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Reviewed, UniProtKB/Swiss-Prot Q08462 (ADCY2_HUMAN)

Last modified November 25, 2008. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Adenylate cyclase type 2
    EC=4.6.1.1
Alternative name(s):
    Adenylate cyclase type II
    ATP pyrophosphate-lyase 2
    Adenylyl cyclase 2
Gene names
Name: ADCY2
Synonyms: KIAA1060
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1091 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in brain.

Sequence similarities

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

Contains 2 guanylate cyclase domains.

Ontologies

Keywords

   Biological processcAMP biosynthesis
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Transmembrane
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   PTMGlycoprotein

Gene Ontology (GO)

   Biological processcAMP biosynthetic process

Non-traceable author statement. Source: UniProtKB

intracellular signaling cascade

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Non-traceable author statement. Source: UniProtKB

   Molecular functionadenylate cyclase activity Ref.4

Non-traceable author statement. Source: UniProtKB

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10911091Adenylate cyclase type 2
PRO_0000195684

Regions

Topological domain1 – 4545Cytoplasmic Potential
Transmembrane46 – 6621 Potential
Transmembrane76 – 9621 Potential
Transmembrane108 – 12821 Potential
Transmembrane133 – 15321 Potential
Transmembrane159 – 17921 Potential
Transmembrane187 – 20721 Potential
Topological domain208 – 601394Cytoplasmic Potential
Transmembrane602 – 62221 Potential
Transmembrane628 – 65225 Potential
Transmembrane680 – 70122 Potential
Transmembrane734 – 75522 Potential
Transmembrane763 – 78018 Potential
Transmembrane801 – 82121 Potential
Topological domain822 – 1091270Cytoplasmic Potential

Sites

Metal binding2951Magnesium 1 By similarity
Metal binding2951Magnesium 2 By similarity
Metal binding2961Magnesium 2; via carbonyl oxygen By similarity
Metal binding3391Magnesium 1 By similarity
Metal binding3391Magnesium 2 By similarity

Amino acid modifications

Glycosylation7131N-linked (GlcNAc...) Potential
Glycosylation7161N-linked (GlcNAc...) Potential

Natural variations

Natural variant1471V → L: dbSNP rs13166360.
VAR_029012

Experimental info

Sequence conflict188 – 20720VWQIL…LAGAY → GLADPGQCDHFHLWEPGXTN in AAP97285. Ref.1
Sequence conflict6751R → Q in CAA52282 and AAA64923. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q08462-1 [UniParc].

Last modified November 28, 2006. Version 5.
Checksum: 41FD8BC607C075D1

FASTA1,091123,603
        10         20         30         40         50         60 
MWQEAMRRRR YLRDRSEEAA GGGDGLPRSR DWLYESYYCM SQQHPLIVFL LLIVMGSCLA 

        70         80         90        100        110        120 
LLAVFFALGL EVEDHVAFLI TVPTALAIFF AIFILVCIES VFKKLLRLFS LVIWICLVAM 

       130        140        150        160        170        180 
GYLFMCFGGT VSPWDQVSFF LFIIFVVYTM LPFNMRDAII ASVLTSSSHT IVLSVCLSAT 

       190        200        210        220        230        240 
PGGKEHLVWQ ILANVIIFIC GNLAGAYHKH LMELALQQTY QDTCNCIKSR IKLEFEKRQQ 

       250        260        270        280        290        300 
ERLLLSLLPA HIAMEMKAEI IQRLQGPKAG QMENTNNFHN LYVKRHTNVS ILYADIVGFT 

       310        320        330        340        350        360 
RLASDCSPGE LVHMLNELFG KFDQIAKENE CMRIKILGDC YYCVSGLPIS LPNHAKNCVK 

       370        380        390        400        410        420 
MGLDMCEAIK KVRDATGVDI NMRVGVHSGN VLCGVIGLQK WQYDVWSHDV TLANHMEAGG 

       430        440        450        460        470        480 
VPGRVHISSV TLEHLNGAYK VEEGDGDIRD PYLKQHLVKT YFVINPKGER RSPQHLFRPR 

