Adenylate cyclase type 8 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P40145 (ADCY8_HUMAN)

Last modified November 3, 2009. Version 85. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Adenylate cyclase type 8
    EC=4.6.1.1
Alternative name(s):
    Adenylate cyclase type VIII
    ATP pyrophosphate-lyase 8
    Adenylyl cyclase 8
    Ca(2+)/calmodulin-activated adenylyl cyclase

Gene names

Name:

ADCY8

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	1251 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This is a membrane-bound, calcium-stimulable adenylyl cyclase. May be involved in learning, in memory and in drug dependence By similarity.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Enzyme regulation	Activated by calcium/calmodulin.
Subcellular location	Membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 2 guanylate cyclase domains.

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Ontologies

Keywords
Biological process	cAMP biosynthesis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	activation of adenylate cyclase activity by G-protein signaling pathway Inferred from Experiment. Source: Reactome activation of protein kinase A activity Inferred from Experiment. Source: Reactome cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW hormone-mediated signaling pathway Inferred from Experiment. Source: Reactome inhibition of adenylate cyclase activity by G-protein signaling Inferred from Experiment. Source: Reactome learning or memory Ref.1 Traceable author statement. Source: ProtInc
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Traceable author statement. Source: ProtInc plasma membrane Ref.1 Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium- and calmodulin-responsive adenylate cyclase activity Traceable author statement. Source: ProtInc magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1251

1251

Adenylate cyclase type 8

PRO_0000195705

Regions

Topological domain

1 – 182

182

Cytoplasmic Potential

Transmembrane

183 – 203

Potential

Transmembrane

212 – 232

Potential

Transmembrane

247 – 267

Potential

Transmembrane

274 – 294

Potential

Transmembrane

296 – 316

Potential

Transmembrane

321 – 341

Potential

Topological domain

342 – 715

374

Cytoplasmic Potential

Transmembrane

716 – 736

Potential

Transmembrane

738 – 758

Potential

Transmembrane

787 – 807

Potential

Transmembrane

831 – 851

Potential

Transmembrane

861 – 881

Potential

Transmembrane

894 – 914

Potential

Topological domain

915 – 1251

337

Cytoplasmic Potential

Sites

Metal binding

419

Magnesium 1 By similarity

Metal binding

419

Magnesium 2 By similarity

Metal binding

420

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

463

Magnesium 1 By similarity

Metal binding

463

Magnesium 2 By similarity

Amino acid modifications

Glycosylation

817

N-linked (GlcNAc...) Potential

Glycosylation

821

N-linked (GlcNAc...) Potential

Glycosylation

888

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

A → T: dbSNP rs2228949.

VAR_029188

Natural variant

881

F → L in a colorectal cancer sample; somatic mutation. Ref.3

VAR_036328

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Sequences

Sequence

Length

Mass (Da)

Tools

P40145-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: ABF25C40493E07C3
Show »

FASTA

1,251

140,122

        10         20         30         40         50         60 
MELSDVRCLT GSEELYTIHP TPPAGDGRSA SRPQRLLWQT AVRHITEQRF IHGHRGGSGS 

        70         80         90        100        110        120 
GSGGSGKASD PAGGGPNHHA PQLSGDSALP LYSLGPGERA HSTCGTKVFP ERSGSGSASG 

       130        140        150        160        170        180 
SGGGGDLGFL HLDCAPSNSD FFLNGGYSYR GVIFPTLRNS FKSRDLERLY QRYFLGQRRK 

       190        200        210        220        230        240 
SEVVMNVLDV LTKLTLLVLH LSLASAPMDP LKGILLGFFT GIEVVICALV VVRKDTTSHT 

       250        260        270        280        290        300 
YLQYSGVVTW VAMTTQILAA GLGYGLLGDG IGYVLFTLFA TYSMLPLPLT WAILAGLGTS 

       310        320        330        340        350        360 
LLQVILQVVI PRLAVISINQ VVAQAVLFMC MNTAGIFISY LSDRAQRQAF LETRRCVEAR 

       370        380        390        400        410        420 
LRLETENQRQ ERLVLSVLPR FVVLEMINDM TNVEDEHLQH QFHRIYIHRY ENVSILFADV 

       430        440        450        460        470        480 
KGFTNLSTTL SAQELVRMLN ELFARFDRLA HEHHCLRIKI LGDCYYCVSG LPEPRQDHAH 

       490        500        510        520        530        540 
CCVEMGLSMI KTIRYVRSRT KHDVDMRIGI HSGSVLCGVL GLRKWQFDVW SWDVDIANKL 

       550        560        570        580        590        600 
ESGGIPGRIH ISKATLDCLN GDYNVEEGHG KERNEFLRKH NIETYLIKQP EDSLLSLPED 

       610        620        630        640        650        660 
IVKESVSSSD RRNSGATFTE GSWSPELPFD NIVGKQNTLA ALTRNSINLL PNHLAQALHV 

       670        680        690        700        710        720 
QSGPEEINKR IEHTIDLRSG DKLRREHIKP FSLMFKDSSL EHKYSQMRDE VFKSNLVCAF 

