ADCY9_XENLA
ID ADCY9_XENLA Reviewed; 1305 AA.
AC P98999;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Adenylate cyclase type 9;
DE EC=4.6.1.1 {ECO:0000269|PubMed:9074644};
DE AltName: Full=ATP pyrophosphate-lyase 9;
DE AltName: Full=Adenylate cyclase type IX;
DE AltName: Full=Adenylyl cyclase 9;
DE Short=xlAC {ECO:0000303|PubMed:9074644};
GN Name=adcy9;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=9074644; DOI=10.1016/s0014-5793(97)00100-2;
RA Torrejon M., Echeverria V., Retamales G., Herrera L., Hinrichs M.V.,
RA Olate J.;
RT "Molecular cloning and expression of an adenylyl cyclase from Xenopus
RT laevis oocytes.";
RL FEBS Lett. 404:91-94(1997).
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:9074644}.
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:9074644};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60503};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O60503}.
CC -!- TISSUE SPECIFICITY: Detected in oocytes. {ECO:0000269|PubMed:9074644}.
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; Z46958; CAA87082.1; -; mRNA.
DR RefSeq; NP_001079302.1; NM_001085833.1.
DR AlphaFoldDB; P98999; -.
DR SMR; P98999; -.
DR GeneID; 378610; -.
DR KEGG; xla:378610; -.
DR CTD; 378610; -.
DR Xenbase; XB-GENE-999261; adcy9.L.
DR OrthoDB; 430975at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 378610; Expressed in muscle tissue and 19 other tissues.
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 Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1305
FT /note="Adenylate cyclase type 9"
FT /id="PRO_0000195711"
FT TOPO_DOM 1..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..134
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..164
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800..810
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 811..831
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 832..859
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 881..883
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 884..904
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 905..911
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 933..966
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 988..1305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 46..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 393..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 393
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 393
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 394
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 435..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 437
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 437
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 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P30803"
FT BINDING 1099
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1176..1178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1183..1187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT BINDING 1223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P26769"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 946
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 951
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1305 AA; 145411 MW; 8E1A5B79466B556A CRC64;
MASPVNQQLL HHTEVRCDGS GDGSSVTVRI NRQHHQAPSR RCKYSISSSC SSGESGVKKT
GGSGGARRQK KLPQLFERST SNWWNPKFDS NNLEEACVER CFPQTQRRFR YALMYLSVAG
LLWSIYFSVH MKTKLVSHLV PTLCFLIVCL GFFFFTFTKS YARHCTAISL LVTLLVFTLT
LASQFQVLNP GLGSDSLSNL TSFSATGSSS CLSQVGSFSI CVEVLLLLYT VMHLPLYLSA
CLGVAYSILF ETFGYHFRDE SCFVLLVGRM AHWELLSKAL LHVCIHAIGV HLFIMSEVRS
RSTFLKVGQS IMHGKDLEVE KALKERMIHS VMPRIIADDL MKQGDDESEN SVKRHSASSP
KSRKKKSSIQ KTPIIFRPFK MQRIEQVSIL FADIVGFTKM SANKSAHALV GLLNDLFGRF
DRLCEETKCE KISTLGDCYY CVAGCPEPRP DHAYCCIEMG LGMIEAIDQF CQEKKEMVNM
RVGVHTGTVL CGILGMRRFK FDVWSNDVNL ANLMEQLGVA GKVHISEKTA RYLDDRYLME
DSMVVERLGQ IVAADQLKGL KTFLISGGRT RVPSCSCSQT LIPVQEGTDL SSPSLAPHVQ
AAISETSDSH TNCTQPETLK SCPSCGETAA RDGPEEGVSA ANGGGEEWKG GAPRPSAIGA
SLKDPERSPE SSTGDTLTNS QASLYDMLQE KGRWCGVSMD QSALLPLRFK NIREKTDAHF
VEVIKEDSLM KDYFFKPPIN PLSLNFLDKE LETSYRASYQ EEVIRMAPVK TFASATFSSL
QDVLLNYFIF VLLSVACLLK PGTNTVSPPT LALVLLSVCG LLGFLSLLVS VRMAFYLEDM
LLCTRRLLEI ISGWVPRHFI GTVLVCLPAA VIFSYLSSDF YTDIHYTMFL CSALLIPMVQ
YCNFCQLSSS ALLLATITGA TMLILIYLPL CPQRPPLDPG TDIEANLSTS NSSYETLDNP
RTELPFTRLG QEIAVAYFLL LLLVWFLNRE FDVSYRLHYH GDVEADLHRT KIQSMRDQAD
WLLRNIIPYH VAEQLKVSQS YSKNHDDAGV IFASIVNFSE FYEENYEGGK ECYRALNELI
GDFDELLSKP HYSCIEKIKT IGATYMAASG LNPSQCQDSS QPHRHLQTLF EFAKEMMSVV
DEFNNNMLWF NFKLRIGFNH GPLTAGVIGT TKLLYDIWGD TVNIASRMDT TGVECRIQAS
EESYRVLVKM GYDFDYRGTV NVKGKGQMKT YHFPKCTDNG GLVPHHQLCI SPDIRVQVDG
SIGRSPTDEI SSLVTGGKGA VELGSGEAER KREKAEERGR DGGAR
