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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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi294 – 2941Magnesium 1 By similarity
Metal bindingi294 – 2941Magnesium 2 By similarity
Metal bindingi295 – 2951Magnesium 2; via carbonyl oxygen By similarity
Metal bindingi338 – 3381Magnesium 1 By similarity
Metal bindingi338 – 3381Magnesium 2 By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. G-protein beta/gamma-subunit complex binding Source: RGD
  3. adenylate cyclase activity Source: BHF-UCL
  4. adenylate cyclase binding Source: BHF-UCL
  5. calcium- and calmodulin-responsive adenylate cyclase activity Source: RGD
  6. metal ion binding Source: UniProtKB-KW
  7. protein binding Source: IntAct
  8. 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4444Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei45 – 6521Helical; Reviewed prediction
Add
BLAST
Transmembranei75 – 9521Helical; Reviewed prediction
Add
BLAST
Transmembranei107 – 12721Helical; Reviewed prediction
Add
BLAST
Transmembranei132 – 15221Helical; Reviewed prediction
Add
BLAST
Transmembranei157 – 17721Helical; Reviewed prediction
Add
BLAST
Transmembranei186 – 20621Helical; Reviewed prediction
Add
BLAST
Topological domaini207 – 600394Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei601 – 62121Helical; Reviewed prediction
Add
BLAST
Transmembranei626 – 64621Helical; Reviewed prediction
Add
BLAST
Transmembranei679 – 69921Helical; Reviewed prediction
Add
BLAST
Transmembranei734 – 75421Helical; Reviewed prediction
Add
BLAST
Transmembranei763 – 78321Helical; Reviewed prediction
Add
BLAST
Transmembranei800 – 82021Helical; Reviewed prediction
Add
BLAST
Topological domaini821 – 1090270Cytoplasmic Reviewed prediction
Add
BLAST

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 2
PRO_0000195686Add
BLAST

Amino acid modifications

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

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

ArrayExpressiP26769.
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

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.

Miscellaneous databases

EvolutionaryTraceiP26769.

Family & Domainsi

Sequence similaritiesi

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.
[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

MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL     50
LIVMGACLAL LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV 100
FKKLLRVFSL VIWICLVAMG YLFMCFGGTV SAWDQVSFFL FIIFVVYTML 150
PFNMRDAIIA SILTSSSHTI VLSVYLSATP GAKEHLFWQI LANVIIFICG 200
NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE RLLLSLLPAH 250
IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR 300
LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL 350
PNHAKNCVKM GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW 400
QYDVWSHDVT LANHMEAGGV PGRVHISSVT LEHLNGAYKV EEGDGEIRDP 450
YLKQHLVKTY FVINPKGERR SPQHLFRPRH TLDGAKMRAS VRMTRYLESW 500
GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR TKSQKKRFEE 550
ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK 600
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL 650
LQCSKKASTS LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL 700
SNSEETTLPT ANTSNANVSV PDNQASILHA RNLFFLPYFI YSCILGLISC 750
SVFLRVNYEL KMLIMMVALV GYNTILLHTH AHVLDAYSQV LFQRPGIWKD 800
LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE REEIETMENL 850
NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT 900
ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL 950
SAIPSQEHAQ EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI 1000
NHGPVIAGVI GAQKPQYDIW GNTVNVASRM DSTGVLDKIQ VTEETSLILQ 1050
TLGYTCTCRG IINVKGKGDL KTYFVNTEMS RSLSQSNLAS 1090
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 CHEMBL2958.

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

ArrayExpressi P26769.
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.
[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: June 11, 2014
This is version 129 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

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