       730        740        750        760        770        780 
IVLLFITAIQ SLLPSSRVMP MTIQFSILIM LHSALVLITT AEDYKCLPLI LRKTCCWINE 

       790        800        810        820        830        840 
TYLARNVIIF ASILINFLGA ILNILWCDFD KSIPLKNLTF NSSAVFTDIC SYPEYFVFTG 

       850        860        870        880        890        900 
VLAMVTCAVF LRLNSVLKLA VLLIMIAIYA LLTETVYAGL FLRYDNLNHS GEDFLGTKEV 

       910        920        930        940        950        960 
SLLLMAMFLL AVFYHGQQLE YTARLDFLWR VQAKEEINEM KELREHNENM LRNILPSHVA 

       970        980        990       1000       1010       1020 
RHFLEKDRDN EELYSQSYDA VGVMFASIPG FADFYSQTEM NNQGVECLRL LNEIIADFDE 

      1030       1040       1050       1060       1070       1080 
LLGEDRFQDI EKIKTIGSTY MAVSGLSPEK QQCEDKWGHL CALADFSLAL TESIQEINKH 

      1090       1100       1110       1120       1130       1140 
SFNNFELRIG ISHGSVVAGV IGAKKPQYDI WGKTVNLASR MDSTGVSGRI QVPEETYLIL 

      1150       1160       1170       1180       1190       1200 
KDQGFAFDYR GEIYVKGISE QEGKIKTYFL LGRVQPNPFI LPPRRLPGQY SLAAVVLGLV 

      1210       1220       1230       1240       1250 
QSLNRQRQKQ LLNENNNTGI IKGHYNRRTL LSPSGTEPGA QAEGTDKSDL P

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the human type VIII adenylyl cyclase." Defer N., Marinx O., Stengel D., Danisova A., Iourgenko V., Matsuoka I., Caput D., Hanoune J. FEBS Lett. 351:109-113(1994) [PubMed: 8076676] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain stem.
[2]	"Sequence of a human brain adenylyl cyclase partial cDNA: evidence for a consensus cyclase specific domain." Parma J., Stengel D., Gannage M.H., Poyard M., Barouki R., Hanoune J. Biochem. Biophys. Res. Commun. 179:455-462(1991) [PubMed: 1715695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 577-1251. Tissue: Brain.
[3]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-881.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	Z35309 mRNA. Translation: CAA84552.1. M83533 mRNA. Translation: AAA35523.2.
IPI	IPI00027356.
PIR	PQ0227. S48687.
RefSeq	NP_001106.1.
UniGene	Hs.591859
3D structure databases
HSSP	HSSP built from PDB template 1CUL based on UniProtKB P30803.
ModBase	Search...
Protein-protein interaction databases
STRING	P40145.
PTM databases
PhosphoSite	P40145.
Proteomic databases
PRIDE	P40145.
Genome annotation databases
Ensembl	ENST00000286355; ENSP00000286355; ENSG00000155897; Homo sapiens. [Genome view] ENST00000377928; ENSP00000367161; ENSG00000155897; Homo sapiens. [Genome view]
GeneID	114.
KEGG	hsa:114.
UCSC	uc003ytd.2. human.
Organism-specific databases
CTD	114.
GeneCards	GC08M131861. GC08M131862.
H-InvDB	HIX0034375.
HGNC	HGNC:239. ADCY8.
HPA	CAB018652. HPA024291.
MIM	103070. gene.
PharmGKB	PA29.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P40145.
HOVERGEN	P40145.
OMA	HNITIST.
Enzyme and pathway databases
BRENDA	4.6.1.1. 247.
Pathway_Interaction_DB	endothelinpathway. Endothelins. lysophospholipid_pathway. LPA receptor mediated events. lpa4_pathway. LPA4-mediated signaling events.
Reactome	REACT_11061. Signalling by NGF. REACT_14797. Signaling by GPCR. REACT_1505. Integration of energy metabolism. REACT_15295. Opioid Signalling. REACT_15380. Diabetes pathways.
Gene expression databases
ArrayExpress	P40145.
Bgee	P40145.
CleanEx	HS_ADCY8.
Genevestigator	P40145.
GermOnline	ENSG00000155897. Homo sapiens.
Family and domain databases
InterPro	IPR001054. A/G_cyclase. IPR018297. A/G_cyclase_CS. IPR009398. Aden_cycl-like. [Graphical view]
Gene3D	G3DSA:3.30.70.1230. A/G_cyclase. 2 hits.
Pfam	PF06327. DUF1053. 1 hit. PF00211. Guanylate_cyc. 2 hits. [Graphical view]
SMART	SM00044. CYCc. 2 hits. [Graphical view]
PROSITE	PS00452. GUANYLATE_CYCLASE_1. 2 hits. PS50125. GUANYLATE_CYCLASE_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	441.
SOURCE	Search...

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Entry information

Entry name

ADCY8_HUMAN

Accession

Primary (citable) accession number: P40145

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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

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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 and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents