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P51829

- ADCY7_MOUSE

UniProt

P51829 - ADCY7_MOUSE

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Protein
Adenylate cyclase type 7
Gene
Adcy7
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Binds 2 magnesium ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi286 – 2861Magnesium 1 By similarity
Metal bindingi286 – 2861Magnesium 2 By similarity
Metal bindingi287 – 2871Magnesium 2; via carbonyl oxygen By similarity
Metal bindingi330 – 3301Magnesium 1 By similarity
Metal bindingi330 – 3301Magnesium 2 By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. adenylate cyclase activity Source: MGI
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. activation of adenylate cyclase activity Source: MGI
  2. cAMP biosynthetic process Source: MGI
  3. cellular response to ethanol Source: Ensembl
  4. intracellular signal transduction Source: InterPro
  5. maternal process involved in female pregnancy Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cAMP biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_210399. Glucagon signaling in metabolic regulation.
REACT_213947. Regulation of water balance by renal Aquaporins.
REACT_220108. PKA activation.
REACT_220758. PKA activation in glucagon signalling.
REACT_222824. Adenylate cyclase inhibitory pathway.
REACT_224974. Adenylate cyclase activating pathway.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:102891. Adcy7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei34 – 5421Helical; Reviewed prediction
Add
BLAST
Transmembranei63 – 8321Helical; Reviewed prediction
Add
BLAST
Transmembranei95 – 11723Helical; Reviewed prediction
Add
BLAST
Transmembranei122 – 14221Helical; Reviewed prediction
Add
BLAST
Transmembranei147 – 16721Helical; Reviewed prediction
Add
BLAST
Transmembranei178 – 19821Helical; Reviewed prediction
Add
BLAST
Topological domaini199 – 595397Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei596 – 61621Helical; Reviewed prediction
Add
BLAST
Transmembranei621 – 64121Helical; Reviewed prediction
Add
BLAST
Transmembranei670 – 68920Helical; Reviewed prediction
Add
BLAST
Transmembranei719 – 73820Helical; Reviewed prediction
Add
BLAST
Transmembranei747 – 76620Helical; Reviewed prediction
Add
BLAST
Transmembranei813 – 83321Helical; Reviewed prediction
Add
BLAST
Topological domaini834 – 1099266Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10991099Adenylate cyclase type 7
PRO_0000195704Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi702 – 7021N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP51829.
PRIDEiP51829.

PTM databases

PhosphoSiteiP51829.

Expressioni

Tissue specificityi

Most abundant in heart, spleen and lung.

Gene expression databases

BgeeiP51829.
CleanExiMM_ADCY7.
GenevestigatoriP51829.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliP51829.
SMRiP51829. Positions 266-455, 890-1088.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2114.
GeneTreeiENSGT00750000117304.
HOVERGENiHBG050458.
InParanoidiQ3U3P2.
KOiK08047.
OMAiESDDCRI.
OrthoDBiEOG76X5ZC.
TreeFamiTF313845.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Adenylate_cyclase-like.
[Graphical view]
PfamiPF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
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.

P51829-1 [UniParc]FASTAAdd to Basket

« Hide

MPAKGRYFLN EGDEGPDQAA LYEKYRLTSL HGPLLLLLLL VAAATCIALI     50
SIAFSHEDLR RHQVVLGTAF LMLTLFVALY VLVYVECLVQ RWLRALALLT 100
WACLMVLGSV LMWDSLENEA HAWEQVPFFL FVVFVVYALL PLSRRAAIVA 150
GVTSTVSHLL VFGAVTRAFQ TSMSSTQLGL QLLANAVILL GGNFTGAFHK 200
HQLQDASRDL FIYTVKCIQI RRKLRVEKRQ QENLLLSVLP AHISMGMKLA 250
IIERLKEGGD RHYMPDNNFH SLYVKRHQNV SILYADIVGF TRLASDCSPK 300
ELVVVLNELF GKFDQIAKAN ECMRIKILGD CYYCVSGLPV SLPTHARNCV 350
KMGLDICEAI KQVREATGVD ISMRVGIHSG NVLCGVIGLR KWQYDVWSHD 400
VSLANRMEAA GVPGRVHITE ATLNHLDKAY EVEDGHGEQR DPYLKEMNIR 450
TYLVIDPRSQ QPPPPSHHLS KPKGDATLKM RASVRVTRYL ESWGAARPFA 500
HLNHRESVSS SETPISNGRR QKAIPLRRHR APDRSASPKG RLEDDCDDEM 550
LSAIEGLSST RPCCSKSDDF HTFGPIFLEK GFEREYRLVP IPRARYDFAC 600
ASLVFVCILL VHLLVMPRMA TLGVSFGLVA CLLGLVLSFC FATEFSRCFP 650
SRSTLQAISE SVETQPLVRL VLVVLTVGSL LTVAIINMPL TLNPGPEQPG 700
DNKTSPLAAQ NRVGTPCELL PYYTCSCILG FIACSVFLRM SLELKAMLLT 750
VALVAYLLLF NLSPCWHVSG NSTETNGTQR TRLLLSDAQS MPSHTLAPGA 800
RETAPSPSYL ERDLKIMVNF YLILFYATLI LLSRQIDYYC RLDCLWKKKF 850
KKEHEEFETM ENVNRLLLEN VLPAHVAAHF IGDKAAEDWY HQSYDCVCVM 900
FASVPDFKVF YTECDVNKEG LECLRLLNEI IADFDELLLK PKFSGVEKIK 950
TIGSTYMAAA GLSAPSGHEN QDLERKHVHI GVLVEFSMAL MSKLDGINRH 1000
SFNSFRLRVG INHGPVIAGV IGARKPQYDI WGNTVNVASR MESTGELGKI 1050
QVTEETCTIL QGLGYSCECR GLINVKGKGE LRTYFVCTDT AKFQGLGLN 1099
Length:1,099
Mass (Da):122,708
Last modified:July 27, 2011 - v2
Checksum:i0EE189EA9070FF73
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti150 – 1501A → V in AAA57554. 1 Publication
Sequence conflicti717 – 7171C → Y in AAA57554. 1 Publication
Sequence conflicti801 – 8011R → Q in AAA57554. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12919 mRNA. Translation: AAA57554.1.
AK154652 mRNA. Translation: BAE32743.1.
CCDSiCCDS22509.1.
PIRiA55405.
RefSeqiNP_001032812.2. NM_001037723.3.
NP_001032813.1. NM_001037724.4.
NP_001103226.1. NM_001109756.1.
NP_031432.2. NM_007406.2.
UniGeneiMm.288206.

