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Protein

Adenylate cyclase type 9

Gene

Adcy9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adenylyl cyclase that catalyzes the formation of the signaling molecule cAMP in response to activation of G protein-coupled receptors. Contributes to signaling cascades activated by CRH (corticotropin-releasing factor), corticosteroids and by beta-adrenergic receptors.By similarity1 Publication

Catalytic activityi

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

Cofactori

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

Enzyme regulationi

Insensitive to calcium/calmodulin, forskolin and somatostatin. Stimulated by beta-adrenergic receptor activation. Activity is down-regulated by calcium/calcineurin.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi399Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi399Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi400Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi443Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi443Magnesium 2; catalyticPROSITE-ProRule annotation1
Binding sitei487ATPBy similarity1
Binding sitei1108ATPBy similarity1
Binding sitei1232ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi399 – 404ATPBy similarity6
Nucleotide bindingi441 – 443ATPBy similarity3
Nucleotide bindingi1185 – 1187ATPBy similarity3
Nucleotide bindingi1192 – 1196ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

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. 3474.
ReactomeiR-MMU-163359. Glucagon signaling in metabolic regulation.
R-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-170660. Adenylate cyclase activating pathway.
R-MMU-170670. Adenylate cyclase inhibitory pathway.
R-MMU-418555. G alpha (s) signalling events.
R-MMU-418597. G alpha (z) signalling events.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-5610787. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 9 (EC:4.6.1.11 Publication)
Alternative name(s):
ATP pyrophosphate-lyase 9
Adenylate cyclase type IX
Adenylyl cyclase 9
Short name:
AC91 Publication
Adenylyl cyclase type 10
Short name:
ACTP10
Gene namesi
Name:Adcy9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:108450. Adcy9.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 117CytoplasmicSequence analysisAdd BLAST117
Transmembranei118 – 138HelicalSequence analysisAdd BLAST21
Topological domaini139 – 141ExtracellularSequence analysis3
Transmembranei142 – 162HelicalSequence analysisAdd BLAST21
Topological domaini163 – 171CytoplasmicSequence analysis9
Transmembranei172 – 192HelicalSequence analysisAdd BLAST21
Topological domaini193 – 215ExtracellularSequence analysisAdd BLAST23
Transmembranei216 – 235HelicalSequence analysisAdd BLAST20
Topological domaini236 – 241CytoplasmicSequence analysis6
Transmembranei242 – 259HelicalSequence analysisAdd BLAST18
Topological domaini260 – 280ExtracellularSequence analysisAdd BLAST21
Transmembranei281 – 301HelicalSequence analysisAdd BLAST21
Topological domaini302 – 786CytoplasmicSequence analysisAdd BLAST485
Transmembranei787 – 807HelicalSequence analysisAdd BLAST21
Topological domaini808 – 818ExtracellularSequence analysisAdd BLAST11
Transmembranei819 – 839HelicalSequence analysisAdd BLAST21
Topological domaini840 – 867CytoplasmicSequence analysisAdd BLAST28
Transmembranei868 – 888HelicalSequence analysisAdd BLAST21
Topological domaini889 – 891ExtracellularSequence analysis3
Transmembranei892 – 912HelicalSequence analysisAdd BLAST21
Topological domaini913 – 920CytoplasmicSequence analysis8
Transmembranei921 – 941HelicalSequence analysisAdd BLAST21
Topological domaini942 – 975ExtracellularSequence analysisAdd BLAST34
Transmembranei976 – 996HelicalSequence analysisAdd BLAST21
Topological domaini997 – 1353CytoplasmicSequence analysisAdd BLAST357

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001957091 – 1353Adenylate cyclase type 9Add BLAST1353

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi206N-linked (GlcNAc...)Sequence analysis1
Modified residuei610PhosphoserineCombined sources1
Modified residuei613PhosphoserineCombined sources1
Modified residuei688PhosphoserineCombined sources1
Modified residuei691PhosphoserineCombined sources1
Modified residuei706PhosphoserineCombined sources1
Glycosylationi955N-linked (GlcNAc...)Sequence analysis1
Glycosylationi964N-linked (GlcNAc...)Sequence analysis1
Modified residuei1257PhosphoserineBy similarity1
Modified residuei1259PhosphoserineBy similarity1
Modified residuei1295PhosphoserineCombined sources1
Modified residuei1307PhosphoserineBy similarity1
Modified residuei1332PhosphoserineCombined sources1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP51830.
PaxDbiP51830.
PeptideAtlasiP51830.
PRIDEiP51830.

