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Reviewed, UniProtKB/Swiss-Prot Q29450 (ADCY7_BOVIN)

Last modified January 19, 2010. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 7
    EC=4.6.1.1
Alternative name(s):
    Adenylate cyclase type VII
    ATP pyrophosphate-lyase 7
    Adenylyl cyclase 7
Gene names
Name: ADCY7
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1078 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Found exclusively in the retinal pigment epithelium.

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
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLyase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processcAMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signaling cascade

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate cyclase activity

Inferred from electronic annotation. Source: EC

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 – 10781078Adenylate cyclase type 7
PRO_0000195702

Regions

Topological domain1 – 3333Cytoplasmic Potential
Transmembrane34 – 5421 Potential
Transmembrane63 – 8321 Potential
Transmembrane95 – 12026 Potential
Transmembrane125 – 14521 Potential
Transmembrane150 – 17021 Potential
Transmembrane176 – 19621 Potential
Topological domain197 – 594398Cytoplasmic Potential
Transmembrane595 – 61521 Potential
Transmembrane620 – 64021 Potential
Transmembrane669 – 68820 Potential
Transmembrane718 – 73720 Potential
Transmembrane746 – 77328 Potential
Transmembrane792 – 81221 Potential
Topological domain813 – 1078266Cytoplasmic Potential

Sites

Metal binding2841Magnesium 1 By similarity
Metal binding2841Magnesium 2 By similarity
Metal binding2851Magnesium 2; via carbonyl oxygen By similarity
Metal binding3281Magnesium 1 By similarity
Metal binding3281Magnesium 2 By similarity

Amino acid modifications

Glycosylation7011N-linked (GlcNAc...) Potential
Glycosylation7761N-linked (GlcNAc...) Potential
Glycosylation7811N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q29450-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 50E89BF08E37FCBB

FASTA1,078120,820
        10         20         30         40         50         60 
MPAKGRYFLN EGEEGPDQDA LYEKYRLTSQ HGPLLLMLLL VAIAACTTLI VITFSYGDPS 

        70         80         90        100        110        120 
RHRAVLGTAF FTLAMFVLLY ALVYVECLDR RGLRISALLI WGCLVTLGYV LVFDFDSPRK 

       130        140        150        160        170        180 
DTLCLWGRCP SSSFVVFVVY TLLPFSMWGA VTAGLVSSIS HLLVLAMHQE DFTSPVGLKL 

       190        200        210        220        230        240 
LATAVVFVCG NLTGAFHKHH MQDASHDLFT YTVKCIQIRR KLRIEKRQQE NLLLSVLPAH 

       250        260        270        280        290        300 
ISMGMKLAII ERLKERGDRR YLPDNNFHNL YVKRHQNVSI LYADIVGFTR LASDCSPKEL 

       310        320        330        340        350        360 
VVVLNELFGK FDQIAKANEC MRIKILGDCY YCVSGLPVSL PNHARNCVKM GLDMCEAIKQ 

       370        380        390        400        410        420 
VREATGVDIS MRVGIHSGNV LCGVIGLRKW QYDVWSHDVS LANRMEAAGV PGRVHITEAT 

       430        440        450        460        470        480 
LKHLDKAYEV EDGHGQQRDP YLKEMNIRTY LVIDPRSQQP PQPSQHNSKN KGNATLKMRA 

       490        500        510        520        530        540 
SVRMTRYLES WGAARPFAHL NQRESVSSSE TLVSHGRRPK AVPLRRHRTP DRSASPKGRS 

       550        560        570        580        590        600 
EDDSYDDEML SAIEGLSSTR PCCSKSDDFS TFGSIFLEKG FEREYRLAPI PRVRYYFACA 

       610        620        630        640        650        660 
SLVFVCILLI HVLLLYSMKT LGVSFGLVAC VLGLVLGLCF ADVFLRCCPA LGKLRAIAES 

       670        680        690        700        710        720 
VETQPLLRVS LAILTIGSLL VIAVVNLPLM PFRDRGLTAG NETGLRAVSG WEMSPCYLLP 

       730        740        750        760        770        780 
YYTCSCILAF IACSVFLRMS LELKVVLLTV ALVAYLVLFN VYPSWQWDCC GHSLGNLTGT 

       790        800        810        820        830        840 
NGTLSSSSCS WHLKTMTNFY LVLFYTTLIM LSRQIDYYCR LDCLWKKKFK KEHEEFETME 

       850        860        870        880        890        900 
NVNRLLLENV LPAHVAAHFI GDKLNEDWYH QSYDCVCVMF ASVPDFKVFY TECDVNKEGL 

       910        920        930        940        950        960 
ECLRLLNEII ADFDELLLKP KFSGVEKIKT IGSTYMAAAG LSVPSGPENQ DLERQHAHIG 

       970        980        990       1000       1010       1020 
IMVEFSTALM SKLDGINRHS FNSFRLRVGI NHGPVIAGVI GARKPQYDIW GNTVNVASRM 

      1030       1040       1050       1060       1070 
ESTGELGKIQ VTEETCTILQ GLGYSCECRG LIDVKGKGEL RTYFVCTDTA KFQGLGLN 

« Hide

References

[1]"Cloning and expression of a bovine adenylyl cyclase type VII specific to the retinal pigment epithelium."
Voelkel H., Beitz E., Klumpp S., Schultz J.E.
FEBS Lett. 378:245-249(1996) [PubMed: 8557110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49806 mRNA. Translation: CAA89894.1. Different initiation.
IPIIPI00712783.
RefSeqNP_776655.1.
UniGeneBt.1165

3D structure databases

SMRQ29450. Positions 264-453, 869-1067.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ29450.

Genome annotation databases

EnsemblENSBTAT00000008153; ENSBTAP00000008153; ENSBTAG00000006208; Bos taurus. [Genome view]
GeneID281603.
KEGGbta:281603.

Organism-specific databases

CTD281603.

Phylogenomic databases

eggNOGmaNOG12842.
HOVERGENQ29450.
InParanoidQ29450.

Enzyme and pathway databases

BRENDA4.6.1.1. 251.

Family and domain databases

InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
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. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADCY7_BOVIN
AccessionPrimary (citable) accession number: Q29450
Secondary accession number(s): O02856
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 19, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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