Genome annotation databases

EnsembliENSMUST00000098521; ENSMUSP00000096122; ENSMUSG00000031659.
ENSMUST00000168545; ENSMUSP00000129252; ENSMUSG00000031659.
ENSMUST00000169037; ENSMUSP00000130594; ENSMUSG00000031659.
ENSMUST00000171456; ENSMUSP00000132528; ENSMUSG00000031659.
GeneIDi11513.
KEGGimmu:11513.
UCSCiuc009mrh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U12919 mRNA. Translation: AAA57554.1 .
AK154652 mRNA. Translation: BAE32743.1 .
CCDSi CCDS22509.1.
PIRi A55405.
RefSeqi NP_001032812.2. NM_001037723.3.
NP_001032813.1. NM_001037724.4.
NP_001103226.1. NM_001109756.1.
NP_031432.2. NM_007406.2.
UniGenei Mm.288206.

3D structure databases

ProteinModelPortali P51829.
SMRi P51829. Positions 266-455, 890-1088.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P51829.

PTM databases

PhosphoSitei P51829.

Proteomic databases

PaxDbi P51829.
PRIDEi P51829.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000098521 ; ENSMUSP00000096122 ; ENSMUSG00000031659 .
ENSMUST00000168545 ; ENSMUSP00000129252 ; ENSMUSG00000031659 .
ENSMUST00000169037 ; ENSMUSP00000130594 ; ENSMUSG00000031659 .
ENSMUST00000171456 ; ENSMUSP00000132528 ; ENSMUSG00000031659 .
GeneIDi 11513.
KEGGi mmu:11513.
UCSCi uc009mrh.2. mouse.

Organism-specific databases

CTDi 113.
MGIi MGI:102891. Adcy7.

Phylogenomic databases

eggNOGi COG2114.
GeneTreei ENSGT00750000117304.
HOVERGENi HBG050458.
InParanoidi Q3U3P2.
KOi K08047.
OMAi ESDDCRI.
OrthoDBi EOG76X5ZC.
TreeFami TF313845.

Enzyme and pathway databases

Reactomei REACT_210399. Glucagon signaling in metabolic regulation.
REACT_213947. Regulation of water balance by renal Aquaporins.
REACT_220108. PKA activation.
REACT_220758. PKA activation in glucagon signalling.
REACT_222824. Adenylate cyclase inhibitory pathway.
REACT_224974. Adenylate cyclase activating pathway.

Miscellaneous databases

ChiTaRSi ADCY7. mouse.
NextBioi 278918.
PROi P51829.
SOURCEi Search...

Gene expression databases

Bgeei P51829.
CleanExi MM_ADCY7.
Genevestigatori P51829.

Family and domain databases

Gene3Di 3.30.70.1230. 2 hits.
InterProi IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Adenylate_cyclase-like.
[Graphical view ]
Pfami PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view ]
SMARTi SM00044. CYCc. 2 hits.
[Graphical view ]
SUPFAMi SSF55073. SSF55073. 2 hits.
PROSITEi PS00452. GUANYLATE_CYCLASE_1. 1 hit.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiADCY7_MOUSE
AccessioniPrimary (citable) accession number: P51829
Secondary accession number(s): Q3U3P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 115 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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