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Protein

Adenylate cyclase type 1

Gene

ADCY1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme 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

GO - Biological processi

  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • cAMP biosynthetic process Source: UniProtKB
  • cAMP-mediated signaling Source: UniProtKB
  • cellular response to calcium ion Source: UniProtKB
  • cellular response to forskolin Source: UniProtKB
  • cGMP biosynthetic process Source: GO_Central
  • regulation of circadian rhythm Source: UniProtKB
  • rhythmic process Source: UniProtKB-KW

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

  • Membrane 2 Publications; Multi-pass membrane protein 2 Publications
  • Cell membrane 2 Publications; Multi-pass membrane protein 1 Publication
  • Cytoplasm By similarity
  • Membrane raft 1 Publication

  • 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.By similarity

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

GO - Cellular componenti

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

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

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: May 10, 2017
This is version 135 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.