Adenylate cyclase type 6 - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot Q03343 (ADCY6_RAT)

Last modified October 13, 2009. Version 83. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Adenylate cyclase type 6
    EC=4.6.1.1
Alternative name(s):
    Adenylate cyclase type VI
      Short name=ACVI
    ATP pyrophosphate-lyase 6
    Adenylyl cyclase 6
    Ca(2+)-inhibitable adenylyl cyclase

Gene names

Name:

Adcy6

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	1166 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Membrane-bound, calcium-inhibitable adenylyl cyclase.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 2 magnesium ions per subunit By similarity.
Enzyme regulation	Inhibition by calcium in the submicromolar concentration range.
Subcellular location	Membrane; Multi-pass membrane protein.
Post-translational modification	Phosphorylation by PKC on Ser-554, Ser-660 and Thr-917 inhibits catalytic activity.
Sequence similarities	Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Contains 2 guanylate cyclase domains.

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Ontologies

Keywords
Biological process	cAMP biosynthesis
Cellular component	Membrane
Domain	Repeat Transmembrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	cAMP biosynthetic process Inferred from direct assay. Source: RGD intracellular signaling cascade Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Inferred from direct assay. Source: RGD membrane raft Inferred from direct assay. Source: RGD microvillus membrane Inferred from direct assay. Source: RGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium- and calmodulin-responsive adenylate cyclase activity Inferred from mutant phenotype. Source: RGD magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1166

1166

Adenylate cyclase type 6

PRO_0000195701

Regions

Topological domain

1 – 149

149

Cytoplasmic Potential

Transmembrane

150 – 166

Potential

Transmembrane

179 – 195

Potential

Transmembrane

212 – 228

Potential

Transmembrane

237 – 253

Potential

Transmembrane

257 – 273

Potential

Transmembrane

287 – 303

Potential

Topological domain

304 – 671

368

Cytoplasmic Potential

Transmembrane

672 – 689

Potential

Transmembrane

700 – 716

Potential

Transmembrane

741 – 757

Potential

Topological domain

758 – 817

Extracellular Potential

Transmembrane

818 – 834

Potential

Transmembrane

837 – 853

Potential

Transmembrane

895 – 911

Potential

Topological domain

912 – 1166

255

Cytoplasmic Potential

Sites

Metal binding

382

Magnesium 1 By similarity

Metal binding

382

Magnesium 2 By similarity

Metal binding

383

Magnesium 2; via carbonyl oxygen By similarity

Metal binding

426

Magnesium 1 By similarity

Metal binding

426

Magnesium 2 By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

554

Phosphoserine; by PKC; in vitro Ref.3

Modified residue

574

Phosphoserine By similarity

Modified residue

660

Phosphoserine; by PKC; in vitro Ref.3

Modified residue

917

Phosphothreonine; by PKC; in vitro Ref.3

Glycosylation

791

N-linked (GlcNAc...) Potential

Glycosylation

876

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

311

S → A: No effect on phosphorylation by PKC. Ref.3

Mutagenesis

554

S → A: Reduces phosphorylation by PKC and PKC-mediated inhibition. Ref.3

Mutagenesis

660

S → A: Reduces phosphorylation by PKC and PKC-mediated inhibition. Ref.3

Mutagenesis

917

T → A: Reduces phosphorylation by PKC, abolishes PKC-mediated inhibition. Ref.3

Sequence conflict

K → E in AAA40678. Ref.2

Sequence conflict

130

R → P in AAA40678. Ref.2

Sequence conflict

538

G → A in AAA40678. Ref.2

Sequence conflict

790

I → L in AAA40678. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q03343-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 5042C650546E4E79
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FASTA

1,166

130,506

        10         20         30         40         50         60 
MSWFSGLLVP KVDERKTAWG ERNGQKRPRQ ATRARGFCAP RYMSCLKNVE PPSPTPAART 

        70         80         90        100        110        120 
RCPWQDEAFI RRAGPGRGVK LGLRSVALGF DDTEVTTPMG TAEVAPDTSP RSGPSCWHRL 

       130        140        150        160        170        180 
AQVFQSKQFR SAKLERLYQR YFFQMNQSSL TLLMAVLVLL MAVLLTFHAA PALPQPAYVA 

       190        200        210        220        230        240 
LLTCASVLFV VLMVVCNRHS FRQDSMWVVS YVVLGILAAV QVGGALAANP RSPSAGLWCP 

       250        260        270        280        290        300 
VFFVYITYTL LPIRMRAAVL SGLGLSTLHL ILAWHLNNGD PFLWKQLGAN VVLFLCTNAI 

       310        320        330        340        350        360 
GVCTHYPAEV SQRQAFQETR GYIQARLHLQ HENRQQERLL LSVLPQHVAM EMKEDINTKK 

       370        380        390        400        410        420 
EDMMFHKIYI QKHDNVSILF ADIEGFTSLA SQCTAQELVM TLNELFARFD KLAAENHCLR 

       430        440        450        460        470        480 
IKILGDCYYC VSGLPEARAD HAHCCVEMGV DMIEAISLVR EVTGVNVNMR VGIHSGRVHC 

       490        500        510        520        530        540 
GVLGLRKWQF DVWSNDVTLA NHMEAGGRAG RIHITRATLQ YLNGDYEVEP GRGGERNGYL 

