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Protein

Adenylate cyclase type 1

Gene

ADCY1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 Ca2+/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).By similarity3 Publications

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.3 Publications

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).By similarity

Activity regulationi

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).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi310Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi310Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi311Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi354Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi354Magnesium 2; catalyticPROSITE-ProRule annotation1
Binding sitei398ATPBy similarity1
Binding sitei923ATPBy similarity1
Binding sitei1047ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi310 – 315ATPBy similarity6
Nucleotide bindingi352 – 354ATPBy similarity3
Nucleotide bindingi1000 – 1002ATPBy similarity3
Nucleotide bindingi1007 – 1011ATPBy similarity5

GO - Molecular functioni

  • adenylate cyclase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • calcium- and calmodulin-responsive adenylate cyclase activity Source: UniProtKB
  • calmodulin binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionCalmodulin-binding, Lyase
Biological processBiological rhythms, cAMP biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.1 908

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 1 (EC:4.6.1.13 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 1
Adenylate cyclase type I
Adenylyl cyclase 1Curated
Short name:
AC11 Publication
Ca(2+)/calmodulin-activated adenylyl cyclaseCurated
Gene namesi
Name:ADCY1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 65CytoplasmicSequence analysisAdd BLAST65
Transmembranei66 – 86HelicalSequence analysisAdd BLAST21
Transmembranei90 – 110HelicalSequence analysisAdd BLAST21
Transmembranei127 – 147HelicalSequence analysisAdd BLAST21
Transmembranei154 – 174HelicalSequence analysisAdd BLAST21
Transmembranei184 – 204HelicalSequence analysisAdd BLAST21
Transmembranei216 – 236HelicalSequence analysisAdd BLAST21
Topological domaini237 – 612CytoplasmicSequence analysisAdd BLAST376
Transmembranei613 – 633HelicalSequence analysisAdd BLAST21
Transmembranei637 – 657HelicalSequence analysisAdd BLAST21
Transmembranei676 – 696HelicalSequence analysisAdd BLAST21
Topological domaini697 – 726ExtracellularSequence analysisAdd BLAST30
Transmembranei727 – 747HelicalSequence analysisAdd BLAST21
Transmembranei755 – 775HelicalSequence analysisAdd BLAST21
Transmembranei777 – 797HelicalSequence analysisAdd BLAST21
Topological domaini798 – 1134CytoplasmicSequence analysisAdd BLAST337

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi503F → A: Impairs interaction with CALM and responses to Ca(2+)/calmodulin. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3549

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001956811 – 1134Adenylate cyclase type 1Add BLAST1134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei553PhosphoserineBy similarity1
Glycosylationi706N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP19754
PRIDEiP19754

PTM databases

iPTMnetiP19754

Expressioni

Tissue specificityi

Detected in brain cortex (at protein level). Detected in brain.1 Publication

Interactioni

Subunit structurei

Interacts with CALM.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000012528

Chemistry databases

BindingDBiP19754

Structurei

3D structure databases

ProteinModelPortaliP19754
SMRiP19754
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini305 – 432Guanylate cyclase 1PROSITE-ProRule annotationAdd BLAST128
Domaini871 – 1013Guanylate cyclase 2PROSITE-ProRule annotationAdd BLAST143

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni495 – 522Interaction with calmodulinCuratedAdd BLAST28
Regioni1027 – 1050Interaction with calmodulinBy similarityAdd BLAST24

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi3 – 34Gly-richAdd BLAST32

Domaini

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.By similarity

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619 Eukaryota
COG2114 LUCA
HOGENOMiHOG000006941
HOVERGENiHBG050458
InParanoidiP19754
KOiK08041

Family and domain databases

Gene3Di3.30.70.1230, 2 hits
InterProiView protein in InterPro
IPR001054 A/G_cyclase
IPR018297 A/G_cyclase_CS
IPR032628 AC_N
IPR030672 Adcy
IPR029787 Nucleotide_cyclase
PfamiView protein in Pfam
PF16214 AC_N, 1 hit
PF00211 Guanylate_cyc, 2 hits
PIRSFiPIRSF039050 Ade_cyc, 1 hit
SMARTiView protein in SMART
SM00044 CYCc, 2 hits
SUPFAMiSSF55073 SSF55073, 2 hits
PROSITEiView protein in PROSITE
PS00452 GUANYLATE_CYCLASE_1, 2 hits
PS50125 GUANYLATE_CYCLASE_2, 2 hits

Sequencei

Sequence statusi: Complete.

