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Adenylate cyclase type 1 (EC 4.6.1.1) (ATP pyrophosphate-lyase 1) (Adenylate cyclase type I) (Adenylyl cyclase 1) (AC1) (Ca(2 )/calmodulin-activated adenylyl cyclase)

 ADCY1_BOVIN             Reviewed;        1134 AA.
P19754;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
10-MAY-2017, entry version 135.
RecName: Full=Adenylate cyclase type 1;
EC=4.6.1.1 {ECO:0000269|PubMed:19029295, ECO:0000269|PubMed:2022671, ECO:0000269|PubMed:2472670};
AltName: Full=ATP pyrophosphate-lyase 1;
AltName: Full=Adenylate cyclase type I;
AltName: Full=Adenylyl cyclase 1 {ECO:0000305};
Short=AC1 {ECO:0000303|PubMed:19029295};
AltName: Full=Ca(2+)/calmodulin-activated adenylyl cyclase {ECO:0000305};
Name=ADCY1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
TISSUE=Brain;
PubMed=2472670; DOI=10.1126/science.2472670;
Krupinski J., Coussen F., Bakalyar H.A., Tang W.-J., Feinstein P.G.,
Orth K., Slaughter C., Reed R.R., Gilman A.G.;
"Adenylyl cyclase amino acid sequence: possible channel- or
transporter-like structure.";
Science 244:1558-1564(1989).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ENZYME REGULATION,
AND GLYCOSYLATION.
PubMed=2022671;
Tang W.J., Krupinski J., Gilman A.G.;
"Expression and characterization of calmodulin-activated (type I)
adenylylcyclase.";
J. Biol. Chem. 266:8595-8603(1991).
[3]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ENZYME REGULATION,
MUTAGENESIS OF PHE-503, AND INTERACTION WITH CALM.
PubMed=19029295; DOI=10.1074/jbc.M807359200;
Masada N., Ciruela A., Macdougall D.A., Cooper D.M.;
"Distinct mechanisms of regulation by Ca2+/calmodulin of type 1 and 8
adenylyl cyclases support their different physiological roles.";
J. Biol. Chem. 284:4451-4463(2009).
[4]
3D-STRUCTURE MODELING OF 295-450; 861-936 AND 950-1045.
PubMed=9391039; DOI=10.1073/pnas.94.25.13414;
Liu Y., Ruoho A.E., Rao V.D., Hurley J.H.;
"Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling
and mutational analysis.";
Proc. Natl. Acad. Sci. U.S.A. 94:13414-13419(1997).
-!- FUNCTION: Catalyzes the formation of the signaling molecule cAMP
in response to G-protein signaling (PubMed:2472670,
PubMed:2022671. PubMed:19029295). Mediates responses to increased
cellular Ca(2+)/calmodulin levels (PubMed:2022671,
PubMed:19029295). May be involved in regulatory processes in the
central nervous system. May play a role in memory and learning.
Plays a role in the regulation of the circadian rhythm of daytime
contrast sensitivity probably by modulating the rhythmic synthesis
of cyclic AMP in the retina (By similarity).
{ECO:0000250|UniProtKB:O88444, ECO:0000269|PubMed:19029295,
ECO:0000269|PubMed:2022671, ECO:0000269|PubMed:2472670}.
-!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
{ECO:0000269|PubMed:19029295, ECO:0000269|PubMed:2022671,
ECO:0000269|PubMed:2472670}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:2022671};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:2022671};
Note=Binds 2 magnesium ions per subunit. Is also active with
manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
-!- ENZYME REGULATION: Activated by calcium/calmodulin
(PubMed:2022671, PubMed:19029295). Activated by forskolin
(PubMed:2472670). Activated by the G protein alpha subunit GNAS
(PubMed:2022671). Inhibited by the G protein beta and gamma
subunit complex (PubMed:2022671). Inhibited by the ATP analogs
adenosine, 2'-deoxyadenosine and 2'-deoxy-3'-AMP (PubMed:2022671).
{ECO:0000269|PubMed:19029295, ECO:0000269|PubMed:2022671,
ECO:0000269|PubMed:2472670}.