       550        560        570        580        590        600 
KEQCIETFLI LGASQKRKEE KAMLVKLQRT RANSMEGLMP RWVPDRAFSR TKDSKAFRQM 

       610        620        630        640        650        660 
GIDDSSKENR GAQDALNPED EVDEFLGRAI DARSIDQLRK DHVRRFLLTF QREDLEKKYS 

       670        680        690        700        710        720 
RKVDPRFGAY VACALLVFCF ICFIQFLVFP HSALILGIYA GIFLLLLVTV LICAVCSCGS 

       730        740        750        760        770        780 
FFPNALQRLS RSIVRSRVHS TAVGVFSVLL VFISAIANMF TCSHTPLRTC AARMLNLTPS 

       790        800        810        820        830        840 
DVTACHLRQI NYSLGLEAPL CEGTAPTCSF PEYFVGSVLL SLLASSVFLH ISSIGKLVMT 

       850        860        870        880        890        900 
FVLGFIYLLL LLLGPPATIF DNYDLLLSVH GLASSNETFD GLDCPAVGRV ALKYMTPVIL 

       910        920        930        940        950        960 
LVFALALYLH AQQVESTARL DFLWKLQATG EKEEMEELQA YNRRLLHNIL PKDVAAHFLA 

       970        980        990       1000       1010       1020 
RERRNDELYY QSCECVAVMF ASIANFSEFY VELEANNEGV ECLRLLNEII ADFDEIISEE 

      1030       1040       1050       1060       1070       1080 
RFRQLEKIKT IGSTYMAASG LNASTYDQVG RSHITALADY AMRLMEQMKH INEHSFNNFQ 

      1090       1100       1110       1120       1130       1140 
MKIGLNMGPV VAGVIGARKP QYDIWGNTVN VSSRMDSTGV PDRIQVTTDL YQVLAAKGYQ 

      1150       1160 
LECRGVVKVK GKGEMTTYFL NGGPSS

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References

[1]	"Molecular diversity in the adenylylcyclase family. Evidence for eight forms of the enzyme and cloning of type VI." Krupinski J., Lehman T.C., Frankenfield C.D., Zwaagstra J.C., Watson P.A. J. Biol. Chem. 267:24858-24862(1992) [PubMed: 1332969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Two members of a widely expressed subfamily of hormone-stimulated adenylyl cyclases." Premont R.T., Chen J., Ma H.-W., Ponnapalli M., Iyengar R. Proc. Natl. Acad. Sci. U.S.A. 89:9809-9813(1992) [PubMed: 1409703] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"Protein kinase C inhibits type VI adenylyl cyclase by phosphorylating the regulatory N domain and two catalytic C1 and C2 domains." Lin T.-H., Lai H.-L., Kao Y.-Y., Sun C.-N., Hwang M.-J., Chern Y. J. Biol. Chem. 277:15721-15728(2002) [PubMed: 11877398] [Abstract] Cited for: PHOSPHORYLATION AT SER-554; SER-660 AND THR-917, MUTAGENESIS OF SER-311; SER-554; SER-660 AND THR-917.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	L01115 mRNA. Translation: AAA40676.1. M96160 mRNA. Translation: AAA40678.1. Different initiation.
IPI	IPI00567549.
PIR	A47202.
RefSeq	NP_036953.2.
UniGene	Rn.3313
3D structure databases
HSSP	HSSP built from PDB template 1AZS based on UniProtKB P30803.
SMR	Q03343. Positions 362-551.
ModBase	Search...
Protein-protein interaction databases
STRING	Q03343.
PTM databases
PhosphoSite	Q03343.
Proteomic databases
PRIDE	Q03343.
Genome annotation databases
Ensembl	ENSRNOT00000016623; ENSRNOP00000016624; ENSRNOG00000011587; Rattus norvegicus. [Genome view] ENSRNOT00000047864; ENSRNOP00000044606; ENSRNOG00000011587; Rattus norvegicus. [Genome view]
GeneID	25289.
KEGG	rno:25289.
UCSC	M96160. rat.
Organism-specific databases
CTD	25289.
RGD	2035. Adcy6.
Phylogenomic databases
HOVERGEN	Q03343.
Enzyme and pathway databases
BRENDA	4.6.1.1. 248.
Gene expression databases
ArrayExpress	Q03343.
Genevestigator	Q03343.
GermOnline	ENSRNOG00000011587. Rattus norvegicus.
Family and domain databases
InterPro	IPR001054. A/G_cyclase. IPR018297. A/G_cyclase_CS. IPR009398. Aden_cycl-like. [Graphical view]
Gene3D	G3DSA:3.30.70.1230. A/G_cyclase. 2 hits.
Pfam	PF06327. DUF1053. 1 hit. PF00211. Guanylate_cyc. 2 hits. [Graphical view]
SMART	SM00044. CYCc. 2 hits. [Graphical view]
PROSITE	PS00452. GUANYLATE_CYCLASE_1. 2 hits. PS50125. GUANYLATE_CYCLASE_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	606029.

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Entry information

Entry name

ADCY6_RAT

Accession

Primary (citable) accession number: Q03343

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	October 13, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents