P84309 (ADCY5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Adenylate cyclase type 5
EC=4.6.1.1

Alternative name(s):
ATP pyrophosphate-lyase 5
Adenylate cyclase type V
Adenylyl cyclase 5

Gene names

Name:

Adcy5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1262 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is a membrane-bound, calcium-inhibitable adenylyl cyclase.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 2 magnesium ions per subunit By similarity. UniProtKB P30803
Enzyme regulation	Inhibition by calcium in the submicromolar concentration range By similarity. Phosphorylation by RAF1 results in its activation By similarity. UniProtKB Q04400
Subunit structure	Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2. Interacts with RAF1 By similarity. Ref.4
Subcellular location	Membrane; Multi-pass membrane protein By similarity. Cell projection › cilium Ref.4.
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	Cell projection Cilium Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenosine receptor signaling pathway Inferred from genetic interaction PubMed 12223546. Source: MGI adenylate cyclase-activating dopamine receptor signaling pathway Inferred from genetic interaction PubMed 12223546. Source: MGI adenylate cyclase-inhibiting dopamine receptor signaling pathway Inferred from genetic interaction PubMed 12223546. Source: MGI intracellular signal transduction Inferred from electronic annotation. Source: InterPro locomotory behavior Inferred from mutant phenotype PubMed 12665504. Source: MGI neuromuscular process controlling balance Inferred from mutant phenotype PubMed 12665504. Source: MGI
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay PubMed 18164588. Source: BHF-UCL primary cilium Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Inferred from direct assay PubMed 17593019. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P84309-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P84309-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1259-1262: PPLS → LGHDGVVGKL...GSEQKKIFIK

