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Protein

Adenylate cyclase type 3

Gene

Adcy3

Organism
Rattus norvegicus (Rat)
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:2255909, PubMed:1633161, PubMed:24363043). Participates in signaling cascades triggered by odorant receptors via its function in cAMP biosynthesis (PubMed:2255909). Required for the perception of odorants. Required for normal sperm motility and normal male fertility. Plays a role in regulating insulin levels and body fat accumulation in response to a high fat diet (By similarity).By similarity3 Publications

Catalytic activityi

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

Cofactori

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

Enzyme regulationi

Activated by forskolin (PubMed:2255909, PubMed:1633161, PubMed:24363043). After forskolin treatment, activity is further increased by calcium/calmodulin (PubMed:1633161). In the absence of forskolin, calcium/calmodulin has little effect on enzyme activity (PubMed:1633161).3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi324Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi324Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi325Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi368Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi368Magnesium 2; catalyticPROSITE-ProRule annotation1
Binding sitei412ATPBy similarity1
Binding sitei975ATPBy similarity1
Binding sitei1109ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi324 – 329ATPBy similarity6
Nucleotide bindingi366 – 368ATPBy similarity3
Nucleotide bindingi1062 – 1064ATPBy similarity3
Nucleotide bindingi1069 – 1073ATPBy similarity5

GO - Molecular functioni

GO - Biological processi

  • acrosome reaction Source: UniProtKB
  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • cAMP biosynthetic process Source: UniProtKB
  • cellular response to forskolin Source: UniProtKB
  • cGMP biosynthetic process Source: GO_Central
  • female meiotic nuclear division Source: RGD
  • flagellated sperm motility Source: UniProtKB
  • intracellular signal transduction Source: RGD
  • olfactory learning Source: UniProtKB
  • sensory perception of smell Source: RGD
  • single fertilization Source: UniProtKB

Keywordsi

Molecular functionCalmodulin-binding, Lyase
Biological processcAMP biosynthesis, Olfaction, Sensory transduction
LigandATP-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 3 (EC:4.6.1.13 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 3
Adenylate cyclase type III1 Publication
Short name:
AC-III
Adenylate cyclase, olfactive type
Adenylyl cyclase 3
Short name:
AC3
Gene namesi
Name:Adcy3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71009 Adcy3

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 – 79CytoplasmicSequence analysisAdd BLAST79
Transmembranei80 – 100HelicalSequence analysisAdd BLAST21
Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Transmembranei139 – 159HelicalSequence analysisAdd BLAST21
Transmembranei173 – 193HelicalSequence analysisAdd BLAST21
Transmembranei226 – 246HelicalSequence analysisAdd BLAST21
Transmembranei381 – 401HelicalSequence analysisAdd BLAST21
Topological domaini402 – 630CytoplasmicSequence analysisAdd BLAST229
Transmembranei631 – 651HelicalSequence analysisAdd BLAST21
Transmembranei662 – 682HelicalSequence analysisAdd BLAST21
Transmembranei706 – 726HelicalSequence analysisAdd BLAST21
Transmembranei755 – 775HelicalSequence analysisAdd BLAST21
Transmembranei777 – 797HelicalSequence analysisAdd BLAST21
Transmembranei833 – 853HelicalSequence analysisAdd BLAST21
Topological domaini854 – 1144CytoplasmicSequence analysisAdd BLAST291

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi465K → R: Abolishes sumoylation. Abolishes location at cilia in the olfactory epithelium. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2095179

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001956891 – 1144Adenylate cyclase type 3Add BLAST1144

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)1 Publication
Modified residuei523PhosphoserineBy similarity1
Modified residuei578PhosphoserineBy similarity1
Glycosylationi734N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1076Phosphoserine; by CaMK2By similarity1

Post-translational modificationi

N-glycosylated.1 Publication
Sumoylated. Sumoylation is required for targeting ot olfactory cilia.1 Publication
Rapidly phosphorylated after stimulation by odorants or forskolin. Phosphorylation by CaMK2 at Ser-1076 down-regulates enzyme activity.By similarity

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP21932
PRIDEiP21932

PTM databases

PhosphoSitePlusiP21932

Expressioni

Tissue specificityi

Detected on cilia on the olfactory epithelium (at protein level) (PubMed:2255909, PubMed:25908845). Detected on cilia on the olfactory epithelium.1 Publication

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi249093, 1 interactor
STRINGi10116.ENSRNOP00000005389

Chemistry databases

BindingDBiP21932

Structurei

3D structure databases

ProteinModelPortaliP21932
SMRiP21932
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 modules have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two modules.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
InParanoidiP21932
KOiK08043
PhylomeDBiP21932

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.

P21932-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEDQGFSDP EYSAEYSAEY SVSLPSDPDR GVGRTHEISV RNSGSCLCLP
60 70 80 90 100
RFMRLTFVPE SLENLYQTYF KRQRHETLLV LVVFAALFDC YVVVMCAVVF
110 120 130 140 150
SSDKLAPLMV AGVGLVLDII LFVLCKKGLL PDRVSRKVVP YLLWLLITAQ
160 170 180 190 200
IFSYLGLNFS RAHAASDTVG WQAFFVFSFF ITLPLSLSPI VIISVVSCVV
210 220 230 240 250
HTLVLGVTVA QQQQDELEGM QLLREILANV FLYLCAIIVG IMSYYMADRK
260 270 280 290 300
HRKAFLEARQ SLEVKMNLEE QSQQQENLML SILPKHVADE MLKDMKKDES
310 320 330 340 350
QKDQQQFNTM YMYRHENVSI LFADIVGFTQ LSSACSAQEL VKLLNELFAR
360 370 380 390 400
FDKLAAKYHQ LRIKILGDCY YCICGLPDYR EDHAVCSILM GLAMVEAISY
410 420 430 440 450
VREKTKTGVD MRVGVHTGTV LGGVLGQKRW QYDVWSTDVT VANKMEAGGI
460 470 480 490 500
PGRVHISQST MDCLKGEFDV EPGDGGSRCD YLDEKGIETY LIIASKPEVK
510 520 530 540 550
KTAQNGLNGS ALPNGAPASK PSSPALIETK EPNGSAHASG STSEEAEEQE
560 570 580 590 600
AQADNPSFPN PRRRLRLQDL ADRVVDASED EHELNQLLNE ALLERESAQV
610 620 630 640 650
VKKRNTFLLT MRFMDPEMET RYSVEKEKQS GAAFSCSCVV LFCTAMVEIL
660 670 680 690 700
IDPWLMTNYV TFVVGEVLLL ILTICSMAAI FPRAFPKKLV AFSSWIDRTR
710 720 730 740 750
WARNTWAMLA IFILVMANVV DMLSCLQYYM GPYNVTTGIE LDGGCMENPK
760 770 780 790 800
YYNYVAVLSL IATIMLVQVS HMVKLTLMLL VTGAVTAINL YAWCPVFDEY
810 820 830 840 850
DHKRFQEKDS PMVALEKMQV LSTPGLNGTD SRLPLVPSKY SMTVMMFVMM
860 870 880 890 900
LSFYYFSRHV EKLARTLFLW KIEVHDQKER VYEMRRWNEA LVTNMLPEHV
910 920 930 940 950
ARHFLGSKKR DEELYSQSYD EIGVMFASLP NFADFYTEES INNGGIECLR
960 970 980 990 1000
FLNEIISDFD SLLDNPKFRV ITKIKTIGST YMAASGVTPD VNTNGFTSSS
1010 1020 1030 1040 1050
KEEKSDKERW QHLADLADFA LAMKDTLTNI NNQSFNNFML RIGMNKGGVL
1060 1070 1080 1090 1100
AGVIGARKPH YDIWGNTVNV ASRMESTGVM GNIQVVEETQ VILREYGFRF
1110 1120 1130 1140
VRRGPIFVKG KGELLTFFLK GRDRPAAFPN GSSVTLPHQV VDNP
Length:1,144
Mass (Da):128,936
Last modified:May 1, 1991 - v1
Checksum:i21098D028DDBAB55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55075 mRNA Translation: AAA40677.1
PIRiA39833
RefSeqiNP_570135.2, NM_130779.2
UniGeneiRn.87800

Genome annotation databases

GeneIDi64508
KEGGirno:64508

Similar proteinsi

Entry informationi

Entry nameiADCY3_RAT
AccessioniPrimary (citable) accession number: P21932
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: May 23, 2018
This is version 141 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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