PTM databases

iPTMnetiP51830.
PhosphoSitePlusiP51830.

Expressioni

Tissue specificityi

Detected in brain, spleen, lung, liver and testis (at protein level). Detected in brain, especially in hippocampus, cerebellum and neocortex. Found in decreasing order in skeletal muscle, heart, adrenal gland, ovary and brain; and to a lesser extent, in kidney, liver, testis, lung, thymus and spleen.1 Publication

Gene expression databases

BgeeiENSMUSG00000005580.
CleanExiMM_ADCY9.
ExpressionAtlasiP51830. baseline and differential.
GenevisibleiP51830. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005719.

Structurei

3D structure databases

ProteinModelPortaliP51830.
SMRiP51830.
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

eggNOGiKOG3618. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000119042.
HOGENOMiHOG000001574.
HOVERGENiHBG050459.
InParanoidiP51830.
KOiK08049.
OMAiWHICLAV.
OrthoDBiEOG091G0285.
PhylomeDBiP51830.
TreeFamiTF313845.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 2 hits.
[Graphical view]
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.

P51830-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSPHQQLL HHHSTEVSCD SSGDSNSVRV KINPKQLSSN THPKHCKYSI
60 70 80 90 100
SSSCSSSGDS GGLPRRVGGG GRLRRQKKLP QLFERASSRW WDPKFDSMNL
110 120 130 140 150
EEACLERCFP QTQRRFRYAL FYVGFACLLW SIYFAVHMKS KVIVMVVPAL
160 170 180 190 200
CFLVVCVGFF LFTFTKLYAR HYAWTSLALT LLVFALTLAA QFQVWTPLSG
210 220 230 240 250
RVDSSNHTLT ATPADTCLSQ VGSFSICIEV LLLLYTVMQL PLYLSLFLGV
260 270 280 290 300
VYSVLFETFG YHFRNEDCYP SPGPGALHWE LLSRALLHVC IHAIGIHLFV
310 320 330 340 350
MSQVRSRSTF LKVGQSIMHG KDLEVEKALK ERMIHSVMPR IIADDLMKQG
360 370 380 390 400
DEESENSVKR HATSSPKNRK KKSSIQKAPI AFRPFKMQQI EEVSILFADI
410 420 430 440 450
VGFTKMSANK SAHALVGLLN DLFGRFDRLC EQTKCEKIST LGDCYYCVAG
460 470 480 490 500
CPEPRADHAY CCIEMGLGMI KAIEQFCQEK KEMVNMRVGV HTGTVLCGIL
510 520 530 540 550
GMRRFKFDVW SNDVNLANLM EQLGVAGKVH ISEATAKYLD DRYEMEDGRV
560 570 580 590 600
IERLGQSVVA DQLKGLKTYL ISGQRAKESH CSCAEALLSG FEVIDDSRES
610 620 630 640 650
SGPRGQGTAS PGSVSDLAQT VKTFDNLKTC PSCGITFAPK SEAGAEGGTV
660 670 680 690 700
QNGCQDEPKT STKASGGPNS KTQNGLLSPP AEEKLTNSQT SLCEILQEKG
710 720 730 740 750
RWAGVSLDQS ALLPLRFKNI REKTDAHFVD VIKEDSLMKD YFFKPPINQF
760 770 780 790 800
SLNFLDQELE RSYRTSYQEE VIKNSPVKTF ASATFSSLLD VFLSTTVFLI
810 820 830 840 850
LSITCFLKYG ATATPPPPAA LAVFGADLLL EVLSLIVSIR MVFFLEDVMT
860 870 880 890 900
CTKWLLEWIA GWLPRHCIGA ILVSLPALAV YSHITSEFET NIHVTMFTGS
910 920 930 940 950
AVLVAVVHYC NFCQLSSWMR SSLATIVGAG LLLLLHISLC QDSSIVMSPL
960 970 980 990 1000
DSAQNFSAQR NPCNSSVLQD GRRPASLIGK ELILTFFLLL LLVWFLNREF
1010 1020 1030 1040 1050
EVSYRLHYHG DVEADLHRTK IQSMRDQADW LLRNIIPYHV AEQLKVSQTY
1060 1070 1080 1090 1100
SKNHDSGGVI FASIVNFSEF YEENYEGGKE CYRVLNELIG DFDELLSKPD
1110 1120 1130 1140 1150
YNSIEKIKTI GATYMAASGL NTAQCQEGGH PQEHLRILFE FAKEMMRVVD
1160 1170 1180 1190 1200
DFNNNMLWFN FKLRVGFNHG PLTAGVIGTT KLLYDIWGDT VNIASRMDTT
1210 1220 1230 1240 1250
GVECRIQVSE ESYRVLSKMG YDFDYRGTVN VKGKGQMKTY LYPKCTDNGV
1260 1270 1280 1290 1300
VPQHQLSISP DIRVQVDGSI GRSPTDEIAN LVPSVQYSDK ASLGSDDSTQ
1310 1320 1330 1340 1350
AKEARLSSKR SWREPVKAEE RFPFGKAIEK DSCEDIGVEE ASELSKLNVS

KSV
Length:1,353
Mass (Da):150,954
Last modified:October 1, 1996 - v1
Checksum:iC65736A8304F689E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti893H → Q in CAA90570 (PubMed:7575502).Curated1
Sequence conflicti1192N → D no nucleotide entry (PubMed:7528319).Curated1
Sequence conflicti1305R → H in CAA90570 (PubMed:7575502).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30602 mRNA. Translation: AAC52603.1.
Z50190 mRNA. Translation: CAA90570.1.
CCDSiCCDS27917.1.
PIRiJC4279.
RefSeqiNP_033754.2. NM_009624.3.
UniGeneiMm.439750.
Mm.482493.

Genome annotation databases

EnsembliENSMUST00000005719; ENSMUSP00000005719; ENSMUSG00000005580.
ENSMUST00000117801; ENSMUSP00000113498; ENSMUSG00000005580.
GeneIDi11515.
KEGGimmu:11515.
UCSCiuc007xzr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30602 mRNA. Translation: AAC52603.1.
Z50190 mRNA. Translation: CAA90570.1.
CCDSiCCDS27917.1.
PIRiJC4279.
RefSeqiNP_033754.2. NM_009624.3.
UniGeneiMm.439750.
Mm.482493.

3D structure databases

ProteinModelPortaliP51830.
SMRiP51830.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000005719.

PTM databases

iPTMnetiP51830.
PhosphoSitePlusiP51830.

Proteomic databases

MaxQBiP51830.
PaxDbiP51830.
PeptideAtlasiP51830.
PRIDEiP51830.

Protocols and materials databases

DNASUi11515.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005719; ENSMUSP00000005719; ENSMUSG00000005580.
ENSMUST00000117801; ENSMUSP00000113498; ENSMUSG00000005580.
GeneIDi11515.
KEGGimmu:11515.
UCSCiuc007xzr.2. mouse.

Organism-specific databases

CTDi115.
MGIiMGI:108450. Adcy9.

Phylogenomic databases

eggNOGiKOG3618. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000119042.
HOGENOMiHOG000001574.
HOVERGENiHBG050459.
InParanoidiP51830.
KOiK08049.
OMAiWHICLAV.
OrthoDBiEOG091G0285.
PhylomeDBiP51830.
TreeFamiTF313845.

Enzyme and pathway databases

BRENDAi4.6.1.1. 3474.
ReactomeiR-MMU-163359. Glucagon signaling in metabolic regulation.
R-MMU-163615. PKA activation.
R-MMU-164378. PKA activation in glucagon signalling.
R-MMU-170660. Adenylate cyclase activating pathway.
R-MMU-170670. Adenylate cyclase inhibitory pathway.
R-MMU-418555. G alpha (s) signalling events.
R-MMU-418597. G alpha (z) signalling events.
R-MMU-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-MMU-5610787. Hedgehog 'off' state.

Miscellaneous databases

PROiP51830.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005580.
CleanExiMM_ADCY9.
ExpressionAtlasiP51830. baseline and differential.
GenevisibleiP51830. MM.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 2 hits.
[Graphical view]
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 nameiADCY9_MOUSE
AccessioniPrimary (citable) accession number: P51830
Secondary accession number(s): Q61279
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 148 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.