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1262	1262	Adenylate cyclase type 5		PRO_0000195695
Regions
	Topological domain	1 – 196	196	Cytoplasmic Potential
	Transmembrane	197 – 217	21	Helical; Potential
	Transmembrane	243 – 263	21	Helical; Potential
	Transmembrane	269 – 289	21	Helical; Potential
	Transmembrane	300 – 320	21	Helical; Potential
	Transmembrane	326 – 346	21	Helical; Potential
	Transmembrane	375 – 395	21	Helical; Potential
	Topological domain	396 – 763	368	Cytoplasmic Potential
	Transmembrane	764 – 784	21	Helical; Potential
	Transmembrane	790 – 810	21	Helical; Potential
	Transmembrane	837 – 857	21	Helical; Potential
	Topological domain	858 – 910	53	Extracellular Potential
	Transmembrane	911 – 931	21	Helical; Potential
	Transmembrane	936 – 956	21	Helical; Potential
	Transmembrane	985 – 1005	21	Helical; Potential
	Topological domain	1006 – 1262	257	Cytoplasmic Potential
	Domain	470 – 597	128	Guanylate cyclase 1
	Domain	1072 – 1211	140	Guanylate cyclase 2
	Coiled coil	1019 – 1045	27	Potential
	Compositional bias	64 – 67	4	Poly-Gln
	Compositional bias	141 – 147	7	Poly-Ala
Sites
	Metal binding	475	1	Magnesium 1 By similarity
	Metal binding	475	1	Magnesium 2 By similarity
	Metal binding	476	1	Magnesium 2; via carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	8	1	Phosphoserine Ref.3
	Glycosylation	239	1	N-linked (GlcNAc...) Potential
	Glycosylation	834	1	N-linked (GlcNAc...) Potential
	Glycosylation	871	1	N-linked (GlcNAc...) Potential
	Glycosylation	888	1	N-linked (GlcNAc...) Potential
	Glycosylation	973	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	1259 – 1262	4	PPLS → LGHDGVVGKLKAGLGVSMEL KGLLFHCGEVTPPHNVWGTG TGRRVACAILSPHLHAQRQC PVRETGLLTREARGHQARSS GSEQKKIFIK in isoform 2.		VSP_022224
Experimental info
	Sequence conflict	25	1	G → S in AAH90846. Ref.2
	Sequence conflict	686	1	G → D in BAE28048. Ref.1
	Sequence conflict	924	1	V → M in AAH90846. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: 342966E7CA67E28D	FASTA	1,262	139,122
	10 20 30 40 50 60 MSGSKSVSPP GYAAQTAASP APRGGPEHRA AWGEADSRAN GYPHAPGGST RGSTKRSGGA 70 80 90 100 110 120 VTPQQQQRLA SRWRGGDDDE DPPLSGDDPL AGGFGFSFRS KSAWQERGGD DGGRGSRRQR 130 140 150 160 170 180 RGAAGGGSTR APPAGGSGSS AAAAAAAGGT EVRPRSVELG LEERRGKGRA AEELEPGTGI 190 200 210 220 230 240 VEDGDGSEDG GSSVASGSGT GAVLSLGACC LALLQIFRSK KFPSDKLERL YQRYFFRLNQ 250 260 270 280 290 300 SSLTMLMAVL VLVCLVMLAF HAARPPLQIA YLAVLAAAVG VILIMAVLCN RAAFHQDHMG 310 320 330 340 350 360 LACYALIAVV LAVQVVGLLL PQPRSASEGI WWTVFFIYTI YTLLPVRMRA AVLSGVLLSA 370 380 390 400 410 420 LHLAISLHTN SQDQFLLKQL VSNVLIFSCT NIVGVCTHYP AEVSQRQAFQ ETRECIQARL 430 440 450 460 470 480 HSQRENQQQE RLLLSVLPRH VAMEMKADIN AKQEDMMFHK IYIQKHDNVS ILFADIEGFT 490 500 510 520 530 540 SLASQCTAQE LVMTLNELFA RFDKLAAENH CLRIKILGDC YYCVSGLPEA RADHAHCCVE 550 560 570 580 590 600 MGMDMIEAIS LVREVTGVNV NMRVGIHSGR VHCGVLGLRK WQFDVWSNDV TLANHMEAGG 610 620 630 640 650 660 KAGRIHITKA TLNYLNGDYE VEPGCGGDRN AYLKEHSIET FLILSCTQKR KEEKAMIAKM 670 680 690 700 710 720 NRQRTNSIGH NPPHWGAERP FYNHLGGNQV SKEMKRMGFE DPKDKNAQES ANPEDEVDEF 730 740 750 760 770 780 LGRAIDARSI DRLRSEHVRK FLLTFREPDL EKKYSKQVDD RFGAYVACAS LVFLFICFVQ 790 800 810 820 830 840 ITIVPHSLFM LSFYLSCFLL LALVVFVSVI YACVKLFPTP LQTLSRKIVR SKKNSTLVGV 850 860 870 880 890 900 FTITLVFLSA FVNMFMCNSK NLVGCLAEEH NITVNQVNAC HVMESAFNYS LGDEQGFCGS 910 920 930 940 950 960 PQPNCNFPEY FTYSVLLSLL ACSVFLQISC IGKLVLMLAI EFIYVLIVEV PGVTLFDNAD 970 980 990 1000 1010 1020 LLVTANAIDF SNNGTSQCPE HATKVALKVV TPIIISVFVL ALYLHAQQVE STARLDFLWK 1030 1040 1050 1060 1070 1080 LQATEEKEEM EELQAYNRRL LHNILPKDVA AHFLARERRN DELYYQSCEC VAVMFASIAN 1090 1100 1110 1120 1130 1140 FSEFYVELEA NNEGVECLRL LNEIIADFDE IISEDRFRQL EKIKTIGSTY MAASGLNDST 1150 1160 1170 1180 1190 1200 YDKAGKTHIK AIADFAMKLM DQMKYINEHS FNNFQMKIGL NIGPVVAGVI GARKPQYDIW 1210 1220 1230 1240 1250 1260 GNTVNVASRM DSTGVPDRIQ VTTDMYQVLA ANTYQLECRG VVKVKGKGEM MTYFLNGGPP LS
	Isoform 2 [UniParc]. Checksum: B4997E3A2BC14305	FASTA	1,348	148,383
	10 20 30 40 50 60 MSGSKSVSPP GYAAQTAASP APRGGPEHRA AWGEADSRAN GYPHAPGGST RGSTKRSGGA 70 80 90 100 110 120 VTPQQQQRLA SRWRGGDDDE DPPLSGDDPL AGGFGFSFRS KSAWQERGGD DGGRGSRRQR 130 140 150 160 170 180 RGAAGGGSTR APPAGGSGSS AAAAAAAGGT EVRPRSVELG LEERRGKGRA AEELEPGTGI 190 200 210 220 230 240 VEDGDGSEDG GSSVASGSGT GAVLSLGACC LALLQIFRSK KFPSDKLERL YQRYFFRLNQ 250 260 270 280 290 300 SSLTMLMAVL VLVCLVMLAF HAARPPLQIA YLAVLAAAVG VILIMAVLCN RAAFHQDHMG 310 320 330 340 350 360 LACYALIAVV LAVQVVGLLL PQPRSASEGI WWTVFFIYTI YTLLPVRMRA AVLSGVLLSA 370 380 390 400 410 420 LHLAISLHTN SQDQFLLKQL VSNVLIFSCT NIVGVCTHYP AEVSQRQAFQ ETRECIQARL 430 440 450 460 470 480 HSQRENQQQE RLLLSVLPRH VAMEMKADIN AKQEDMMFHK IYIQKHDNVS ILFADIEGFT 490 500 510 520 530 540 SLASQCTAQE LVMTLNELFA RFDKLAAENH CLRIKILGDC YYCVSGLPEA RADHAHCCVE 550 560 570 580 590 600 MGMDMIEAIS LVREVTGVNV NMRVGIHSGR VHCGVLGLRK WQFDVWSNDV TLANHMEAGG 610 620 630 640 650 660 KAGRIHITKA TLNYLNGDYE VEPGCGGDRN AYLKEHSIET FLILSCTQKR KEEKAMIAKM 670 680 690 700 710 720 NRQRTNSIGH NPPHWGAERP FYNHLGGNQV SKEMKRMGFE DPKDKNAQES ANPEDEVDEF 730 740 750 760 770 780 LGRAIDARSI DRLRSEHVRK FLLTFREPDL EKKYSKQVDD RFGAYVACAS LVFLFICFVQ 790 800 810 820 830 840 ITIVPHSLFM LSFYLSCFLL LALVVFVSVI YACVKLFPTP LQTLSRKIVR SKKNSTLVGV 850 860 870 880 890 900 FTITLVFLSA FVNMFMCNSK NLVGCLAEEH NITVNQVNAC HVMESAFNYS LGDEQGFCGS 910 920 930 940 950 960 PQPNCNFPEY FTYSVLLSLL ACSVFLQISC IGKLVLMLAI EFIYVLIVEV PGVTLFDNAD 970 980 990 1000 1010 1020 LLVTANAIDF SNNGTSQCPE HATKVALKVV TPIIISVFVL ALYLHAQQVE STARLDFLWK 1030 1040 1050 1060 1070 1080 LQATEEKEEM EELQAYNRRL LHNILPKDVA AHFLARERRN DELYYQSCEC VAVMFASIAN 1090 1100 1110 1120 1130 1140 FSEFYVELEA NNEGVECLRL LNEIIADFDE IISEDRFRQL EKIKTIGSTY MAASGLNDST 1150 1160 1170 1180 1190 1200 YDKAGKTHIK AIADFAMKLM DQMKYINEHS FNNFQMKIGL NIGPVVAGVI GARKPQYDIW 1210 1220 1230 1240 1250 1260 GNTVNVASRM DSTGVPDRIQ VTTDMYQVLA ANTYQLECRG VVKVKGKGEM MTYFLNGGLG 1270 1280 1290 1300 1310 1320 HDGVVGKLKA GLGVSMELKG LLFHCGEVTP PHNVWGTGTG RRVACAILSP HLHAQRQCPV 1330 1340 RETGLLTREA RGHQARSSGS EQKKIFIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Head.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6. Tissue: Brain and Retina.
[3]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, MASS SPECTROMETRY. Tissue: Brain cortex.
[4]	"Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases." Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J., Pontoglio M., Somlo S., Igarashi P. Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AKAP5; ADCY6; PDE4C AND PKD2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK147649 mRNA. Translation: BAE28048.1. AK160942 mRNA. Translation: BAE36104.1. BC035550 mRNA. No translation available. BC090846 mRNA. Translation: AAH90846.1.
IPI	IPI00756908. IPI00816877.
RefSeq	NP_001012783.3. NM_001012765.4.
UniGene	Mm.41137.
3D structure databases
ProteinModelPortal	P84309.
SMR	P84309. Positions 455-644, 1065-1256.
ModBase	Search...
PTM databases
PhosphoSite	P84309.
Proteomic databases
PaxDb	P84309.
PRIDE	P84309.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000114913; ENSMUSP00000110563; ENSMUSG00000022840.
GeneID	224129.
KEGG	mmu:224129.
UCSC	uc007zbj.1. mouse.
Organism-specific databases
CTD	111.
MGI	MGI:99673. Adcy5.
Phylogenomic databases
eggNOG	COG2114.
GeneTree	ENSGT00680000099709.
HOGENOM	HOG000006941.
HOVERGEN	HBG050458.
KO	K08045.
OMA	GDEQGFC.
OrthoDB	EOG4255S0.
Gene expression databases
Bgee	P84309.
CleanEx	MM_ADCY5.
Genevestigator	P84309.
GermOnline	ENSMUSG00000022840. Mus musculus.
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	P84309.
ChEMBL	CHEMBL2561.
NextBio	377103.
SOURCE	Search...

Entry information

Entry name

ADCY5_MOUSE

Accession

Primary (citable) accession number: P84309
Secondary accession number(s): Q3TU67, Q3UH09, Q5BL06

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 21, 2004
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program