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O88444 (ADCY1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylate cyclase type 1
EC=4.6.1.1
Alternative name(s):
ATP pyrophosphate-lyase 1
Adenylate cyclase type I
Adenylyl cyclase 1
Ca(2+)/calmodulin-activated adenylyl cyclase
Gene names
Name:Adcy1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1118 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning 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. Inhibited by the G protein beta and gamma subunit complex By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

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

Contains 2 guanylate cyclase domains.

Ontologies

Keywords
   Biological processcAMP biosynthesis
   Cellular componentMembrane
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Calmodulin-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLyase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of adenylate cyclase activity

Traceable author statement Ref.2. Source: MGI

axonogenesis

Inferred from mutant phenotype PubMed 17229090. Source: MGI

circadian rhythm

Inferred from electronic annotation. Source: Compara

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

long-term memory

Inferred from genetic interaction PubMed 10482244. Source: MGI

response to drug

Inferred from electronic annotation. Source: Compara

response to lithium ion

Inferred from electronic annotation. Source: Compara

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: Compara

plasma membrane

Traceable author statement Ref.2. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate cyclase activity

Inferred from genetic interaction PubMed 10482244. Source: MGI

calcium- and calmodulin-responsive adenylate cyclase activity

Inferred from electronic annotation. Source: Compara

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11181118Adenylate cyclase type 1
PRO_0000195683

Regions

Topological domain1 – 6262Cytoplasmic Potential
Transmembrane63 – 8321Helical; Potential
Transmembrane87 – 10721Helical; Potential
Transmembrane124 – 14421Helical; Potential
Transmembrane157 – 17721Helical; Potential
Transmembrane182 – 20221Helical; Potential
Transmembrane213 – 23321Helical; Potential
Topological domain234 – 609376Cytoplasmic Potential
Transmembrane610 – 63021Helical; Potential
Transmembrane634 – 65421Helical; Potential
Transmembrane673 – 69321Helical; Potential
Transmembrane724 – 74421Helical; Potential
Transmembrane752 – 77221Helical; Potential
Transmembrane774 – 79320Helical; Potential
Topological domain794 – 1118325Cytoplasmic Potential
Region492 – 51928Interaction with calmodulin By similarity
Region1023 – 104624Interaction with calmodulin By similarity

Sites

Metal binding3071Magnesium 1 By similarity
Metal binding3071Magnesium 2 By similarity
Metal binding3081Magnesium 2; via carbonyl oxygen By similarity
Metal binding3511Magnesium 1 By similarity
Metal binding3511Magnesium 2 By similarity

Amino acid modifications

Glycosylation7031N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict147 – 1559SSAGGAMGS → ALQEAQWAR in AAC29478. Ref.2
Sequence conflict2341T → A in AAC29478. Ref.2
Sequence conflict2701L → M in AAC29478. Ref.2
Sequence conflict3191T → K in AAC29478. Ref.2
Sequence conflict4661R → K in AAC29478. Ref.2
Sequence conflict5231F → I in AAC29478. Ref.2
Sequence conflict5421S → T in AAC29478. Ref.2
Sequence conflict5491S → T in AAC29478. Ref.2
Sequence conflict5701R → L in AAC29478. Ref.2
Sequence conflict5981Q → R in AAC29478. Ref.2
Sequence conflict6921G → V in AAC29478. Ref.2
Sequence conflict6971A → S in AAC29478. Ref.2
Sequence conflict7071V → L in AAC29478. Ref.2
Sequence conflict7131G → C in AAC29478. Ref.2
Sequence conflict720 – 7212AL → GP in AAC29478. Ref.2
Sequence conflict774 – 7763VGG → AMGA in AAC29478. Ref.2
Sequence conflict867 – 8693GVM → AVL in AAC29478. Ref.2
Sequence conflict9381R → K in AAC29478. Ref.2
Sequence conflict9911R → C in AAC29478. Ref.2
Sequence conflict10201T → I in AAC29478. Ref.2
Sequence conflict10301C → S in AAC29478. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O88444 [UniParc].

Last modified April 12, 2005. Version 2.
Checksum: CEFAFF3940B22277

FASTA1,118123,373
        10         20         30         40         50         60 
MAGAPRGQGG GGGAGEPGGA ERAAGPGGRR GFRACGEEFA CPELEALFRG YTLRLEQAAT 

        70         80         90        100        110        120 
LKALAVLSLL AGALALAELL GAPGPAPGLA KGSHPVHCIL FLALFVVTNV RSLQVSQLQQ 

       130        140        150        160        170        180 
VGQLALFFSL TFALLCCPFA LGGPARSSAG GAMGSTVAEQ GVWQLLLVTF VSYALLPVRS 

       190        200        210        220        230        240 
LLAIGFGLVV AASHLLVTAA LVPAKRPRLW RTLGANALLF FGVNMYGVFV RILTERSQRK 

       250        260        270        280        290        300 
AFLQARNCIE DRLRLEDENE KQERLLMSLL PRNVAMEMKE DFLKPPERIF HKIYIQRHDN 

       310        320        330        340        350        360 
VSILFADIVG FTGLASQCTA QELVKLLNEL FGKFDELATE NHCRRIKILG DCYYCVSGLT 

       370        380        390        400        410        420 
QPKTDHAHCC VEMGLDMIDT ITSVAEATEV DLNMRVGLHT GRVLCGVLGL RKWQYDVWSN 

       430        440        450        460        470        480 
DVTLANVMEA AGLPGKVHIT KTTLACLNGD YEVEPGHGHE RNTFLRTHNI ETFFIVPSHR 

       490        500        510        520        530        540 
RKIFPGLILS DIKPAKRMKF KTVCYLLVQL MHCRKMFKAE IPFSNVMTCE DDDKRRALRT 

       550        560        570        580        590        600 
ASEKLRNRSS FSTNVVYTTP GTRVNRYISR LLEARQTELE MADLNFFTLK YKHVEREQKY 

       610        620        630        640        650        660 
HQLQDEYFTS AVVLALILAA LFGLIYLLVI PQSVAVLLLL VFSICFLVAC TLYLHITRVQ 

       670        680        690        700        710        720 
CFPGCLTIQI RTALCVFIVV LIYSVAQGCV VGCLPWAWSS QSNSSLVVLA AGGRRTVLPA 

       730        740        750        760        770        780 
LPCESAHHAL LCCLVGTLPL AIFLRVSSLP KMILLSGLTT SYILVLELSG YTKVGGGALS 

       790        800        810        820        830        840 
GRSYEPIMAI LLFSCTLALH ARQVDVRLRL DYLWAAQAEE ERDDMERVKL DNKRILFNLL 

       850        860        870        880        890        900 
PAHVAQHFLM SNPRNMDLYY QSYSQVGVMF ASIPNFNDFY IELDGNNMGV ECLRLLNEII 

       910        920        930        940        950        960 
ADFDELMDKD FYKDLEKIKT IGSTYMAAVG LAPTAGTRAK KSISSHLCTL ADFAIDMFDV 

       970        980        990       1000       1010       1020 
LDEINYQSYN DFVLRVGINV GPVVAGVIGA RRPQYDIWGN TVNVASRMDS TGVQGRIQVT 

      1030       1040       1050       1060       1070       1080 
EEVHRLLKRC SYQFVCRGKV SVKGKGEMLT YFLEGRTDGN SSHGRTFRLE RRMCPYGRGG 

      1090       1100       1110 
GQARRPPLCP AAGPPVRPGL PPAPTSQYLS STAAGKEA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL669838 Genomic DNA. Translation: CAI25155.1.
AF053980 mRNA. Translation: AAC29478.1.
IPIIPI00130949.
RefSeqNP_033752.1. NM_009622.1.
UniGeneMm.259733.

3D structure databases

ProteinModelPortalO88444.
SMRO88444. Positions 289-476, 859-1053.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000020706.

PTM databases

PhosphoSiteO88444.

Proteomic databases

PaxDbO88444.
PRIDEO88444.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431.
GeneID432530.
KEGGmmu:432530.
UCSCuc007hzf.1. mouse.

Organism-specific databases

CTD107.
MGIMGI:99677. Adcy1.

Phylogenomic databases

eggNOGCOG2114.
GeneTreeENSGT00680000099709.
HOGENOMHOG000006941.
HOVERGENHBG050458.
InParanoidO88444.
KOK08041.
OMACLPWAWS.
OrthoDBEOG4TQM8C.

Gene expression databases

ArrayExpressO88444.
BgeeO88444.
CleanExMM_ADCY1.
GenevestigatorO88444.
GermOnlineENSMUSG00000020431. Mus musculus.

Family and domain databases

Gene3D3.30.70.1230. 2 hits.
InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
[Graphical view]
PfamPF00211. Guanylate_cyc. 2 hits.
[Graphical view]
SMARTSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMSSF55073. A/G_cyclase. 2 hits.
PROSITEPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

BindingDBO88444.
ChEMBLCHEMBL3532.
ChiTaRSADCY1. mouse.
NextBio407738.
SOURCESearch...

Entry information

Entry nameADCY1_MOUSE
AccessionPrimary (citable) accession number: O88444
Secondary accession number(s): Q5SS89
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: April 12, 2005
Last modified: April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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