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Protein

Adenylate cyclase type 8

Gene

Adcy8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is a membrane-bound, calcium-stimulable adenylyl cyclase. May be involved in learning, in memory and in drug dependence.1 Publication

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.1 Publication

Cofactori

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

Enzyme regulationi

Activated by calcium/calmodulin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi416 – 4161Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi416 – 4161Magnesium 2; catalyticPROSITE-ProRule annotation
Metal bindingi417 – 4171Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation
Metal bindingi460 – 4601Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi460 – 4601Magnesium 2; catalyticPROSITE-ProRule annotation
Binding sitei504 – 5041ATPBy similarity
Binding sitei1031 – 10311ATPBy similarity
Binding sitei1153 – 11531ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi416 – 4216ATPBy similarity
Nucleotide bindingi458 – 4603ATPBy similarity
Nucleotide bindingi1106 – 11083ATPBy similarity
Nucleotide bindingi1113 – 11175ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium- and calmodulin-responsive adenylate cyclase activity Source: RGD
  • calmodulin binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • protein C-terminus binding Source: RGD
  • protein N-terminus binding Source: RGD

GO - Biological processi

  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: WormBase
  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: GO_Central
  • cAMP biosynthetic process Source: RGD
  • cAMP-mediated signaling Source: RGD
  • cellular response to calcium ion Source: RGD
  • response to organic cyclic compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cAMP biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi4.6.1.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 8 (EC:4.6.1.11 Publication)
Alternative name(s):
ATP pyrophosphate-lyase 8
Adenylate cyclase type VIIICurated
Adenylyl cyclase 8
Ca(2+)/calmodulin-activated adenylyl cyclase
Gene namesi
Name:Adcy8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2036. Adcy8.

Subcellular locationi

  • Membrane 1 Publication; Multi-pass membrane protein Curated

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 179179CytoplasmicSequence analysisAdd
BLAST
Transmembranei180 – 20021HelicalSequence analysisAdd
BLAST
Transmembranei209 – 22921HelicalSequence analysisAdd
BLAST
Transmembranei244 – 26421HelicalSequence analysisAdd
BLAST
Transmembranei271 – 29121HelicalSequence analysisAdd
BLAST
Transmembranei293 – 31321HelicalSequence analysisAdd
BLAST
Transmembranei318 – 33821HelicalSequence analysisAdd
BLAST
Topological domaini339 – 712374CytoplasmicSequence analysisAdd
BLAST
Transmembranei713 – 73321HelicalSequence analysisAdd
BLAST
Transmembranei735 – 75521HelicalSequence analysisAdd
BLAST
Transmembranei784 – 80421HelicalSequence analysisAdd
BLAST
Transmembranei828 – 84821HelicalSequence analysisAdd
BLAST
Transmembranei858 – 87821HelicalSequence analysisAdd
BLAST
Transmembranei891 – 91121HelicalSequence analysisAdd
BLAST
Topological domaini912 – 1248337CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • membrane Source: RGD
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2095179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12481248Adenylate cyclase type 8PRO_0000195707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei611 – 6111PhosphoserineBy similarity
Modified residuei621 – 6211PhosphoserineCombined sources
Glycosylationi814 – 8141N-linked (GlcNAc...)Sequence analysis
Glycosylationi818 – 8181N-linked (GlcNAc...)Sequence analysis
Glycosylationi885 – 8851N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP40146.
PRIDEiP40146.

PTM databases

iPTMnetiP40146.
PhosphoSiteiP40146.

Expressioni

Tissue specificityi

Brain.1 Publication

Interactioni

GO - Molecular functioni

  • calmodulin binding Source: RGD
  • protein C-terminus binding Source: RGD
  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000006789.

