Adenylate cyclase type 2 - Rattus norvegicus (Rat)

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P26769 (ADCY2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

Adcy2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1090 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is a membrane-bound, calmodulin-insensitive adenylyl cyclase.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Enzyme regulation	Insensitive to calcium/calmodulin. Stimulated by the G protein beta and gamma subunit complex. Phosphorylation by RAF1 results in its activation By similarity.
Subunit structure	Interacts with RAF1 By similarity.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in brain and, at lower levels, in olfactory epithelium and lung.
Post-translational modification	Phosphorylated by RAF1 By similarity.
Sequence similarities	Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 2 guanylate cyclase domains.

Ontologies

Keywords
Biological process	cAMP biosynthesis
Cellular component	Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-modulating G-protein coupled receptor signaling pathway Inferred from direct assay PubMed 18164588. Source: BHF-UCL intracellular signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara dendrite Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular Inferred from direct assay PubMed 18164588. Source: BHF-UCL membrane raft Inferred from direct assay PubMed 18164588. Source: BHF-UCL plasma membrane Inferred from direct assay PubMed 18164588. Source: BHF-UCL protein complex Inferred from direct assay PubMed 16967511. Source: RGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase binding Inferred from direct assay PubMed 18164588. Source: BHF-UCL calcium- and calmodulin-responsive adenylate cyclase activity Inferred from direct assay PubMed 11350817. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein heterodimerization activity Inferred from direct assay PubMed 18164588. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1090

1090

Adenylate cyclase type 2

PRO_0000195686

Regions

Topological domain

1 – 44

Cytoplasmic Potential

Transmembrane

45 – 65

Helical; Potential

Transmembrane

75 – 95

Helical; Potential

Transmembrane

107 – 127

Helical; Potential

Transmembrane

132 – 152

Helical; Potential

Transmembrane

157 – 177

Helical; Potential

Transmembrane

186 – 206

Helical; Potential

Topological domain

207 – 600

394

Cytoplasmic Potential

Transmembrane

601 – 621

Helical; Potential

Transmembrane

626 – 646

Helical; Potential

Transmembrane

679 – 699

Helical; Potential

Transmembrane

734 – 754

Helical; Potential

Transmembrane

763 – 783

Helical; Potential

Transmembrane

800 – 820

Helical; Potential

Topological domain

821 – 1090

270

Cytoplasmic Potential

Sites

Metal binding

294

Magnesium 1 By similarity

Metal binding

294

Magnesium 2 By similarity

Metal binding

295

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

338

Magnesium 1 By similarity

Metal binding

338

Magnesium 2 By similarity

Amino acid modifications

Glycosylation

712

N-linked (GlcNAc...) Potential

Glycosylation

717

N-linked (GlcNAc...) Potential

Secondary structure

1090

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P26769 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 935CE44DF73199B3
Show »

FASTA

1,090

123,316

        10         20         30         40         50         60 
MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL LIVMGACLAL 

        70         80         90        100        110        120 
LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV FKKLLRVFSL VIWICLVAMG 

       130        140        150        160        170        180 
YLFMCFGGTV SAWDQVSFFL FIIFVVYTML PFNMRDAIIA SILTSSSHTI VLSVYLSATP 

       190        200        210        220        230        240 
GAKEHLFWQI LANVIIFICG NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE 

       250        260        270        280        290        300 
RLLLSLLPAH IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR 

       310        320        330        340        350        360 
LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL PNHAKNCVKM 

       370        380        390        400        410        420 
GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW QYDVWSHDVT LANHMEAGGV 

       430        440        450        460        470        480 
PGRVHISSVT LEHLNGAYKV EEGDGEIRDP YLKQHLVKTY FVINPKGERR SPQHLFRPRH 

       490        500        510        520        530        540 
TLDGAKMRAS VRMTRYLESW GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR 

       550        560        570        580        590        600 
TKSQKKRFEE ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK 

       610        620        630        640        650        660 
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL LQCSKKASTS 

       670        680        690        700        710        720 
LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL SNSEETTLPT ANTSNANVSV 

       730        740        750        760        770        780 
PDNQASILHA RNLFFLPYFI YSCILGLISC SVFLRVNYEL KMLIMMVALV GYNTILLHTH 

       790        800        810        820        830        840 
AHVLDAYSQV LFQRPGIWKD LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE 

       850        860        870        880        890        900 
REEIETMENL NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT 

       910        920        930        940        950        960 
ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL SAIPSQEHAQ 

       970        980        990       1000       1010       1020 
EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI NHGPVIAGVI GAQKPQYDIW 

      1030       1040       1050       1060       1070       1080 
GNTVNVASRM DSTGVLDKIQ VTEETSLILQ TLGYTCTCRG IINVKGKGDL KTYFVNTEMS 

      1090 
RSLSQSNLAS

« Hide

References

[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]	"Two-metal-ion catalysis in adenylyl cyclase." Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R. Science 285:756-760(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF COMPLEX WITH G(S)-ALPHA.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M80550 mRNA. Translation: AAA40682.1.

IPI

IPI00196228.

PIR

A41541.

RefSeq

NP_112269.1. NM_031007.1.

UniGene

Rn.10731.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P26769.

SMR

P26769. Positions 277-463, 878-1077.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-164N.

IntAct

P26769. 2 interactions.

STRING

10116.ENSRNOP00000038994.

PTM databases

PhosphoSite

P26769.

Proteomic databases

PaxDb

P26769.

PRIDE

P26769.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

81636.

KEGG

rno:81636.

UCSC

RGD:619965. rat.

Organism-specific databases

CTD

108.

RGD

619965. Adcy2.

Phylogenomic databases

eggNOG

COG2114.

HOGENOM

HOG000006941.

HOVERGEN

HBG050458.

InParanoid

P26769.

K08042.

OrthoDB

EOG48D0TJ.

Enzyme and pathway databases

BRENDA

4.6.1.1. 5301.

Gene expression databases

ArrayExpress

P26769.

Genevestigator

P26769.

GermOnline

ENSRNOG00000032150. Rattus norvegicus.

Family and domain databases

Gene3D

3.30.70.1230. 2 hits.

InterPro

IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Adenylate_cyclase-like.
[Graphical view]

Pfam

PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]

SMART

SM00044. CYCc. 2 hits.
[Graphical view]

SUPFAM

SSF55073. A/G_cyclase. 2 hits.

PROSITE

PS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P26769.

ChEMBL

CHEMBL2958.

EvolutionaryTrace

P26769.

NextBio

615124.

Entry information

Entry name

ADCY2_RAT

Accession

Primary (citable) accession number: P26769

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents