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P19754 (ADCY1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length1134 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

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.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Brain.

Sequence similarities

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

Contains 2 guanylate cyclase domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11341134Adenylate cyclase type 1
PRO_0000195681

Regions

Topological domain1 – 6565Cytoplasmic Potential
Transmembrane66 – 8621Helical; Potential
Transmembrane90 – 11021Helical; Potential
Transmembrane127 – 14721Helical; Potential
Transmembrane154 – 17421Helical; Potential
Transmembrane184 – 20421Helical; Potential
Transmembrane216 – 23621Helical; Potential
Topological domain237 – 612376Cytoplasmic Potential
Transmembrane613 – 63321Helical; Potential
Transmembrane637 – 65721Helical; Potential
Transmembrane676 – 69621Helical; Potential
Topological domain697 – 72630Extracellular Potential
Transmembrane727 – 74721Helical; Potential
Transmembrane755 – 77521Helical; Potential
Transmembrane777 – 79721Helical; Potential
Topological domain798 – 1134337Cytoplasmic Potential
Domain305 – 432128Guanylate cyclase 1
Domain871 – 1013143Guanylate cyclase 2
Region495 – 52228Interaction with calmodulin By similarity
Region1027 – 105024Interaction with calmodulin By similarity
Compositional bias3 – 3432Gly-rich

Sites

Metal binding3101Magnesium 1 By similarity
Metal binding3101Magnesium 2 By similarity
Metal binding3111Magnesium 2; via carbonyl oxygen By similarity
Metal binding3541Magnesium 1 By similarity
Metal binding3541Magnesium 2 By similarity

Amino acid modifications

Glycosylation7061N-linked (GlcNAc...) Potential

Secondary structure

1 ..................................................... 1134
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19754 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: CC4A10BCE224DFF3

FASTA1,134123,979
        10         20         30         40         50         60 
MAGAPRGRGG GGGGGGAGES GGAERAAGPG GRRGLRACDE EFACPELEAL FRGYTLRLEQ 

        70         80         90        100        110        120 
AATLKALAVL SLLAGALALA ELLGAPGPAP GLAKGSHPVH CVLFLALLVV TNVRSLQVPQ 

       130        140        150        160        170        180 
LQQVGQLALL FSLTFALLCC PFALGGPAGA HAGAAAVPAT ADQGVWQLLL VTFVSYALLP 

       190        200        210        220        230        240 
VRSLLAIGFG LVVAASHLLV TATLVPAKRP RLWRTLGANA LLFLGVNVYG IFVRILAERA 

       250        260        270        280        290        300 
QRKAFLQARN CIEDRLRLED ENEKQERLLM SLLPRNVAME MKEDFLKPPE RIFHKIYIQR 

       310        320        330        340        350        360 
HDNVSILFAD IVGFTGLASQ CTAQELVKLL NELFGKFDEL ATENHCRRIK ILGDCYYCVS 

       370        380        390        400        410        420 
GLTQPKTDHA HCCVEMGLDM IDTITSVAEA TEVDLNMRVG LHTGRVLCGV LGLRKWQYDV 

       430        440        450        460        470        480 
WSNDVTLANV MEAAGLPGKV HITKTTLACL NGDYEVEPGH GHERNSFLKT HNIETFFIVP 

       490        500        510        520        530        540 
SHRRKIFPGL ILSDIKPAKR MKFKTVCYLL VQLMHCRKMF KAEIPFSNVM TCEDDDKRRA 

       550        560        570        580        590        600 
LRTASEKLRN RSSFSTNVVQ TTPGTRVNRY IGRLLEARQM ELEMADLNFF TLKYKQAERE 

       610        620        630        640        650        660 
RKYHQLQDEY FTSAVVLALI LAALFGLVYL LIIPQSVAVL LLLVFCICFL VACVLYLHIT 

       670        680        690        700        710        720 
RVQCFPGCLT IQIRTVLCIF IVVLIYSVAQ GCVVGCLPWS WSSSPNGSLV VLSSGGRDPV 

       730        740        750        760        770        780 
LPVPPCESAP HALLCGLVGT LPLAIFLRVS SLPKMILLAV LTTSYILVLE LSGYTKAMGA 

       790        800        810        820        830        840 
GAISGRSFEP IMAILLFSCT LALHARQVDV KLRLDYLWAA QAEEERDDME KVKLDNKRIL 

       850        860        870        880        890        900 
FNLLPAHVAQ HFLMSNPRNM DLYYQSYSQV GVMFASIPNF NDFYIELDGN NMGVECLRLL 

       910        920        930        940        950        960 
NEIIADFDEL MDKDFYKDLE KIKTIGSTYM AAVGLAPTAG TKAKKCISSH LSTLADFAIE 

       970        980        990       1000       1010       1020 
MFDVLDEINY QSYNDFVLRV GINVGPVVAG VIGARRPQYD IWGNTVNVAS RMDSTGVQGR 

      1030       1040       1050       1060       1070       1080 
IQVTEEVHRL LRRGSYRFVC RGKVSVKGKG EMLTYFLEGR TDGNGSQTRS LNSERKMYPF 

      1090       1100       1110       1120       1130 
GRAGLQTRLA AGHPPVPPAA GLPVGAGPGA LQGSGLAPGP PGQHLPPGAS GKEA

« Hide

References

[1]"Adenylyl cyclase amino acid sequence: possible channel- or transporter-like structure."
Krupinski J., Coussen F., Bakalyar H.A., Tang W.-J., Feinstein P.G., Orth K., Slaughter C., Reed R.R., Gilman A.G.
Science 244:1558-1564(1989) [PubMed: 2472670] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.
[2]"Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and mutational analysis."
Liu Y., Ruoho A.E., Rao V.D., Hurley J.H.
Proc. Natl. Acad. Sci. U.S.A. 94:13414-13419(1997) [PubMed: 9391039] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 295-450; 861-936 AND 950-1045.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M25579 mRNA. Translation: AAA79957.1.
IPIIPI00710035.
PIRA41350.
RefSeqNP_776654.1. NM_174229.2.
UniGeneBt.517.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWKmodel-A295-1058[»]
ProteinModelPortalP19754.
SMRP19754. Positions 290-479, 862-1057.
ModBaseSearch...

Protein-protein interaction databases

STRINGP19754.

Proteomic databases

PRIDEP19754.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281601.
KEGGbta:281601.

Organism-specific databases

CTD107.

Phylogenomic databases

eggNOGmaNOG13401.
GeneTreeENSGT00590000082802.
HOVERGENHBG050458.
InParanoidP19754.
OrthoDBEOG4TQM8C.

Enzyme and pathway databases

BRENDA4.6.1.1. 908.

Family and domain databases

InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
[Graphical view]
Gene3DG3DSA:3.30.70.1230. A/G_cyclase. 2 hits.
KOK08041.
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...

Entry information

Entry nameADCY1_BOVIN
AccessionPrimary (citable) accession number: P19754
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 16, 2011
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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