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Protein

Adenylate cyclase type 4

Gene

Adcy4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.1 Publication

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).By similarity

Enzyme regulationi

Activated by forskolin. Insensitive to calcium/calmodulin. Stimulated by GNAS and by the G-protein beta and gamma subunit complex.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi278Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi278Magnesium 2; catalyticPROSITE-ProRule annotation1
Metal bindingi279Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi322Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi322Magnesium 2; catalyticPROSITE-ProRule annotation1
Binding sitei366ATPBy similarity1
Binding sitei914ATPBy similarity1
Binding sitei1041ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi278 – 283ATPBy similarity6
Nucleotide bindingi320 – 322ATPBy similarity3
Nucleotide bindingi994 – 996ATPBy similarity3
Nucleotide bindingi1001 – 1005ATPBy similarity5

GO - Molecular functioni

  • adenylate cyclase activity Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • G-protein beta/gamma-subunit complex binding Source: RGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cAMP biosynthesis

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 4 (EC:4.6.1.11 Publication)
Alternative name(s):
ATP pyrophosphate-lyase 4
Adenylate cyclase type IV
Adenylyl cyclase 4
Gene namesi
Name:Adcy4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2034. Adcy4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 28CytoplasmicSequence analysisAdd BLAST28
Transmembranei29 – 50HelicalSequence analysisAdd BLAST22
Transmembranei61 – 80HelicalSequence analysisAdd BLAST20
Transmembranei94 – 117HelicalSequence analysisAdd BLAST24
Transmembranei120 – 138HelicalSequence analysisAdd BLAST19
Transmembranei141 – 162HelicalSequence analysisAdd BLAST22
Transmembranei170 – 190HelicalSequence analysisAdd BLAST21
Topological domaini191 – 582CytoplasmicSequence analysisAdd BLAST392
Transmembranei583 – 604HelicalSequence analysisAdd BLAST22
Transmembranei608 – 630HelicalSequence analysisAdd BLAST23
Transmembranei661 – 684HelicalSequence analysisAdd BLAST24
Topological domaini685 – 707ExtracellularSequence analysisAdd BLAST23
Transmembranei708 – 733HelicalSequence analysisAdd BLAST26
Transmembranei741 – 761HelicalSequence analysisAdd BLAST21
Transmembranei788 – 804HelicalSequence analysisAdd BLAST17
Topological domaini805 – 1064CytoplasmicSequence analysisAdd BLAST260

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: BHF-UCL
  • plasma membrane Source: GO_Central
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2095179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001956921 – 1064Adenylate cyclase type 4Add BLAST1064

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei517PhosphoserineCombined sources1
Modified residuei533PhosphothreonineCombined sources1
Glycosylationi694N-linked (GlcNAc...)Sequence analysis1
Glycosylationi701N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP26770.
PRIDEiP26770.

PTM databases

iPTMnetiP26770.
PhosphoSitePlusiP26770.

Expressioni

Tissue specificityi

Widely distributed.1 Publication

Interactioni

GO - Molecular functioni

  • G-protein beta/gamma-subunit complex binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027719.

Structurei

3D structure databases

ProteinModelPortaliP26770.
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 modules have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two modules.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.
InParanoidiP26770.

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. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26770-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLFSPRPP PSEDLFYETY YSLSQQYPLL ILLLVIVLCA IVALPAVAWA
60 70 80 90 100
SGRELTSDPS FLTTVLCALG GFSLLLGLAS REQQLQRWTR PLSGLIWAAL
110 120 130 140 150
LALGYGFLFT GGVVSAWDQV SFFLFIIFTV YAMLPLGMRD AAAAGVISSL
160 170 180 190 200
SHLLVLGLYL GWRPESQRDL LPQLAANAVL FLCGNVVGAY HKALMERALR
210 220 230 240 250
ATFREALSSL HSRRRLDTEK KHQEHLLLSI LPAYLAREMK AEIMARLQAG
260 270 280 290 300
QSSRPENTNN FHSLYVKRHQ GVSVLYADIV GFTRLASECS PKELVLMLNE
310 320 330 340 350
LFGKFDQIAK EHECMRIKIL GDCYYCVSGL PLSLPDHAIN CVRMGLDMCR
360 370 380 390 400
AIRKLRVATG VDINMRVGVH SGSVLCGVIG LQKWQYDVWS HDVTLANHME
410 420 430 440 450
AGGVPGRVHI TGATLALLAG AYAVERADME HRDPYLRELG EPTYLVIDPW
460 470 480 490 500
AEEEDEKGTE RGLLSSLEGH TMRPSLLMTR YLESWGAAKP FAHLSHVDSP
510 520 530 540 550
ASTSTPLPEK AFSPQWSLDR SRTPRGLHDE LDTGDAKFFQ VIEQLNSQKQ
560 570 580 590 600
WKQSKDFNLL TLYFREKEME KQYRLSALPA FKYYAACTFL VFLSNFTIQM
610 620 630 640 650
LVTTRPPALA TTYSITFLLF LLLLFVCFSE HLTKCVQKGP KMLHWLPALS
660 670 680 690 700
VLVATRPGLR VALGTATILL VFTMAVVSLL FLPVSSDCPF LAPNVSSVAF
710 720 730 740 750
NTSWELPASL PLISIPYSMH CCVLGFLSCS LFLHMSFELK LLLLLLWLVA
760 770 780 790 800
SCSLFLHSHA WLSDCLIARL YQGSLGSRPG VLKEPKLMGA IYFFIFFFTL
810 820 830 840 850
LVLARQNEYY CRLDFLWKKK LRQEREETET MENVLPAHVA PQLIGQNRRN
860 870 880 890 900
EDLYHQSYEC VCVLFASIPD FKEFYSESNI NHEGLECLRL LNEIIADFDE
910 920 930 940 950
LLSKPKFSGV EKIKTIGSTY MAATGLNATP GQDTQQDAER SCSHLGTMVE
960 970 980 990 1000
FAVALGSKLG VINKHSFNNF RLRVGLNHGP VVAGVIGAQK PQYDIWGNTV
1010 1020 1030 1040 1050
NVASRMESTG VLGKIQVTEE TARALQSLGY TCYSRGVIKV KGKGQLCTYF
1060
LNTDLTRTGS PSAS
Length:1,064
Mass (Da):118,799
Last modified:August 1, 1992 - v1
Checksum:i5A2A0B895B5A0DA8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80633 mRNA. Translation: AAA40665.1.
PIRiA41542.
UniGeneiRn.1904.

Genome annotation databases

UCSCiRGD:2034. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80633 mRNA. Translation: AAA40665.1.
PIRiA41542.
UniGeneiRn.1904.

3D structure databases

ProteinModelPortaliP26770.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027719.

Chemistry databases

ChEMBLiCHEMBL2095179.

PTM databases

iPTMnetiP26770.
PhosphoSitePlusiP26770.

Proteomic databases

PaxDbiP26770.
PRIDEiP26770.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2034. rat.

Organism-specific databases

RGDi2034. Adcy4.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP26770.

Miscellaneous databases

PROiP26770.

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. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADCY4_RAT
AccessioniPrimary (citable) accession number: P26770
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 2, 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.