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Protein

Adenylate cyclase type 7

Gene

ADCY7

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

This is a membrane-bound, calcium-inhibitable adenylyl cyclase.

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi284 – 2841Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi284 – 2841Magnesium 2; catalyticPROSITE-ProRule annotation
Metal bindingi285 – 2851Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation
Metal bindingi328 – 3281Magnesium 1; catalyticPROSITE-ProRule annotation
Metal bindingi328 – 3281Magnesium 2; catalyticPROSITE-ProRule annotation
Binding sitei372 – 3721ATPBy similarity
Binding sitei929 – 9291ATPBy similarity
Binding sitei1055 – 10551ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi284 – 2896ATPBy similarity
Nucleotide bindingi326 – 3283ATPBy similarity
Nucleotide bindingi1008 – 10103ATPBy similarity
Nucleotide bindingi1015 – 10195ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cAMP biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 7 (EC:4.6.1.1)
Alternative name(s):
ATP pyrophosphate-lyase 7
Adenylate cyclase type VII
Adenylyl cyclase 7
Gene namesi
Name:ADCY7
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333CytoplasmicSequence analysisAdd
BLAST
Transmembranei34 – 5421HelicalSequence analysisAdd
BLAST
Transmembranei63 – 8321HelicalSequence analysisAdd
BLAST
Transmembranei95 – 12026HelicalSequence analysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence analysisAdd
BLAST
Transmembranei150 – 17021HelicalSequence analysisAdd
BLAST
Transmembranei176 – 19621HelicalSequence analysisAdd
BLAST
Topological domaini197 – 594398CytoplasmicSequence analysisAdd
BLAST
Transmembranei595 – 61521HelicalSequence analysisAdd
BLAST
Transmembranei620 – 64021HelicalSequence analysisAdd
BLAST
Transmembranei669 – 68820HelicalSequence analysisAdd
BLAST
Transmembranei718 – 73720HelicalSequence analysisAdd
BLAST
Transmembranei746 – 77328HelicalSequence analysisAdd
BLAST
Transmembranei792 – 81221HelicalSequence analysisAdd
BLAST
Topological domaini813 – 1078266CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: GOC
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10781078Adenylate cyclase type 7PRO_0000195702Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi701 – 7011N-linked (GlcNAc...)Sequence analysis
Glycosylationi776 – 7761N-linked (GlcNAc...)Sequence analysis
Glycosylationi781 – 7811N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ29450.
PRIDEiQ29450.

Expressioni

Tissue specificityi

Found exclusively in the retinal pigment epithelium.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008153.

Structurei

3D structure databases

ProteinModelPortaliQ29450.
SMRiQ29450. Positions 264-453, 869-1067.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain.By similarity

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
Contains 2 guanylate cyclase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ29450.
KOiK08047.
OrthoDBiEOG76X5ZC.
TreeFamiTF313845.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q29450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAKGRYFLN EGEEGPDQDA LYEKYRLTSQ HGPLLLMLLL VAIAACTTLI
60 70 80 90 100
VITFSYGDPS RHRAVLGTAF FTLAMFVLLY ALVYVECLDR RGLRISALLI
110 120 130 140 150
WGCLVTLGYV LVFDFDSPRK DTLCLWGRCP SSSFVVFVVY TLLPFSMWGA
160 170 180 190 200
VTAGLVSSIS HLLVLAMHQE DFTSPVGLKL LATAVVFVCG NLTGAFHKHH
210 220 230 240 250
MQDASHDLFT YTVKCIQIRR KLRIEKRQQE NLLLSVLPAH ISMGMKLAII
260 270 280 290 300
ERLKERGDRR YLPDNNFHNL YVKRHQNVSI LYADIVGFTR LASDCSPKEL
310 320 330 340 350
VVVLNELFGK FDQIAKANEC MRIKILGDCY YCVSGLPVSL PNHARNCVKM
360 370 380 390 400
GLDMCEAIKQ VREATGVDIS MRVGIHSGNV LCGVIGLRKW QYDVWSHDVS
410 420 430 440 450
LANRMEAAGV PGRVHITEAT LKHLDKAYEV EDGHGQQRDP YLKEMNIRTY
460 470 480 490 500
LVIDPRSQQP PQPSQHNSKN KGNATLKMRA SVRMTRYLES WGAARPFAHL
510 520 530 540 550
NQRESVSSSE TLVSHGRRPK AVPLRRHRTP DRSASPKGRS EDDSYDDEML
560 570 580 590 600
SAIEGLSSTR PCCSKSDDFS TFGSIFLEKG FEREYRLAPI PRVRYYFACA
610 620 630 640 650
SLVFVCILLI HVLLLYSMKT LGVSFGLVAC VLGLVLGLCF ADVFLRCCPA
660 670 680 690 700
LGKLRAIAES VETQPLLRVS LAILTIGSLL VIAVVNLPLM PFRDRGLTAG
710 720 730 740 750
NETGLRAVSG WEMSPCYLLP YYTCSCILAF IACSVFLRMS LELKVVLLTV
760 770 780 790 800
ALVAYLVLFN VYPSWQWDCC GHSLGNLTGT NGTLSSSSCS WHLKTMTNFY
810 820 830 840 850
LVLFYTTLIM LSRQIDYYCR LDCLWKKKFK KEHEEFETME NVNRLLLENV
860 870 880 890 900
LPAHVAAHFI GDKLNEDWYH QSYDCVCVMF ASVPDFKVFY TECDVNKEGL
910 920 930 940 950
ECLRLLNEII ADFDELLLKP KFSGVEKIKT IGSTYMAAAG LSVPSGPENQ
960 970 980 990 1000
DLERQHAHIG IMVEFSTALM SKLDGINRHS FNSFRLRVGI NHGPVIAGVI
1010 1020 1030 1040 1050
GARKPQYDIW GNTVNVASRM ESTGELGKIQ VTEETCTILQ GLGYSCECRG
1060 1070
LIDVKGKGEL RTYFVCTDTA KFQGLGLN
Length:1,078
Mass (Da):120,820
Last modified:November 1, 1997 - v1
Checksum:i50E89BF08E37FCBB
GO

Sequence cautioni

The sequence CAA89894.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49806 mRNA. Translation: CAA89894.1. Different initiation.
RefSeqiNP_776655.1. NM_174230.2.
XP_005218501.1. XM_005218444.3.
UniGeneiBt.1165.

Genome annotation databases

GeneIDi281603.
KEGGibta:281603.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49806 mRNA. Translation: CAA89894.1. Different initiation.
RefSeqiNP_776655.1. NM_174230.2.
XP_005218501.1. XM_005218444.3.
UniGeneiBt.1165.

3D structure databases

ProteinModelPortaliQ29450.
SMRiQ29450. Positions 264-453, 869-1067.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008153.

Proteomic databases

PaxDbiQ29450.
PRIDEiQ29450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281603.
KEGGibta:281603.

Organism-specific databases

CTDi113.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiQ29450.
KOiK08047.
OrthoDBiEOG76X5ZC.
TreeFamiTF313845.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.

Entry informationi

Entry nameiADCY7_BOVIN
AccessioniPrimary (citable) accession number: Q29450
Secondary accession number(s): O02856
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.