Adenylate cyclase type 9 - Homo sapiens (Human)

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O60503 (ADCY9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 116. History...

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

Documents (5) |

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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 9
EC=4.6.1.1

Alternative name(s):
ATP pyrophosphate-lyase 9
Adenylate cyclase type IX
Adenylyl cyclase 9

Gene names

Name:	ADCY9
Synonyms:	KIAA0520

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1353 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a fundamental role in situations where fine interplay between intracellular calcium and cAMP determines the cellular function. May be a physiologically relevant docking site for calcineurin By similarity.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 2 magnesium ions per subunit.
Enzyme regulation	Insensitive to calcium/calmodulin, forskolin and somatostatin. Stimulated by beta-adrenergic receptor activation.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in multiple cells of the lung, with expression highest in airway smooth muscle. Ref.2
Sequence similarities	Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 2 guanylate cyclase domains.
Sequence caution	The sequence AAC24201.1 differs from that shown. Reason: Frameshift at position 1252. The sequence BAA25446.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	cAMP biosynthesis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	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	activation of phospholipase C activity Traceable author statement. Source: Reactome activation of protein kinase A activity Traceable author statement. Source: Reactome adenylate cyclase-activating G-protein coupled receptor signaling pathway Traceable author statement. Source: Reactome adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Traceable author statement. Source: Reactome cellular response to glucagon stimulus Traceable author statement. Source: Reactome energy reserve metabolic process Traceable author statement. Source: Reactome epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome intracellular signal transduction Inferred from electronic annotation. Source: InterPro neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome synaptic transmission Traceable author statement. Source: Reactome transmembrane transport Traceable author statement. Source: Reactome water transport Traceable author statement. Source: Reactome
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1353

1353

Adenylate cyclase type 9

PRO_0000195708

Regions

Topological domain

1 – 117

117

Cytoplasmic Potential

Transmembrane

118 – 138

Helical; Potential

Topological domain

139 – 141

Extracellular Potential

Transmembrane

142 – 162

Helical; Potential

Topological domain

163 – 171

Cytoplasmic Potential

Transmembrane

172 – 192

Helical; Potential

Topological domain

193 – 215

Extracellular Potential

Transmembrane

216 – 235

Helical; Potential

Topological domain

236 – 241

Cytoplasmic Potential

Transmembrane

242 – 259

Helical; Potential

Topological domain

260 – 280

Extracellular Potential

Transmembrane

281 – 301

Helical; Potential

Topological domain

302 – 786

485

Cytoplasmic Potential

Transmembrane

787 – 807

Helical; Potential

Topological domain

808 – 818

Extracellular Potential

Transmembrane

819 – 839

Helical; Potential

Topological domain

840 – 867

Cytoplasmic Potential

Transmembrane

868 – 888

Helical; Potential

Topological domain

889 – 891

Extracellular Potential

Transmembrane

892 – 912

Helical; Potential

Topological domain

913 – 920

Cytoplasmic Potential

Transmembrane

921 – 941

Helical; Potential

Topological domain

942 – 975

Extracellular Potential

Transmembrane

976 – 996

Helical; Potential

Topological domain

997 – 1353

357

Cytoplasmic Potential

Domain

394 – 521

128

Guanylate cyclase 1

Domain

1058 – 1198

141

Guanylate cyclase 2

Sites

Metal binding

399

Magnesium 1 By similarity

Metal binding

399

Magnesium 2 By similarity

Metal binding

400

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

443

Magnesium 1 By similarity

Metal binding

443

Magnesium 2 By similarity

Amino acid modifications

Modified residue

608

Phosphothreonine By similarity

Modified residue

610

Phosphoserine By similarity

Modified residue

1259

Phosphoserine Ref.11

Modified residue

1307

Phosphoserine Ref.12

Glycosylation

206

N-linked (GlcNAc...) Potential

Glycosylation

955

N-linked (GlcNAc...) Potential

Glycosylation

964

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

772

I → M in 37.5% of the Asian population, in 30% of the Caucasian population and in 16.3% of the African-American population; reduced adenylyl cyclase activity in response to stimulation of the beta-adregnergic receptor by the agonists Mn(2+), isoproteronol and NaF; increased albuterol-stimulated adenylyl cyclase activity in the presence of corticosteroid. Ref.2 Ref.3
Corresponds to variant rs2230739 [ dbSNP | Ensembl ].

VAR_023750

Experimental info

Sequence conflict

493

G → R in CAB65084. Ref.4

Sequence conflict

884

V → A in CAB65084. Ref.4

Sequence conflict

1154

N → S in CAB65084. Ref.4

Sequence conflict

1154

N → S in BAA25446. Ref.6

Sequence conflict

1308

P → R in CAB65084. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

O60503 [UniParc].

Last modified December 13, 2002. Version 4.
Checksum: 4CBF051EA49B5B7B
Show »

FASTA

1,353

150,701

        10         20         30         40         50         60 
MASPPHQQLL HHHSTEVSCD SSGDSNSVRV KINPKQLSSN SHPKHCKYSI SSSCSSSGDS 

        70         80         90        100        110        120 
GGVPRRVGGG GRLRRQKKLP QLFERASSRW WDPKFDSVNL EEACLERCFP QTQRRFRYAL 

       130        140        150        160        170        180 
FYIGFACLLW SIYFAVHMRS RLIVMVAPAL CFLLVCVGFF LFTFTKLYAR HYAWTSLALT 

       190        200        210        220        230        240 
LLVFALTLAA QFQVLTPVSG RGDSSNLTAT ARPTDTCLSQ VGSFSMCIEV LFLLYTVMHL 

       250        260        270        280        290        300 
PLYLSLCLGV AYSVLFETFG YHFRDEACFP SPGAGALHWE LLSRGLLHGC IHAIGVHLFV 

       310        320        330        340        350        360 
MSQVRSRSTF LKVGQSIMHG KDLEVEKALK ERMIHSVMPR IIADDLMKQG DEESENSVKR 

       370        380        390        400        410        420 
HATSSPKNRK KKSSIQKAPI AFRPFKMQQI EEVSILFADI VGFTKMSANK SAHALVGLLN 

       430        440        450        460        470        480 
DLFGRFDRLC EETKCEKIST LGDCYYCVAG CPEPRADHAY CCIEMGLGMI KAIEQFCQEK 

       490        500        510        520        530        540 
KEMVNMRVGV HTGTVLCGIL GMRRFKFDVW SNDVNLANLM EQLGVAGKVH ISEATAKYLD 

       550        560        570        580        590        600 
DRYEMEDGKV IERLGQSVVA DQLKGLKTYL ISGQRAKESR CSCAEALLSG FEVIDGSQVS 

       610        620        630        640        650        660 
SGPRGQGTAS SGNVSDLAQT VKTFDNLKTC PSCGITFAPK SEAGAEGGAP QNGCQDEHKN 

       670        680        690        700        710        720 
STKASGGPNP KTQNGLLSPP QEEKLTNSQT SLCEILQEKG RWAGVSLDQS ALLPLRFKNI 

       730        740        750        760        770        780 
REKTDAHFVD VIKEDSLMKD YFFKPPINQF SLNFLDQELE RSYRTSYQEE VIKNSPVKTF 

       790        800        810        820        830        840 
ASPTFSSLLD VFLSTTVFLT LSTTCFLKYE AATVPPPPAA LAVFSAALLL EVLSLAVSIR 

       850        860        870        880        890        900 
MVFFLEDVMA CTKRLLEWIA GWLPRHCIGA ILVSLPALAV YSHVTSEYET NIHFPVFTGS 

       910        920        930        940        950        960 
AALIAVVHYC NFCQLSSWMR SSLATVVGAG PLLLLYVSLC PDSSVLTSPL DAVQNFSSER 

       970        980        990       1000       1010       1020 
NPCNSSVPRD LRRPASLIGQ EVVLVFFLLL LLVWFLNREF EVSYRLHYHG DVEADLHRTK 

      1030       1040       1050       1060       1070       1080 
IQSMRDQADW LLRNIIPYHV AEQLKVSQTY SKNHDSGGVI FASIVNFSEF YEENYEGGKE 

      1090       1100       1110       1120       1130       1140 
CYRVLNELIG DFDELLSKPD YSSIEKIKTI GATYMAASGL NTAQAQDGSH PQEHLQILFE 

      1150       1160       1170       1180       1190       1200 
FAKEMMRVVD DFNNNMLWFN FKLRVGFNHG PLTAGVIGTT KLLYDIWGDT VNIASRMDTT 

      1210       1220       1230       1240       1250       1260 
GVECRIQVSE ESYRVLSKMG YDFDYRGTVN VKGKGQMKTY LYPKCTDHRV IPQHQLSISP 

      1270       1280       1290       1300       1310       1320 
DIRVQVDGSI GRSPTDEIAN LVPSVQYVDK TSLGSDSSTQ AKDAHLSPKR PWKEPVKAEE 

      1330       1340       1350 
RGRFGKAIEK DDCDETGIEE ANELTKLNVS KSV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, chromosomal mapping, and regulatory properties of the human type 9 adenylyl cyclase (ADCY9)." Hacker B.M., Tomlinson J.E., Wayman G.A., Sultana R., Chan G., Villacres E., Disteche C., Storm D.R. Genomics 50:97-104(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"An Ile to Met polymorphism in the catalytic domain of adenylyl cyclase type 9 confers reduced beta2-adrenergic receptor stimulation." Small K.M., Brown K.M., Theiss C.T., Seman C.A., Weiss S.T., Liggett S.B. Pharmacogenetics 13:535-541(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT MET-772.
[3]	"Molecular properties and pharmacogenetics of a polymorphism of adenylyl cyclase type 9 in asthma: interaction between beta-agonist and corticosteroid pathways." Tantisira K.G., Small K.M., Litonjua A.A., Weiss S.T., Liggett S.B. Hum. Mol. Genet. 14:1671-1677(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-772.
[4]	"Cloning and characterisation of human adenylyl cyclase IX: differential mRNA regulation and inhibition by Ca2+/calcineurin." Paterson J.M., Smith S.M., Simpson J., Grace O.C., Bell J.E., Antoni F.A. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Mutation screening, case control study and transmission disequilibrium analysis of adenylate cyclase type 9 (ADCY9) gene in functional psychoses." Toyota T., Yamada K., Meerabux J., Hattori E., Saito K., Yoshitsugu K., Shimizu H., Nankai M., Toru M., Detera-Wadleigh S.D., Yoshikawa T. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[8]	Ohara O., Nagase T., Kikuno R., Ishikawa K. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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].
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1259, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1307, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF036927 mRNA. Translation: AAC24201.1. Frameshift. DQ008441 mRNA. Translation: AAY27880.1. DQ005545 mRNA. Translation: AAY21237.1. AJ133123 mRNA. Translation: CAB65084.1. AY028959 AY028957 Genomic DNA. Translation: AAK29464.1. AB011092 mRNA. Translation: BAA25446.3. Different initiation. CH471112 Genomic DNA. Translation: EAW85331.1. CH471112 Genomic DNA. Translation: EAW85332.1. BC136657 mRNA. Translation: AAI36658.1. BC136658 mRNA. Translation: AAI36659.1. BC151207 mRNA. Translation: AAI51208.1.
IPI	IPI00030099.
RefSeq	NP_001107.2. NM_001116.3.
UniGene	Hs.391860. Hs.610484.
3D structure databases
ProteinModelPortal	O60503.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000294016.
PTM databases
PhosphoSite	O60503.
Proteomic databases
PaxDb	O60503.
PRIDE	O60503.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000294016; ENSP00000294016; ENSG00000162104.
GeneID	115.
KEGG	hsa:115.
UCSC	uc002cvx.3. human.
Organism-specific databases
CTD	115.
GeneCards	GC16M004003.
HGNC	HGNC:240. ADCY9.
HPA	HPA041328. HPA044225.
MIM	603302. gene.
neXtProt	NX_O60503.
PharmGKB	PA30.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2114.
HOVERGEN	HBG050459.
InParanoid	O60503.
KO	K08049.
OMA	HMRSKLI.
OrthoDB	EOG4CRKZB.
PhylomeDB	O60503.
Enzyme and pathway databases
Pathway_Interaction_DB	endothelinpathway. Endothelins. lysophospholipid_pathway. LPA receptor mediated events. lpa4_pathway. LPA4-mediated signaling events.
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease. REACT_13685. Neuronal System. REACT_15518. Transmembrane transport of small molecules. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	O60503.
Bgee	O60503.
CleanEx	HS_ADCY9.
Genevestigator	O60503.
GermOnline	ENSG00000162104. Homo sapiens.
Family and domain databases
Gene3D	3.30.70.1230. 2 hits.
InterPro	IPR001054. A/G_cyclase. IPR018297. A/G_cyclase_CS. [Graphical view]
Pfam	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	O60503.
ChEMBL	CHEMBL2655.
ChiTaRS	ADCY9. human.
GenomeRNAi	115.
NextBio	445.
SOURCE	Search...

Entry information

Entry name

ADCY9_HUMAN

Accession

Primary (citable) accession number: O60503
Secondary accession number(s): A7E2V5

Q9UGP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	December 13, 2002
Last modified:	May 29, 2013
This is version 116 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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

Natural variations

Experimental info

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