UniProtKB - P26769 (ADCY2_RAT)

BLAST

>sp|P26769|ADCY2_RAT Adenylate cyclase type 2 OS=Rattus norvegicus OX=10116 GN=Adcy2 PE=1 SV=1
MRRRRYLRDRAEAAAAAAAGGGEGLQRSRDWLYESYYCMSQQHPLIVFLLLIVMGACLAL
LAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRVFSLVIWICLVAMG
YLFMCFGGTVSAWDQVSFFLFIIFVVYTMLPFNMRDAIIASILTSSSHTIVLSVYLSATP
GAKEHLFWQILANVIIFICGNLAGAYHKHLMELALQQTYRDTCNCIKSRIKLEFEKRQQE
RLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFTR
LASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKM
GLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGV
PGRVHISSVTLEHLNGAYKVEEGDGEIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPRH
TLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTLR
TKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKNIEKEYRATALPAFK
YYVTCACLIFLCIFIVQILVLPKTSILGFSFGAAFLSLIFILFVCFAGQLLQCSKKASTS
LMWLLKSSGIIANRPWPRISLTIVTTAIILTMAVFNMFFLSNSEETTLPTANTSNANVSV
PDNQASILHARNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHTH
AHVLDAYSQVLFQRPGIWKDLKTMGSVSLSIFFITLLVLGRQSEYYCRLDFLWKNKFKKE
REEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFYT
ESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAIPSQEHAQ
EPERQYMHIGTMVEFAYALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDIW
GNTVNVASRMDSTGVLDKIQVTEETSLILQTLGYTCTCRGIINVKGKGDLKTYFVNTEMS
RSLSQSNLAS

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Format
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History
Entry version 160 (07 Nov 2018)
Sequence version 1 (01 Aug 1992)
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Protein

Adenylate cyclase type 2

Gene

Adcy2

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:22906005, PubMed:24363043, PubMed:10427002, PubMed:1719547, PubMed:7761832, PubMed:21596131, PubMed:11087399, PubMed:15591060, PubMed:19243146, PubMed:16766715). Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production (PubMed:24363043). Functions in signaling cascades downstream of the muscarinic acetylcholine receptors (PubMed:22906005).10 Publications

Catalytic activityⁱ

ATP = 3',5'-cyclic AMP + diphosphate.10 Publications

Cofactorⁱ

Mg²⁺6 Publications, Mn²⁺3 PublicationsNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).1 Publication1 Publication

Activity regulationⁱ

Activated by forskolin (PubMed:1719547, PubMed:22906005, PubMed:24363043). Is not activated by calmodulin (PubMed:1719547). Inhibited by calcium ions, already at micromolar concentration. Activated by the G protein alpha subunit GNAS (PubMed:1719547, PubMed:7761832, PubMed:21596131). Activated by the G protein beta and gamma subunit complex (PubMed:7761832, PubMed:21596131, PubMed:22906005). Phosphorylation by RAF1 results in its activation (By similarity). Phosphorylation by PKC activates the enzyme (PubMed:22906005).By similarity5 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	294	Magnesium 1; catalyticPROSITE-ProRule annotationCurated	1
Metal bindingⁱ	294	Magnesium 2; catalyticPROSITE-ProRule annotationCurated1 Publication	1
Metal bindingⁱ	295	Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotationCurated1 Publication	1
Metal bindingⁱ	338	Magnesium 1; catalyticPROSITE-ProRule annotationCurated	1
Metal bindingⁱ	338	Magnesium 2; catalyticPROSITE-ProRule annotationCurated1 Publication	1
Binding siteⁱ	382	ATPBy similarity	1
Binding siteⁱ	938	ATP5 Publications	1
Binding siteⁱ	1065	ATP5 Publications	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	294 – 299	ATPBy similarity	6
Nucleotide bindingⁱ	336 – 338	ATPBy similarity	3
Nucleotide bindingⁱ	1018 – 1020	ATP5 Publications	3
Nucleotide bindingⁱ	1025 – 1029	ATPCombined sources1 Publication	5

GO - Molecular functionⁱ

adenylate cyclase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 10427002
adenylate cyclase binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18164588
ATP binding Source: UniProtKB-KW
G-protein beta/gamma-subunit complex binding
Source: RGD
Inferred from physical interactionⁱ
- 16967511
magnesium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10427002
manganese ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 10427002
protein heterodimerization activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 18164588

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

adenylate cyclase-activating G protein-coupled receptor signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 7761832
adenylate cyclase-modulating G protein-coupled receptor signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 18164588
cAMP biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 10427002
cAMP-mediated signaling
Source: UniProtKB
Inferred from direct assayⁱ
- 7761832
cellular response to forskolin
Source: UniProtKB
Inferred from direct assayⁱ
- 1719547

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Biological process	cAMP biosynthesis
Ligand	ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAⁱ	4.6.1.1 5301

BRENDAⁱ

4.6.1.1 5301

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Adenylate cyclase type 2 (EC:4.6.1.17 Publications) Alternative name(s): ATP pyrophosphate-lyase 2 Adenylate cyclase type II Adenylyl cyclase 2 Short name: AC21 Publication
Gene namesⁱ	Name:Adcy2
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	619965 Adcy2

RGDⁱ

619965 Adcy2

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 44	CytoplasmicSequence analysisAdd BLAST	44
Transmembraneⁱ	45 – 65	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	75 – 95	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	107 – 127	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	132 – 152	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	157 – 177	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	186 – 206	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	207 – 600	CytoplasmicSequence analysisAdd BLAST	394
Transmembraneⁱ	601 – 621	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	626 – 646	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	679 – 699	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	734 – 754	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	763 – 783	HelicalSequence analysisAdd BLAST	21
Transmembraneⁱ	800 – 820	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	821 – 1090	CytoplasmicSequence analysisCuratedAdd BLAST	270

Keywords - Cellular componentⁱ

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	490	S → A: Reduces activation by PKC. Abolishes activation by PKC; when associated with A-543. 1 Publication	1
Mutagenesisⁱ	490	S → D: Increases basal level of enzyme activity. Abolishes activation by PKC; when associated with D-543. 1 Publication	1
Mutagenesisⁱ	543	S → A: Reduces activation by PKC. Abolishes activation by PKC; when associated with A-490. 1 Publication	1
Mutagenesisⁱ	543	S → D: Increases basal level of enzyme activity. Abolishes activation by PKC; when associated with D-490. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL2958

ChEMBLⁱ

CHEMBL2958

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000195686	1 – 1090	Adenylate cyclase type 2Add BLAST		1090

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	490	Phosphoserine; by PKC1 Publication	1
Modified residueⁱ	543	Phosphoserine; by PKC1 Publication	1
Glycosylationⁱ	712	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	717	N-linked (GlcNAc...) asparagineSequence analysis	1

Post-translational modificationⁱ

Phosphorylated by RAF1 (By similarity).By similarity

Keywords - PTMⁱ

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbⁱ	P26769
PRIDEⁱ	P26769

PTM databases

iPTMnetⁱ	P26769
PhosphoSitePlusⁱ	P26769

Expressionⁱ

Tissue specificityⁱ

Expressed in brain, olfactory epithelium and lung.1 Publication

Interactionⁱ

Subunit structureⁱ

Interacts with RAF1 (By similarity). Interacts with GNAS (PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Interacts with the G protein beta and gamma subunit complex (PubMed:21596131).By similarity7 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
AKAP9	Q99996-4	3	EBI-1027877,EBI-15676518	From a different organism.
PDE4D	Q08499-2	3	EBI-1027877,EBI-8095525	From a different organism.

GO - Molecular functionⁱ

adenylate cyclase binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 18164588
protein heterodimerization activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 18164588

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	249536, 1 interactor
Database of interacting proteins More...DIPⁱ	DIP-164N
IntActⁱ	P26769, 8 interactors
Molecular INTeraction database More...MINTⁱ	P26769
STRINGⁱ	10116.ENSRNOP00000038994

Chemistry databases

BindingDBⁱ

P26769

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	879 – 891	Combined sources	13
Helixⁱ	895 – 898	Combined sources	4
Turnⁱ	903 – 908	Combined sources	6
Helixⁱ	909 – 923	Combined sources	15
Helixⁱ	924 – 927	Combined sources	4
Helixⁱ	929 – 931	Combined sources	3
Beta strandⁱ	934 – 940	Combined sources	7
Beta strandⁱ	943 – 948	Combined sources	6
Helixⁱ	967 – 987	Combined sources	21
Turnⁱ	988 – 991	Combined sources	4
Beta strandⁱ	997 – 1010	Combined sources	14
Beta strandⁱ	1012 – 1014	Combined sources	3
Beta strandⁱ	1016 – 1021	Combined sources	6
Helixⁱ	1022 – 1032	Combined sources	11
Beta strandⁱ	1039 – 1041	Combined sources	3
Helixⁱ	1043 – 1052	Combined sources	10
Beta strandⁱ	1056 – 1064	Combined sources	9
Turnⁱ	1065 – 1067	Combined sources	3
Beta strandⁱ	1068 – 1075	Combined sources	8

Show more details

3D structure databases

ProteinModelPortalⁱ	P26769
SMRⁱ	P26769
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P26769

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	904 – 921	Interaction with GNAS1 PublicationAdd BLAST		18
Regionⁱ	989 – 992	Interaction with GNAS1 Publication		4

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.6 Publications

Sequence similaritiesⁱ

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation

Keywords - Domainⁱ

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3619 Eukaryota COG2114 LUCA
HOGENOMⁱ	HOG000006941
HOVERGENⁱ	HBG050458
InParanoidⁱ	P26769
KEGG Orthology (KO) More...KOⁱ	K08042
PhylomeDBⁱ	P26769

Family and domain databases

Gene3Dⁱ	3.30.70.1230, 2 hits
InterProⁱ	View protein in InterPro IPR001054 A/G_cyclase IPR018297 A/G_cyclase_CS IPR032628 AC_N IPR030672 Adcy IPR009398 Adcy_conserved_dom IPR029787 Nucleotide_cyclase
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16214 AC_N, 1 hit PF06327 DUF1053, 1 hit PF00211 Guanylate_cyc, 2 hits
PIRSFⁱ	PIRSF039050 Ade_cyc, 1 hit
SMARTⁱ	View protein in SMART SM00044 CYCc, 2 hits
SUPFAMⁱ	SSF55073 SSF55073, 2 hits
PROSITEⁱ	View protein in PROSITE PS00452 GUANYLATE_CYCLASE_1, 2 hits PS50125 GUANYLATE_CYCLASE_2, 2 hits

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

P26769-1 [UniParc]FASTA Add 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

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	F1LV12	F1LV12_RAT		Adenylate cyclase type 2 Adenylate cyclase type 2	Adcy2	852	Annotation score:

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M80550 mRNA Translation: AAA40682.1
PIRⁱ	A41541
NCBI Reference Sequences More...RefSeqⁱ	NP_112269.1, NM_031007.1
UniGeneⁱ	Rn.10731

Genome annotation databases

GeneIDⁱ	81636
KEGGⁱ	rno:81636
UCSC genome browser More...UCSCⁱ	RGD:619965 rat

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P26769	Adenylate cyclase type 2		RAT		852	UniRef100_P26769
UPI0000110DF8		RAT		208
UPI00001106EF		RAT		212
UPI000011045D		RAT		220

Protein	Similar proteins		Species	Score	Length	Source
P26769	Adenylate cyclase type 2		HUMAN		1091	UniRef90_P26769
Adenylate cyclase type 2		MOUSE		1090
Adenylate cyclase type 2		RAT		852
Adenylate cyclase		MESAU		1121
Adenylate cyclase		DELLE		1098
+98

Protein	Similar proteins		Species	Score	Length	Source
P26769	Adenylate cyclase type 2		HUMAN		1091	UniRef50_P26769
Adenylate cyclase type 2		MOUSE		1090
Adenylate cyclase type 7		BOVIN		1078
Adenylate cyclase type 2		RAT		852
Adenylate cyclase		MESAU		1121
+634

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ 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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	249536, 1 interactor
DIPⁱ	DIP-164N
IntActⁱ	P26769, 8 interactors
MINTⁱ	P26769
STRINGⁱ	10116.ENSRNOP00000038994

Chemistry databases

BindingDBⁱ	P26769
ChEMBLⁱ	CHEMBL2958

PTM databases

iPTMnetⁱ	P26769
PhosphoSitePlusⁱ	P26769

Proteomic databases

PaxDbⁱ	P26769
PRIDEⁱ	P26769

Protocols and materials databases

Structural Biology Knowledgebase	Search...

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	KOG3619 Eukaryota COG2114 LUCA
HOGENOMⁱ	HOG000006941
HOVERGENⁱ	HBG050458
InParanoidⁱ	P26769
KOⁱ	K08042
PhylomeDBⁱ	P26769

Enzyme and pathway databases

BRENDAⁱ	4.6.1.1 5301

BRENDAⁱ

4.6.1.1 5301

Miscellaneous databases

EvolutionaryTraceⁱ	P26769
Protein Ontology More...PROⁱ	PR:P26769

Family and domain databases

Gene3Dⁱ	3.30.70.1230, 2 hits
InterProⁱ	View protein in InterPro IPR001054 A/G_cyclase IPR018297 A/G_cyclase_CS IPR032628 AC_N IPR030672 Adcy IPR009398 Adcy_conserved_dom IPR029787 Nucleotide_cyclase
Pfamⁱ	View protein in Pfam PF16214 AC_N, 1 hit PF06327 DUF1053, 1 hit PF00211 Guanylate_cyc, 2 hits
PIRSFⁱ	PIRSF039050 Ade_cyc, 1 hit
SMARTⁱ	View protein in SMART SM00044 CYCc, 2 hits
SUPFAMⁱ	SSF55073 SSF55073, 2 hits
PROSITEⁱ	View protein in PROSITE PS00452 GUANYLATE_CYCLASE_1, 2 hits PS50125 GUANYLATE_CYCLASE_2, 2 hits
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ADCY2_RAT
Accessionⁱ	P26769Primary (citable) accession number: P26769
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
	Last sequence update:	August 1, 1992
	Last modified:	November 7, 2018
	This is version 160 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P26769 (ADCY2_RAT)

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Adenylate cyclase type 2

Adcy2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Other locations

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