       490        500        510        520        530        540 
HTLDGAKMRA SVRMTRYLES WGAAKPFAHL HHRDSMTTEN GKISTTDVPM GQHNFQNRTL 

       550        560        570        580        590        600 
RTKSQKKRFE EELNERMIQA IDGINAQKQW LKSEDIQRIS LLFYNKVLEK EYRATALPAF 

       610        620        630        640        650        660 
KYYVTCACLI FFCIFIVQIL VLPKTSVLGI SFGAAFLLLA FILFVCFAGQ LLQCSKKASP 

       670        680        690        700        710        720 
LLMWLLKSSG IIANRPWPRI SLTIITTAII LMMAVFNMFF LSDSEETIPP TANTTNTSFS 

       730        740        750        760        770        780 
ASNNQVAILR AQNLFFLPYF IYSCILGLIS CSVFLRVNYE LKMLIMMVAL VGYNTILLHT 

       790        800        810        820        830        840 
HAHVLGDYSQ VLFERPGIWK DLKTMGSVSL SIFFITLLVL GRQNEYYCRL DFLWKNKFKK 

       850        860        870        880        890        900 
EREEIETMEN LNRVLLENVL PAHVAEHFLA RSLKNEELYH QSYDCVCVMF ASIPDFKEFY 

       910        920        930        940        950        960 
TESDVNKEGL ECLRLLNEII ADFDDLLSKP KFSGVEKIKT IGSTYMAATG LSAVPSQEHS 

       970        980        990       1000       1010       1020 
QEPERQYMHI GTMVEFAFAL VGKLDAINKH SFNDFKLRVG INHGPVIAGV IGAQKPQYDI 

      1030       1040       1050       1060       1070       1080 
WGNTVNVASR MDSTGVLDKI QVTEETSLVL QTLGYTCTCR GIINVKGKGD LKTYFVNTEM 

      1090 
SRSLSQSNVA S 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of human adenylyl cyclase gene."
Guo J.H., Yu L.
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-147.
[3]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed: 10470851] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-1091.
Tissue: Brain.
[4]"Different chromosomal localization of two adenylyl cyclase genes expressed in human brain."
Stengel D., Parma J., Gannage M.-H., Roeckel N., Mattei M.-G., Barouki R., Hanoune J.
Hum. Genet. 90:126-130(1992) [PubMed: 1427768] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 616-1091.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF410885 mRNA. Translation: AAP97285.1.
BC111743 mRNA. Translation: AAI11744.1.
AB028983 mRNA. Translation: BAA83012.1.
X74210 mRNA. Translation: CAA52282.1.
L21993 mRNA. Translation: AAA64923.1.
PIRI37136.
RefSeqNP_065433.2.
UniGeneHs.481545

3D structure databases

HSSPHSSP built from PDB template 1AB8 based on UniProtKB P26769.
SMRQ08462. Positions 879-1078.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:422N.

PTM databases

PhosphoSiteQ08462.

Genome annotation databases

EnsemblENSG00000078295. Homo sapiens. [Contig view]
GeneID108.
KEGGhsa:108.

Organism-specific databases

HGNCHGNC:233. ADCY2.
MIM103071. gene.
PharmGKBPA24561.
HUGESearch...
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ08462.

Gene expression databases

ArrayExpressQ08462.
CleanExHS_ADCY2.
GermOnlineENSG00000078295. Homo sapiens.

Family and domain databases

InterProIPR001054. A/G_cyclase.
IPR009398. Aden_cycl_like.
[Graphical view]
Gene3DG3DSA:3.30.70.1230. A/G_cyclase. 2 hits.
PfamPF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
SMARTSM00044. CYCc. 2 hits.
[Graphical view]
PROSITEPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio419.
SOURCESearch...

Entry information

Entry nameADCY2_HUMAN
AccessionPrimary (citable) accession number: Q08462
Secondary accession number(s): Q2NKL8, Q9UPU2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 28, 2006
Last modified: November 25, 2008
This is version 84 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

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