Structurei

3D structure databases

ProteinModelPortaliP40146.
SMRiP40146. Positions 399-584, 968-1142.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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
Contains 2 guanylate cyclase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP40146.
KOiK08048.
PhylomeDBiP40146.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40146-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSDVHCLS GSEELYTIHP TPPAADGGSG SRPQRLLWQT AVRHITEQRF
60 70 80 90 100
IHGHRGGGGG GSRKASNPAG SGPNHHAPQL SSDSVLPLYS LGSGERAHNT
110 120 130 140 150
GGTKVFPERS GSGSASGSGG GGDLGFLHLD CAPSNSDFFL NGGYSYRGVI
160 170 180 190 200
FPTLRNSFKS RDLERLYQRY FLGQRRKSEV VMNVLDVLTK LTLLVLHLSL
210 220 230 240 250
ASAPMDPLKG ILLGFFTGIE VVICALVVVR KDTTSHTYLQ YSGVVTWVAM
260 270 280 290 300
TTQILAAGLG YGLLGDGIGY VLFTLFATYS MLPLPLTWAI LAGLGTSLLQ
310 320 330 340 350
VTLQVLIPRL AVFSINQVLA QVVLFMCMNT AGIFISYLSD RAQRQAFLET
360 370 380 390 400
RRCVEARLRL ETENQRQERL VLSVLPRFVV LEMINDMTNV EDEHLQHQFH
410 420 430 440 450
RIYIHRYENV SILFADVKGF TNLSTTLSAQ ELVRMLNELF ARFDRLAHEH
460 470 480 490 500
HCLRIKILGD CYYCVSGLPE PRQDHAHCCV EMGLSMIKTI RFVRSRTKHD
510 520 530 540 550
VDMRIGIHSG SVLCGVLGLR KWQFDVWSWD VDIANKLESG GIPGRIHISK
560 570 580 590 600
ATLDCLSGDY NVEEGHGKER NEFLRKHNIE TYLIKQPEES LLSLPEDIVK
610 620 630 640 650
ESVSCSDRRN SGATFTEGSW SPELPFDNIV GKQNTLAALT RNSINLLPNH
660 670 680 690 700
LAQALHVQSG PEEINKRIEH TIDLRSGDKL RREHIKPFSL MFKDSSLEHK
710 720 730 740 750
YSQMRDEVFK SNLVCAFIVL LFITAIQSLL PSSRLMPMTI QFSILIMLHS
760 770 780 790 800
ALVLITTAED YKCLPLILRK TCCWINETYL ARNVIIFASI LINFLGAVIN
810 820 830 840 850
ILWCDFDKSI PLKNLTFNSS AVFTDICSYP EYFVFTGVLA MVTCAVFLRL
860 870 880 890 900
NSVLKLAVLL IMIAIYALLT ETIYAGLFLS YDNLNHSGED FLGTKEASLL
910 920 930 940 950
LMAMFLLAVF YHGQQLEYTA RLDFLWRVQA KEEINEMKDL REHNENMLRN
960 970 980 990 1000
ILPGHVARHF LEKDRDNEEL YSQSYDAVGV MFASIPGFAD FYSQTEMNNQ
1010 1020 1030 1040 1050
GVECLRLLNE IIADFDELLG EDRFQDIEKI KTIGSTYMAV SGLSPEKQQC
1060 1070 1080 1090 1100
EDKWGHLCAL ADFSLALTES IQEINKHSFN NFELRIGISH GSVVAGVIGA
1110 1120 1130 1140 1150
KKPQYDIWGK TVNLASRMDS TGVSGRIQVP EETYLILKDQ GFAFDYRGEI
1160 1170 1180 1190 1200
YVKGISEQEG KIKTYFLLGR VQPNPFILPP RRLPGQYSLA AVVLGLVQSL
1210 1220 1230 1240
NRQRQKQLLN ENSNSGIIKS HYNRRTLLTP SGPEPGAQAE GTDKSDLP
Length:1,248
Mass (Da):139,823
Last modified:February 1, 1995 - v1
Checksum:i0171A3CEED034961
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26986 mRNA. Translation: AAA20504.1.
PIRiA53588.
RefSeqiNP_058838.1. NM_017142.1.
UniGeneiRn.10382.

Genome annotation databases

GeneIDi29241.
KEGGirno:29241.
UCSCiRGD:2036. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26986 mRNA. Translation: AAA20504.1.
PIRiA53588.
RefSeqiNP_058838.1. NM_017142.1.
UniGeneiRn.10382.

3D structure databases

ProteinModelPortaliP40146.
SMRiP40146. Positions 399-584, 968-1142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000006789.

Chemistry

ChEMBLiCHEMBL2095179.

PTM databases

iPTMnetiP40146.
PhosphoSiteiP40146.

Proteomic databases

PaxDbiP40146.
PRIDEiP40146.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29241.
KEGGirno:29241.
UCSCiRGD:2036. rat.

Organism-specific databases

CTDi114.
RGDi2036. Adcy8.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP40146.
KOiK08048.
PhylomeDBiP40146.

Enzyme and pathway databases

BRENDAi4.6.1.1. 5301.

Miscellaneous databases

PROiP40146.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADCY8_RAT
AccessioniPrimary (citable) accession number: P40146
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.