-!- SUBUNIT: Interacts with CALM. {ECO:0000269|PubMed:19029295}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:2022671,
ECO:0000269|PubMed:2472670}; Multi-pass membrane protein
{ECO:0000305|PubMed:2022671, ECO:0000305|PubMed:2472670}. Cell
membrane {ECO:0000269|PubMed:19029295,
ECO:0000269|PubMed:2022671}; Multi-pass membrane protein
{ECO:0000305|PubMed:2022671}. Cytoplasm
{ECO:0000250|UniProtKB:O88444}. Membrane raft
{ECO:0000269|PubMed:19029295}. Note=Expressed in the cytoplasm of
supporting cells and hair cells of the cochlea vestibule, as well
as to the cochlear hair cell nuclei and stereocilia.
{ECO:0000250|UniProtKB:O88444}.
-!- TISSUE SPECIFICITY: Detected in brain cortex (at protein level).
Detected in brain. {ECO:0000269|PubMed:2472670}.
-!- DOMAIN: The protein contains two modules with six transmembrane
helices each; both are required for catalytic activity. Isolated
N-terminal or C-terminal guanylate cyclase domains have no
catalytic activity, but when they are brought together, enzyme
activity is restored. The active site is at the interface of the
two domains. Both contribute substrate-binding residues, but the
catalytic metal ions are bound exclusively via the N-terminal
guanylate cyclase domain. {ECO:0000250|UniProtKB:P30803}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:2022671}.
-!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
-----------------------------------------------------------------------
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EMBL; M25579; AAA79957.1; -; mRNA.
PIR; A41350; A41350.
RefSeq; NP_776654.1; NM_174229.2.
UniGene; Bt.517; -.
PDB; 1AWK; Model; -; A=295-1058.
PDBsum; 1AWK; -.
ProteinModelPortal; P19754; -.
SMR; P19754; -.
STRING; 9913.ENSBTAP00000012528; -.
BindingDB; P19754; -.
ChEMBL; CHEMBL3549; -.
iPTMnet; P19754; -.
PaxDb; P19754; -.
PRIDE; P19754; -.
GeneID; 281601; -.
KEGG; bta:281601; -.
CTD; 107; -.
eggNOG; KOG3619; Eukaryota.
eggNOG; COG2114; LUCA.
HOGENOM; HOG000006941; -.
HOVERGEN; HBG050458; -.
InParanoid; P19754; -.
KO; K08041; -.
BRENDA; 4.6.1.1; 908.
PRO; PR:P19754; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0008074; C:guanylate cyclase complex, soluble; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
GO; GO:1904322; P:cellular response to forskolin; IMP:UniProtKB.
GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
Gene3D; 3.30.70.1230; -; 2.
InterPro; IPR001054; A/G_cyclase.
InterPro; IPR018297; A/G_cyclase_CS.
InterPro; IPR032628; AC_N.
InterPro; IPR030672; Adcy.
InterPro; IPR029787; Nucleotide_cyclase.
Pfam; PF16214; AC_N; 1.
Pfam; PF00211; Guanylate_cyc; 2.
PIRSF; PIRSF039050; Ade_cyc; 1.
SMART; SM00044; CYCc; 2.
SUPFAM; SSF55073; SSF55073; 2.
PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
1: Evidence at protein level;
3D-structure; ATP-binding; Biological rhythms; Calmodulin-binding;
cAMP biosynthesis; Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycoprotein; Lyase; Magnesium; Manganese;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix.
CHAIN 1 1134 Adenylate cyclase type 1.
/FTId=PRO_0000195681.
TOPO_DOM 1 65 Cytoplasmic. {ECO:0000255}.
TRANSMEM 66 86 Helical. {ECO:0000255}.
TRANSMEM 90 110 Helical. {ECO:0000255}.
TRANSMEM 127 147 Helical. {ECO:0000255}.
TRANSMEM 154 174 Helical. {ECO:0000255}.
TRANSMEM 184 204 Helical. {ECO:0000255}.
TRANSMEM 216 236 Helical. {ECO:0000255}.
TOPO_DOM 237 612 Cytoplasmic. {ECO:0000255}.
TRANSMEM 613 633 Helical. {ECO:0000255}.
TRANSMEM 637 657 Helical. {ECO:0000255}.
TRANSMEM 676 696 Helical. {ECO:0000255}.
TOPO_DOM 697 726 Extracellular. {ECO:0000255}.
TRANSMEM 727 747 Helical. {ECO:0000255}.
TRANSMEM 755 775 Helical. {ECO:0000255}.
TRANSMEM 777 797 Helical. {ECO:0000255}.
