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P26769

- ADCY2_RAT

UniProt

P26769 - ADCY2_RAT

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Protein

Adenylate cyclase type 2

Gene

Adcy2

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

Functioni

This is a membrane-bound, calmodulin-insensitive adenylyl cyclase.

Catalytic activityi

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

Cofactori

Binds 2 magnesium ions per subunit.By similarity

Enzyme regulationi

Insensitive to calcium/calmodulin. Stimulated by the G protein beta and gamma subunit complex. Phosphorylation by RAF1 results in its activation (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi294 – 2941Magnesium 1PROSITE-ProRule annotation
Metal bindingi294 – 2941Magnesium 2PROSITE-ProRule annotation
Metal bindingi295 – 2951Magnesium 2; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi338 – 3381Magnesium 1PROSITE-ProRule annotation
Metal bindingi338 – 3381Magnesium 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. adenylate cyclase activity Source: BHF-UCL
  2. adenylate cyclase binding Source: BHF-UCL
  3. ATP binding Source: UniProtKB-KW
  4. calcium- and calmodulin-responsive adenylate cyclase activity Source: RGD
  5. G-protein beta/gamma-subunit complex binding Source: RGD
  6. metal ion binding Source: UniProtKB-KW
  7. protein heterodimerization activity Source: BHF-UCL

GO - Biological processi

  1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: BHF-UCL
  2. cAMP biosynthetic process Source: BHF-UCL
  3. intracellular signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cAMP biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi4.6.1.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 2 (EC:4.6.1.1)
Alternative name(s):
ATP pyrophosphate-lyase 2
Adenylate cyclase type II
Adenylyl cyclase 2
Gene namesi
Name:Adcy2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi619965. Adcy2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
  2. dendrite Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. intracellular Source: BHF-UCL
  5. membrane Source: UniProtKB
  6. membrane raft Source: BHF-UCL
  7. plasma membrane Source: BHF-UCL
  8. protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10901090Adenylate cyclase type 2PRO_0000195686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi712 – 7121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi717 – 7171N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Phosphorylated by RAF1.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP26769.
PRIDEiP26769.

PTM databases

PhosphoSiteiP26769.

Expressioni

Tissue specificityi

Expressed in brain and, at lower levels, in olfactory epithelium and lung.

Gene expression databases

ExpressionAtlasiP26769. baseline.
GenevestigatoriP26769.

Interactioni

Subunit structurei

Interacts with RAF1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PDE4DQ08499-23EBI-1027877,EBI-8095525From a different organism.

Protein-protein interaction databases

BioGridi249536. 1 interaction.
DIPiDIP-164N.
IntActiP26769. 7 interactions.
MINTiMINT-8041796.
STRINGi10116.ENSRNOP00000038994.

Structurei

Secondary structure

1
1090
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi879 – 89113
Helixi895 – 8984
Turni903 – 9086
Helixi909 – 92315
Helixi924 – 9274
Helixi929 – 9313
Beta strandi934 – 9407
Beta strandi943 – 9486
Helixi967 – 98721
Turni988 – 9914
Beta strandi997 – 101014
Beta strandi1012 – 10143
Beta strandi1016 – 10216
Helixi1022 – 103211
Beta strandi1039 – 10413
Helixi1043 – 105210
Beta strandi1056 – 10649
Turni1065 – 10673
Beta strandi1068 – 10758

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AB8X-ray2.20A/B871-1090[»]
1AZSX-ray2.30B870-1081[»]
1CJKX-ray3.00B870-1081[»]
1CJTX-ray2.80B870-1081[»]
1CJUX-ray2.80B870-1081[»]
1CJVX-ray3.00B870-1081[»]
1CS4X-ray2.50B870-1081[»]
1CULX-ray2.40B874-1081[»]
1TL7X-ray2.80B870-1081[»]
1U0HX-ray2.90B870-1081[»]
2GVDX-ray2.90B870-1081[»]
2GVZX-ray3.27B870-1081[»]
3C14X-ray2.68B870-1081[»]
3C15X-ray2.78B870-1081[»]
3C16X-ray2.87B870-1081[»]
3G82X-ray3.11B870-1081[»]
3MAAX-ray3.00B870-1081[»]
ProteinModelPortaliP26769.
SMRiP26769. Positions 277-463, 878-1077.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26769.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4444CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini207 – 600394CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini821 – 1090270CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei45 – 6521HelicalSequence AnalysisAdd
BLAST
Transmembranei75 – 9521HelicalSequence AnalysisAdd
BLAST
Transmembranei107 – 12721HelicalSequence AnalysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence AnalysisAdd
BLAST
Transmembranei157 – 17721HelicalSequence AnalysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence AnalysisAdd
BLAST
Transmembranei601 – 62121HelicalSequence AnalysisAdd
BLAST
Transmembranei626 – 64621HelicalSequence AnalysisAdd
BLAST
Transmembranei679 – 69921HelicalSequence AnalysisAdd
BLAST
Transmembranei734 – 75421HelicalSequence AnalysisAdd
BLAST
Transmembranei763 – 78321HelicalSequence AnalysisAdd
BLAST
Transmembranei800 – 82021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

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

eggNOGiCOG2114.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP26769.
KOiK08042.
PhylomeDBiP26769.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Adenylate_cyclase-like.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF06327. DUF1053. 1 hit.
PF00211. 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.

P26769-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL
60 70 80 90 100
LIVMGACLAL LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV
110 120 130 140 150
FKKLLRVFSL VIWICLVAMG YLFMCFGGTV SAWDQVSFFL FIIFVVYTML
160 170 180 190 200
PFNMRDAIIA SILTSSSHTI VLSVYLSATP GAKEHLFWQI LANVIIFICG
210 220 230 240 250
NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE RLLLSLLPAH
260 270 280 290 300
IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR
310 320 330 340 350
LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL
360 370 380 390 400
PNHAKNCVKM GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW
410 420 430 440 450
QYDVWSHDVT LANHMEAGGV PGRVHISSVT LEHLNGAYKV EEGDGEIRDP
460 470 480 490 500
YLKQHLVKTY FVINPKGERR SPQHLFRPRH TLDGAKMRAS VRMTRYLESW
510 520 530 540 550
GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR TKSQKKRFEE
560 570 580 590 600
ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK
610 620 630 640 650
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL
660 670 680 690 700
LQCSKKASTS LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL
710 720 730 740 750
SNSEETTLPT ANTSNANVSV PDNQASILHA RNLFFLPYFI YSCILGLISC
760 770 780 790 800
SVFLRVNYEL KMLIMMVALV GYNTILLHTH AHVLDAYSQV LFQRPGIWKD
810 820 830 840 850
LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE REEIETMENL
860 870 880 890 900
NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT
910 920 930 940 950
ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL
960 970 980 990 1000
SAIPSQEHAQ EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI
1010 1020 1030 1040 1050
NHGPVIAGVI GAQKPQYDIW GNTVNVASRM DSTGVLDKIQ VTEETSLILQ
1060 1070 1080 1090
TLGYTCTCRG IINVKGKGDL KTYFVNTEMS RSLSQSNLAS
Length:1,090
Mass (Da):123,316
Last modified:August 1, 1992 - v1
Checksum:i935CE44DF73199B3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M80550 mRNA. Translation: AAA40682.1.
PIRiA41541.
RefSeqiNP_112269.1. NM_031007.1.
UniGeneiRn.10731.

Genome annotation databases

GeneIDi81636.
KEGGirno:81636.
UCSCiRGD:619965. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M80550 mRNA. Translation: AAA40682.1 .
PIRi A41541.
RefSeqi NP_112269.1. NM_031007.1.
UniGenei Rn.10731.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AB8 X-ray 2.20 A/B 871-1090 [» ]
1AZS X-ray 2.30 B 870-1081 [» ]
1CJK X-ray 3.00 B 870-1081 [» ]
1CJT X-ray 2.80 B 870-1081 [» ]
1CJU X-ray 2.80 B 870-1081 [» ]
1CJV X-ray 3.00 B 870-1081 [» ]
1CS4 X-ray 2.50 B 870-1081 [» ]
1CUL X-ray 2.40 B 874-1081 [» ]
1TL7 X-ray 2.80 B 870-1081 [» ]
1U0H X-ray 2.90 B 870-1081 [» ]
2GVD X-ray 2.90 B 870-1081 [» ]
2GVZ X-ray 3.27 B 870-1081 [» ]
3C14 X-ray 2.68 B 870-1081 [» ]
3C15 X-ray 2.78 B 870-1081 [» ]
3C16 X-ray 2.87 B 870-1081 [» ]
3G82 X-ray 3.11 B 870-1081 [» ]
3MAA X-ray 3.00 B 870-1081 [» ]
ProteinModelPortali P26769.
SMRi P26769. Positions 277-463, 878-1077.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249536. 1 interaction.
DIPi DIP-164N.
IntActi P26769. 7 interactions.
MINTi MINT-8041796.
STRINGi 10116.ENSRNOP00000038994.

Chemistry

BindingDBi P26769.
ChEMBLi CHEMBL2095179.

PTM databases

PhosphoSitei P26769.

Proteomic databases

PaxDbi P26769.
PRIDEi P26769.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 81636.
KEGGi rno:81636.
UCSCi RGD:619965. rat.

Organism-specific databases

CTDi 108.
RGDi 619965. Adcy2.

Phylogenomic databases

eggNOGi COG2114.
HOGENOMi HOG000006941.
HOVERGENi HBG050458.
InParanoidi P26769.
KOi K08042.
PhylomeDBi P26769.

Enzyme and pathway databases

BRENDAi 4.6.1.1. 5301.

Miscellaneous databases

EvolutionaryTracei P26769.
NextBioi 615124.

Gene expression databases

ExpressionAtlasi P26769. baseline.
Genevestigatori P26769.

Family and domain databases

Gene3Di 3.30.70.1230. 2 hits.
InterProi IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Adenylate_cyclase-like.
IPR029787. Nucleotide_cyclase.
[Graphical view ]
Pfami PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view ]
SMARTi SM00044. CYCc. 2 hits.
[Graphical view ]
SUPFAMi SSF55073. SSF55073. 2 hits.
PROSITEi PS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and characterization of a Ca2+/calmodulin-insensitive adenylyl cyclase from rat brain."
    Feinstein P.G., Schrader K.A., Bakalyar H.A., Tang W.J., Krupinski J., Gilman A.G., Reed R.R.
    Proc. Natl. Acad. Sci. U.S.A. 88:10173-10177(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Structure of the adenylyl cyclase catalytic core."
    Zhang G., Liu Y., Ruoho A.E., Hurley J.H.
    Nature 386:247-253(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 871-1090.
  3. Erratum
    Zhang G., Liu Y., Ruoho A.E., Hurley J.H.
    Nature 388:204-204(1997)
  4. "Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS."
    Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.
    Science 278:1907-1916(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 870-1081 OF COMPLEX WITH G(S)-ALPHA.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF COMPLEX WITH G(S)-ALPHA.

Entry informationi

Entry nameiADCY2_RAT
AccessioniPrimary (citable) accession number: P26769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 131 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3