
DE AltName: Full=ATP pyrophosphate-lyase 9;
DE AltName: Full=Adenylate cyclase type IX {ECO:0000303|PubMed:11322775};
DE AltName: Full=Adenylyl cyclase 9;
GN Name=ADCY9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=11322775; DOI=10.1006/bbrc.2001.4725;
RA Cui H., Green R.D.;
RT "Cell-specific properties of type V and type IX adenylyl cyclase isozymes
RT in 293T cells and embryonic chick ventricular myocytes.";
RL Biochem. Biophys. Res. Commun. 283:107-112(2001).
CC -!- FUNCTION: Adenylyl cyclase that catalyzes the formation of the
CC signaling molecule cAMP in response to activation of G protein-coupled
CC receptors. {ECO:0000269|PubMed:11322775}.
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:11322775};
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 Activity is down-regulated by calcium/calcineurin.
CC {ECO:0000250|UniProtKB:O60503}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60503};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O60503}. Membrane
CC {ECO:0000269|PubMed:11322775}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic heart (at protein level).
CC {ECO:0000269|PubMed:11322775}.
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}.
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DR EMBL; AJ401469; CAC04147.1; -; mRNA.
DR AlphaFoldDB; Q9DGG6; -.
DR SMR; Q9DGG6; -.
DR STRING; 9031.ENSGALP00000012606; -.
DR PaxDb; Q9DGG6; -.
DR PRIDE; Q9DGG6; -.
DR VEuPathDB; HostDB:geneid_395339; -.
DR eggNOG; KOG3618; Eukaryota.
DR InParanoid; Q9DGG6; -.
DR PhylomeDB; Q9DGG6; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004016; F:adenylate cyclase activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006171; P:cAMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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..1334
FT /note="Adenylate cyclase type 9"
FT /id="PRO_0000195710"
FT TOPO_DOM 1..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..768
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 790..800
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 850..870
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 871..873
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 874..894
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 895..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 903..923
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 924..957
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 958..978
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 979..1334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..28
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 338..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 388..393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 388
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 388
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 389
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 430..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 432
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 432
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 476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 1090
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1167..1169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1174..1178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 946
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1334 AA; 149292 MW; F05594AADE1CC403 CRC64;
MASPPHQQLL HHHSTEVSCD SSGDSNSVTV RINPRQQQAL SAKRCKYSIS SSCSSGESGG
VGRGGGGGLR RQKKLPQLFE RASSRWWDPK FDSTNLEEAS MERCFPQTQR RFRYALFYIG
SACLLWGIYF GVHMREKQMV FMVPALCFLL VCVAFFAFTF TKAYARRYVW TSGYTLLVFA
LTLAPQFQPW TLGERQRVQP RPAAPVDTCL SQVGSFSMCV EVLLLLYTVM HLPLYLSLFL
GLSYSVLFET SAFRDESCTL LGGGAVYWEL LSKAFLHVCI HAIGIHLFIM SEVRSRSTFL
KVGQSIMHGK DLEVEKALKE RMIHSVMPRI IADDLMKQGD DESENSVKRH STSSPKNRKK
KPSIQKTPII FRPFKMQQIE QVSILFADIV GFTKMSANKS AHALVGLLND LFGRFDRLCE
DTKCEKISTL GDCYYCVAGC PEPRADHAYC CIEMGLGMIK AIEQFCQEKK EMVNMRVGVH
TGTVLCGILG MRRFKFDVWS NDVNLANLME QLGVAGKVHI SEATAKYLDD RYEMEDGKVT
ERVGQSAVAD QLKGLKTYLI SGQKVKEPHC SCSQALLQLG GWGWSQMQAA PSAENTADST
KALKHVEKPK PCPSCSTTLV PPCDVSIDEG AIQNGCQDEH KNSTKAPGGH SPKTQNGLLS
PPQEEKLSNS QTSLYEMLQE KGRWGGVSLD QSALLPLRFK NIREKTDAHF VDVIKEDSLM
KDYFFKPPIS KLSLNFLDQD LEMAYRTSYQ EEVMRNAPVK TFASATFSSL LDVFLSTTVF
LILSVTCFLK HGMVASPPPP AAVVVFVIAI LLEVLSLVIS VRMVFFLEEV MACTKRLLEL
ISGWLPRHFL GAILVSLPAL AVFSHFTSDF ETNIHYTMFM CCAILIAIVQ YCNFCQLSSW
MRSLLATVVG AVLLILLYVS LCPDSSVETL HLDLAQNLSS RKSPCNSSMP ADVKRPADLI
GQEVILAVFL LLLLVWFLNR SFEVSYRLHY HGDVEADLHR TKIQSMRDQP DSCVRNIIPY
HVADELKVSQ SYSKNHDSGG VIFASIVNFS EFYEENYEGG KECYRVLNEL IGDFDELLSK
PHYSSIEKIK TIGATYMAAS GLNTSQCQDS NHPHGHLQTL FEFAKEMMRV VDDFNNNMLW
FNFKLRIGFN HGPLTAGVIG TTKLLYDIWG DTVNIASRMD TIGVECRIQV SEETYRILSK
MGYDFDYRGT VNVKGKGQMK TYLYPKCMDN GIVPHHQLSI SPDIRVQVDG SIGRSPTDEI
ANLVPSVQNS DKTAHATDNS ETKDALPSSK KLQKEPTKAE ERCRFGKAVE KTDCEEAGTE
EVNELTKLNV SKSV