TOPO_DOM 798 1134 Cytoplasmic. {ECO:0000255}.
DOMAIN 305 432 Guanylate cyclase 1.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
DOMAIN 871 1013 Guanylate cyclase 2.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
NP_BIND 310 315 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 352 354 ATP. {ECO:0000250|UniProtKB:P30803}.
NP_BIND 1000 1002 ATP. {ECO:0000250|UniProtKB:P26769}.
NP_BIND 1007 1011 ATP. {ECO:0000250|UniProtKB:P26769}.
REGION 495 522 Interaction with calmodulin.
{ECO:0000305}.
REGION 1027 1050 Interaction with calmodulin.
{ECO:0000250}.
COMPBIAS 3 34 Gly-rich.
METAL 310 310 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 310 310 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 311 311 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00099}.
METAL 354 354 Magnesium 1; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
METAL 354 354 Magnesium 2; catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00099}.
BINDING 398 398 ATP. {ECO:0000250|UniProtKB:P30803}.
BINDING 923 923 ATP. {ECO:0000250|UniProtKB:P26769}.
BINDING 1047 1047 ATP. {ECO:0000250|UniProtKB:P26769}.
MOD_RES 553 553 Phosphoserine.
{ECO:0000250|UniProtKB:O88444}.
CARBOHYD 706 706 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 503 503 F->A: Impairs interaction with CALM and
responses to Ca(2+)/calmodulin.
{ECO:0000269|PubMed:19029295}.
SEQUENCE 1134 AA; 123979 MW; CC4A10BCE224DFF3 CRC64;
MAGAPRGRGG GGGGGGAGES GGAERAAGPG GRRGLRACDE EFACPELEAL FRGYTLRLEQ
AATLKALAVL SLLAGALALA ELLGAPGPAP GLAKGSHPVH CVLFLALLVV TNVRSLQVPQ
LQQVGQLALL FSLTFALLCC PFALGGPAGA HAGAAAVPAT ADQGVWQLLL VTFVSYALLP
VRSLLAIGFG LVVAASHLLV TATLVPAKRP RLWRTLGANA LLFLGVNVYG IFVRILAERA
QRKAFLQARN CIEDRLRLED ENEKQERLLM SLLPRNVAME MKEDFLKPPE RIFHKIYIQR
HDNVSILFAD IVGFTGLASQ CTAQELVKLL NELFGKFDEL ATENHCRRIK ILGDCYYCVS
GLTQPKTDHA HCCVEMGLDM IDTITSVAEA TEVDLNMRVG LHTGRVLCGV LGLRKWQYDV
WSNDVTLANV MEAAGLPGKV HITKTTLACL NGDYEVEPGH GHERNSFLKT HNIETFFIVP
SHRRKIFPGL ILSDIKPAKR MKFKTVCYLL VQLMHCRKMF KAEIPFSNVM TCEDDDKRRA
LRTASEKLRN RSSFSTNVVQ TTPGTRVNRY IGRLLEARQM ELEMADLNFF TLKYKQAERE
RKYHQLQDEY FTSAVVLALI LAALFGLVYL LIIPQSVAVL LLLVFCICFL VACVLYLHIT
RVQCFPGCLT IQIRTVLCIF IVVLIYSVAQ GCVVGCLPWS WSSSPNGSLV VLSSGGRDPV
LPVPPCESAP HALLCGLVGT LPLAIFLRVS SLPKMILLAV LTTSYILVLE LSGYTKAMGA
GAISGRSFEP IMAILLFSCT LALHARQVDV KLRLDYLWAA QAEEERDDME KVKLDNKRIL
FNLLPAHVAQ HFLMSNPRNM DLYYQSYSQV GVMFASIPNF NDFYIELDGN NMGVECLRLL
NEIIADFDEL MDKDFYKDLE KIKTIGSTYM AAVGLAPTAG TKAKKCISSH LSTLADFAIE
MFDVLDEINY QSYNDFVLRV GINVGPVVAG VIGARRPQYD IWGNTVNVAS RMDSTGVQGR
IQVTEEVHRL LRRGSYRFVC RGKVSVKGKG EMLTYFLEGR TDGNGSQTRS LNSERKMYPF
GRAGLQTRLA AGHPPVPPAA GLPVGAGPGA LQGSGLAPGP PGQHLPPGAS GKEA


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