P19754-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGAPRGRGG GGGGGGAGES GGAERAAGPG GRRGLRACDE EFACPELEAL
60 70 80 90 100
FRGYTLRLEQ AATLKALAVL SLLAGALALA ELLGAPGPAP GLAKGSHPVH
110 120 130 140 150
CVLFLALLVV TNVRSLQVPQ LQQVGQLALL FSLTFALLCC PFALGGPAGA
160 170 180 190 200
HAGAAAVPAT ADQGVWQLLL VTFVSYALLP VRSLLAIGFG LVVAASHLLV
210 220 230 240 250
TATLVPAKRP RLWRTLGANA LLFLGVNVYG IFVRILAERA QRKAFLQARN
260 270 280 290 300
CIEDRLRLED ENEKQERLLM SLLPRNVAME MKEDFLKPPE RIFHKIYIQR
310 320 330 340 350
HDNVSILFAD IVGFTGLASQ CTAQELVKLL NELFGKFDEL ATENHCRRIK
360 370 380 390 400
ILGDCYYCVS GLTQPKTDHA HCCVEMGLDM IDTITSVAEA TEVDLNMRVG
410 420 430 440 450
LHTGRVLCGV LGLRKWQYDV WSNDVTLANV MEAAGLPGKV HITKTTLACL
460 470 480 490 500
NGDYEVEPGH GHERNSFLKT HNIETFFIVP SHRRKIFPGL ILSDIKPAKR
510 520 530 540 550
MKFKTVCYLL VQLMHCRKMF KAEIPFSNVM TCEDDDKRRA LRTASEKLRN
560 570 580 590 600
RSSFSTNVVQ TTPGTRVNRY IGRLLEARQM ELEMADLNFF TLKYKQAERE
610 620 630 640 650
RKYHQLQDEY FTSAVVLALI LAALFGLVYL LIIPQSVAVL LLLVFCICFL
660 670 680 690 700
VACVLYLHIT RVQCFPGCLT IQIRTVLCIF IVVLIYSVAQ GCVVGCLPWS
710 720 730 740 750
WSSSPNGSLV VLSSGGRDPV LPVPPCESAP HALLCGLVGT LPLAIFLRVS
760 770 780 790 800
SLPKMILLAV LTTSYILVLE LSGYTKAMGA GAISGRSFEP IMAILLFSCT
810 820 830 840 850
LALHARQVDV KLRLDYLWAA QAEEERDDME KVKLDNKRIL FNLLPAHVAQ
860 870 880 890 900
HFLMSNPRNM DLYYQSYSQV GVMFASIPNF NDFYIELDGN NMGVECLRLL
910 920 930 940 950
NEIIADFDEL MDKDFYKDLE KIKTIGSTYM AAVGLAPTAG TKAKKCISSH
960 970 980 990 1000
LSTLADFAIE MFDVLDEINY QSYNDFVLRV GINVGPVVAG VIGARRPQYD
1010 1020 1030 1040 1050
IWGNTVNVAS RMDSTGVQGR IQVTEEVHRL LRRGSYRFVC RGKVSVKGKG
1060 1070 1080 1090 1100
EMLTYFLEGR TDGNGSQTRS LNSERKMYPF GRAGLQTRLA AGHPPVPPAA
1110 1120 1130
GLPVGAGPGA LQGSGLAPGP PGQHLPPGAS GKEA
Length:1,134
Mass (Da):123,979
Last modified:February 1, 1991 - v1
Checksum:iCC4A10BCE224DFF3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25579 mRNA Translation: AAA79957.1
PIRiA41350
RefSeqiNP_776654.1, NM_174229.2
UniGeneiBt.517

Genome annotation databases

GeneIDi281601
KEGGibta:281601

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M25579 mRNA Translation: AAA79957.1
PIRiA41350
RefSeqiNP_776654.1, NM_174229.2
UniGeneiBt.517

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AWKmodel-A295-1058[»]
ProteinModelPortaliP19754
SMRiP19754
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000012528

Chemistry databases

BindingDBiP19754
ChEMBLiCHEMBL3549

PTM databases

iPTMnetiP19754

Proteomic databases

PaxDbiP19754
PRIDEiP19754

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281601
KEGGibta:281601

Organism-specific databases

CTDi107

Phylogenomic databases

eggNOGiKOG3619 Eukaryota
COG2114 LUCA
HOGENOMiHOG000006941
HOVERGENiHBG050458
InParanoidiP19754
KOiK08041

Enzyme and pathway databases

BRENDAi4.6.1.1 908

Miscellaneous databases

PROiPR:P19754

Family and domain databases

Gene3Di3.30.70.1230, 2 hits
InterProiView protein in InterPro
IPR001054 A/G_cyclase
IPR018297 A/G_cyclase_CS
IPR032628 AC_N
IPR030672 Adcy
IPR029787 Nucleotide_cyclase
PfamiView protein in Pfam
PF16214 AC_N, 1 hit
PF00211 Guanylate_cyc, 2 hits
PIRSFiPIRSF039050 Ade_cyc, 1 hit
SMARTiView protein in SMART
SM00044 CYCc, 2 hits
SUPFAMiSSF55073 SSF55073, 2 hits
PROSITEiView protein in PROSITE
PS00452 GUANYLATE_CYCLASE_1, 2 hits
PS50125 GUANYLATE_CYCLASE_2, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiADCY1_BOVIN
AccessioniPrimary (citable) accession number: P19754
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 7, 2018
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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