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P51829 (ADCY7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Adcy7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1099 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

Most abundant in heart, spleen and lung.

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 – 10991099Adenylate cyclase type 7
PRO_0000195704

Regions

Topological domain1 – 3333Cytoplasmic Potential
Transmembrane34 – 5421Helical; Potential
Transmembrane63 – 8321Helical; Potential
Transmembrane95 – 11723Helical; Potential
Transmembrane122 – 14221Helical; Potential
Transmembrane147 – 16721Helical; Potential
Transmembrane178 – 19821Helical; Potential
Topological domain199 – 595397Cytoplasmic Potential
Transmembrane596 – 61621Helical; Potential
Transmembrane621 – 64121Helical; Potential
Transmembrane670 – 68920Helical; Potential
Transmembrane719 – 73820Helical; Potential
Transmembrane747 – 76620Helical; Potential
Transmembrane813 – 83321Helical; Potential
Topological domain834 – 1099266Cytoplasmic Potential

Sites

Metal binding2861Magnesium 1 By similarity
Metal binding2861Magnesium 2 By similarity
Metal binding2871Magnesium 2; via carbonyl oxygen By similarity
Metal binding3301Magnesium 1 By similarity
Metal binding3301Magnesium 2 By similarity

Amino acid modifications

Glycosylation7021N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1501A → V in AAA57554. Ref.1
Sequence conflict7171C → Y in AAA57554. Ref.1
Sequence conflict8011R → Q in AAA57554. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51829 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0EE189EA9070FF73

FASTA1,099122,708
        10         20         30         40         50         60 
MPAKGRYFLN EGDEGPDQAA LYEKYRLTSL HGPLLLLLLL VAAATCIALI SIAFSHEDLR 

        70         80         90        100        110        120 
RHQVVLGTAF LMLTLFVALY VLVYVECLVQ RWLRALALLT WACLMVLGSV LMWDSLENEA 

       130        140        150        160        170        180 
HAWEQVPFFL FVVFVVYALL PLSRRAAIVA GVTSTVSHLL VFGAVTRAFQ TSMSSTQLGL 

       190        200        210        220        230        240 
QLLANAVILL GGNFTGAFHK HQLQDASRDL FIYTVKCIQI RRKLRVEKRQ QENLLLSVLP 

       250        260        270        280        290        300 
AHISMGMKLA IIERLKEGGD RHYMPDNNFH SLYVKRHQNV SILYADIVGF TRLASDCSPK 

       310        320        330        340        350        360 
ELVVVLNELF GKFDQIAKAN ECMRIKILGD CYYCVSGLPV SLPTHARNCV KMGLDICEAI 

       370        380        390        400        410        420 
KQVREATGVD ISMRVGIHSG NVLCGVIGLR KWQYDVWSHD VSLANRMEAA GVPGRVHITE 

       430        440        450        460        470        480 
ATLNHLDKAY EVEDGHGEQR DPYLKEMNIR TYLVIDPRSQ QPPPPSHHLS KPKGDATLKM 

       490        500        510        520        530        540 
RASVRVTRYL ESWGAARPFA HLNHRESVSS SETPISNGRR QKAIPLRRHR APDRSASPKG 

       550        560        570        580        590        600 
RLEDDCDDEM LSAIEGLSST RPCCSKSDDF HTFGPIFLEK GFEREYRLVP IPRARYDFAC 

       610        620        630        640        650        660 
ASLVFVCILL VHLLVMPRMA TLGVSFGLVA CLLGLVLSFC FATEFSRCFP SRSTLQAISE 

       670        680        690        700        710        720 
SVETQPLVRL VLVVLTVGSL LTVAIINMPL TLNPGPEQPG DNKTSPLAAQ NRVGTPCELL 

       730        740        750        760        770        780 
PYYTCSCILG FIACSVFLRM SLELKAMLLT VALVAYLLLF NLSPCWHVSG NSTETNGTQR 

       790        800        810        820        830        840 
TRLLLSDAQS MPSHTLAPGA RETAPSPSYL ERDLKIMVNF YLILFYATLI LLSRQIDYYC 

       850        860        870        880        890        900 
RLDCLWKKKF KKEHEEFETM ENVNRLLLEN VLPAHVAAHF IGDKAAEDWY HQSYDCVCVM 

       910        920        930        940        950        960 
FASVPDFKVF YTECDVNKEG LECLRLLNEI IADFDELLLK PKFSGVEKIK TIGSTYMAAA 

       970        980        990       1000       1010       1020 
GLSAPSGHEN QDLERKHVHI GVLVEFSMAL MSKLDGINRH SFNSFRLRVG INHGPVIAGV 

      1030       1040       1050       1060       1070       1080 
IGARKPQYDI WGNTVNVASR MESTGELGKI QVTEETCTIL QGLGYSCECR GLINVKGKGE 

      1090 
LRTYFVCTDT AKFQGLGLN 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the type VII isoform of mammalian adenylyl cyclase expressed widely in mouse tissues and in S49 mouse lymphoma cells."
Watson P.A., Krupinski J., Kempinski A.M., Frankenfield C.D.
J. Biol. Chem. 269:28893-28898(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoma.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12919 mRNA. Translation: AAA57554.1.
AK154652 mRNA. Translation: BAE32743.1.
CCDSCCDS22509.1.
PIRA55405.
RefSeqNP_001032812.2. NM_001037723.3.
NP_001032813.1. NM_001037724.4.
NP_001103226.1. NM_001109756.1.
NP_031432.2. NM_007406.2.
UniGeneMm.288206.

3D structure databases

ProteinModelPortalP51829.
SMRP51829. Positions 266-455, 890-1088.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP51829.

PTM databases

PhosphoSiteP51829.

Proteomic databases

PaxDbP51829.
PRIDEP51829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000098521; ENSMUSP00000096122; ENSMUSG00000031659.
ENSMUST00000168545; ENSMUSP00000129252; ENSMUSG00000031659.
ENSMUST00000169037; ENSMUSP00000130594; ENSMUSG00000031659.
ENSMUST00000171456; ENSMUSP00000132528; ENSMUSG00000031659.
GeneID11513.
KEGGmmu:11513.
UCSCuc009mrh.2. mouse.

Organism-specific databases

CTD113.
MGIMGI:102891. Adcy7.

Phylogenomic databases

eggNOGCOG2114.
GeneTreeENSGT00750000117304.
HOVERGENHBG050458.
InParanoidQ3U3P2.
KOK08047.
OMAESDDCRI.
OrthoDBEOG76X5ZC.
TreeFamTF313845.

Gene expression databases

BgeeP51829.
CleanExMM_ADCY7.
GenevestigatorP51829.

Family and domain databases

Gene3D3.30.70.1230. 2 hits.
InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Adenylate_cyclase-like.
[Graphical view]
PfamPF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
SMARTSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMSSF55073. SSF55073. 2 hits.
PROSITEPS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSADCY7. mouse.
NextBio278918.
PROP51829.
SOURCESearch...

Entry information

Entry nameADCY7_MOUSE
AccessionPrimary (citable) accession number: P51829
Secondary accession number(s): Q3U3P2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot