Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O88444

- ADCY1_MOUSE

UniProt

O88444 - ADCY1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Adenylate cyclase type 1

Gene

Adcy1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina.1 Publication

Catalytic activityi

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

Cofactori

Binds 2 magnesium ions per subunit.By similarity

Enzyme regulationi

Activated by calcium/calmodulin. Inhibited by the G protein beta and gamma subunit complex (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi307 – 3071Magnesium 1PROSITE-ProRule annotation
Metal bindingi307 – 3071Magnesium 2PROSITE-ProRule annotation
Metal bindingi308 – 3081Magnesium 2; via carbonyl oxygenPROSITE-ProRule annotation
Metal bindingi351 – 3511Magnesium 1PROSITE-ProRule annotation
Metal bindingi351 – 3511Magnesium 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. adenylate cyclase activity Source: MGI
  2. ATP binding Source: UniProtKB-KW
  3. calcium- and calmodulin-responsive adenylate cyclase activity Source: Ensembl
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. activation of adenylate cyclase activity Source: MGI
  2. axonogenesis Source: MGI
  3. cAMP biosynthetic process Source: MGI
  4. circadian rhythm Source: Ensembl
  5. intracellular signal transduction Source: InterPro
  6. long-term memory Source: MGI
  7. regulation of circadian rhythm Source: UniProtKB
  8. response to drug Source: Ensembl
  9. response to lithium ion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Biological rhythms, cAMP biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
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.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Adcy1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:99677. Adcy1.

Subcellular locationi

Membrane; Multi-pass membrane protein. Cytoplasm 1 Publication
Note: Expressed in the cytoplasm of supporting cells and hair cells of the cochlea vestibule, as well as to the cochlear hair cell nuclei and stereocilia.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: Ensembl
  3. integral component of membrane Source: UniProtKB-KW
  4. nucleus Source: Ensembl
  5. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show a significant reduction in daytime contrast sensitivity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11181118Adenylate cyclase type 1PRO_0000195683Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi703 – 7031N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO88444.
PaxDbiO88444.
PRIDEiO88444.

PTM databases

PhosphoSiteiO88444.

Expressioni

Tissue specificityi

Expressed throughout inner ear development.1 Publication

Inductioni

Expression in the retina oscillates in a circadian manner.1 Publication

Gene expression databases

BgeeiO88444.
CleanExiMM_ADCY1.
ExpressionAtlasiO88444. baseline and differential.
GenevestigatoriO88444.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020706.

Structurei

3D structure databases

ProteinModelPortaliO88444.
SMRiO88444. Positions 289-476, 859-1053.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6262CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini234 – 609376CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini794 – 1118325CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei63 – 8321HelicalSequence AnalysisAdd
BLAST
Transmembranei87 – 10721HelicalSequence AnalysisAdd
BLAST
Transmembranei124 – 14421HelicalSequence AnalysisAdd
BLAST
Transmembranei157 – 17721HelicalSequence AnalysisAdd
BLAST
Transmembranei182 – 20221HelicalSequence AnalysisAdd
BLAST
Transmembranei213 – 23321HelicalSequence AnalysisAdd
BLAST
Transmembranei610 – 63021HelicalSequence AnalysisAdd
BLAST
Transmembranei634 – 65421HelicalSequence AnalysisAdd
BLAST
Transmembranei673 – 69321HelicalSequence AnalysisAdd
BLAST
Transmembranei724 – 74421HelicalSequence AnalysisAdd
BLAST
Transmembranei752 – 77221HelicalSequence AnalysisAdd
BLAST
Transmembranei774 – 79320HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni492 – 51928Interaction with calmodulinBy similarityAdd
BLAST
Regioni1023 – 104624Interaction with calmodulinBy similarityAdd
BLAST

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

eggNOGiCOG2114.
GeneTreeiENSGT00760000119042.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiO88444.
KOiK08041.
OMAiCLPWAWS.
OrthoDBiEOG7B8S30.
PhylomeDBiO88444.
TreeFamiTF313845.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF00211. Guanylate_cyc. 2 hits.
[Graphical view]
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.

O88444 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGAPRGQGG GGGAGEPGGA ERAAGPGGRR GFRACGEEFA CPELEALFRG
60 70 80 90 100
YTLRLEQAAT LKALAVLSLL AGALALAELL GAPGPAPGLA KGSHPVHCIL
110 120 130 140 150
FLALFVVTNV RSLQVSQLQQ VGQLALFFSL TFALLCCPFA LGGPARSSAG
160 170 180 190 200
GAMGSTVAEQ GVWQLLLVTF VSYALLPVRS LLAIGFGLVV AASHLLVTAA
210 220 230 240 250
LVPAKRPRLW RTLGANALLF FGVNMYGVFV RILTERSQRK AFLQARNCIE
260 270 280 290 300
DRLRLEDENE KQERLLMSLL PRNVAMEMKE DFLKPPERIF HKIYIQRHDN
310 320 330 340 350
VSILFADIVG FTGLASQCTA QELVKLLNEL FGKFDELATE NHCRRIKILG
360 370 380 390 400
DCYYCVSGLT QPKTDHAHCC VEMGLDMIDT ITSVAEATEV DLNMRVGLHT
410 420 430 440 450
GRVLCGVLGL RKWQYDVWSN DVTLANVMEA AGLPGKVHIT KTTLACLNGD
460 470 480 490 500
YEVEPGHGHE RNTFLRTHNI ETFFIVPSHR RKIFPGLILS DIKPAKRMKF
510 520 530 540 550
KTVCYLLVQL MHCRKMFKAE IPFSNVMTCE DDDKRRALRT ASEKLRNRSS
560 570 580 590 600
FSTNVVYTTP GTRVNRYISR LLEARQTELE MADLNFFTLK YKHVEREQKY
610 620 630 640 650
HQLQDEYFTS AVVLALILAA LFGLIYLLVI PQSVAVLLLL VFSICFLVAC
660 670 680 690 700
TLYLHITRVQ CFPGCLTIQI RTALCVFIVV LIYSVAQGCV VGCLPWAWSS
710 720 730 740 750
QSNSSLVVLA AGGRRTVLPA LPCESAHHAL LCCLVGTLPL AIFLRVSSLP
760 770 780 790 800
KMILLSGLTT SYILVLELSG YTKVGGGALS GRSYEPIMAI LLFSCTLALH
810 820 830 840 850
ARQVDVRLRL DYLWAAQAEE ERDDMERVKL DNKRILFNLL PAHVAQHFLM
860 870 880 890 900
SNPRNMDLYY QSYSQVGVMF ASIPNFNDFY IELDGNNMGV ECLRLLNEII
910 920 930 940 950
ADFDELMDKD FYKDLEKIKT IGSTYMAAVG LAPTAGTRAK KSISSHLCTL
960 970 980 990 1000
ADFAIDMFDV LDEINYQSYN DFVLRVGINV GPVVAGVIGA RRPQYDIWGN
1010 1020 1030 1040 1050
TVNVASRMDS TGVQGRIQVT EEVHRLLKRC SYQFVCRGKV SVKGKGEMLT
1060 1070 1080 1090 1100
YFLEGRTDGN SSHGRTFRLE RRMCPYGRGG GQARRPPLCP AAGPPVRPGL
1110
PPAPTSQYLS STAAGKEA
Length:1,118
Mass (Da):123,373
Last modified:April 12, 2005 - v2
Checksum:iCEFAFF3940B22277
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1559SSAGGAMGS → ALQEAQWAR in AAC29478. (PubMed:9662407)Curated
Sequence conflicti234 – 2341T → A in AAC29478. (PubMed:9662407)Curated
Sequence conflicti270 – 2701L → M in AAC29478. (PubMed:9662407)Curated
Sequence conflicti319 – 3191T → K in AAC29478. (PubMed:9662407)Curated
Sequence conflicti466 – 4661R → K in AAC29478. (PubMed:9662407)Curated
Sequence conflicti523 – 5231F → I in AAC29478. (PubMed:9662407)Curated
Sequence conflicti542 – 5421S → T in AAC29478. (PubMed:9662407)Curated
Sequence conflicti549 – 5491S → T in AAC29478. (PubMed:9662407)Curated
Sequence conflicti570 – 5701R → L in AAC29478. (PubMed:9662407)Curated
Sequence conflicti598 – 5981Q → R in AAC29478. (PubMed:9662407)Curated
Sequence conflicti692 – 6921G → V in AAC29478. (PubMed:9662407)Curated
Sequence conflicti697 – 6971A → S in AAC29478. (PubMed:9662407)Curated
Sequence conflicti707 – 7071V → L in AAC29478. (PubMed:9662407)Curated
Sequence conflicti713 – 7131G → C in AAC29478. (PubMed:9662407)Curated
Sequence conflicti720 – 7212AL → GP in AAC29478. (PubMed:9662407)Curated
Sequence conflicti774 – 7763VGG → AMGA in AAC29478. (PubMed:9662407)Curated
Sequence conflicti867 – 8693GVM → AVL in AAC29478. (PubMed:9662407)Curated
Sequence conflicti938 – 9381R → K in AAC29478. (PubMed:9662407)Curated
Sequence conflicti991 – 9911R → C in AAC29478. (PubMed:9662407)Curated
Sequence conflicti1020 – 10201T → I in AAC29478. (PubMed:9662407)Curated
Sequence conflicti1030 – 10301C → S in AAC29478. (PubMed:9662407)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL669838 Genomic DNA. Translation: CAI25155.1.
AF053980 mRNA. Translation: AAC29478.1.
CCDSiCCDS24426.1.
RefSeqiNP_033752.1. NM_009622.1.
UniGeneiMm.259733.

Genome annotation databases

EnsembliENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431.
GeneIDi432530.
KEGGimmu:432530.
UCSCiuc007hzf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL669838 Genomic DNA. Translation: CAI25155.1 .
AF053980 mRNA. Translation: AAC29478.1 .
CCDSi CCDS24426.1.
RefSeqi NP_033752.1. NM_009622.1.
UniGenei Mm.259733.

3D structure databases

ProteinModelPortali O88444.
SMRi O88444. Positions 289-476, 859-1053.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000020706.

Chemistry

BindingDBi O88444.

PTM databases

PhosphoSitei O88444.

Proteomic databases

MaxQBi O88444.
PaxDbi O88444.
PRIDEi O88444.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020706 ; ENSMUSP00000020706 ; ENSMUSG00000020431 .
GeneIDi 432530.
KEGGi mmu:432530.
UCSCi uc007hzf.1. mouse.

Organism-specific databases

CTDi 107.
MGIi MGI:99677. Adcy1.

Phylogenomic databases

eggNOGi COG2114.
GeneTreei ENSGT00760000119042.
HOGENOMi HOG000006941.
HOVERGENi HBG050458.
InParanoidi O88444.
KOi K08041.
OMAi CLPWAWS.
OrthoDBi EOG7B8S30.
PhylomeDBi O88444.
TreeFami TF313845.

Enzyme and pathway databases

Reactomei REACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
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 ADCY1. mouse.
NextBioi 407738.
PROi O88444.
SOURCEi Search...

Gene expression databases

Bgeei O88444.
CleanExi MM_ADCY1.
ExpressionAtlasi O88444. baseline and differential.
Genevestigatori O88444.

Family and domain databases

Gene3Di 3.30.70.1230. 2 hits.
InterProi IPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR029787. Nucleotide_cyclase.
[Graphical view ]
Pfami PF00211. Guanylate_cyc. 2 hits.
[Graphical view ]
SMARTi SM00044. CYCc. 2 hits.
[Graphical view ]
SUPFAMi SSF55073. SSF55073. 2 hits.
PROSITEi PS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "Loss of adenylyl cyclase I activity disrupts patterning of mouse somatosensory cortex."
    Abdel-Majid R.M., Leong W.L., Schalkwyk L.C., Smallman D.S., Wong S.T., Storm D.R., Fine A., Dobson M.J., Guernsey D.L., Neumann P.E.
    Nat. Genet. 19:289-291(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 100-1050.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Circadian rhythm of contrast sensitivity is regulated by a dopamine-neuronal PAS-domain protein 2-adenylyl cyclase 1 signaling pathway in retinal ganglion cells."
    Hwang C.K., Chaurasia S.S., Jackson C.R., Chan G.C., Storm D.R., Iuvone P.M.
    J. Neurosci. 33:14989-14997(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
  4. "Adenylate cyclase 1 (ADCY1) mutations cause recessive hearing impairment in humans and defects in hair cell function and hearing in zebrafish."
    Santos-Cortez R.L., Lee K., Giese A.P., Ansar M., Amin-Ud-Din M., Rehn K., Wang X., Aziz A., Chiu I., Hussain Ali R., Smith J.D., Shendure J., Bamshad M., Nickerson D.A., Ahmed Z.M., Ahmad W., Riazuddin S., Leal S.M.
    Hum. Mol. Genet. 23:3289-3298(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiADCY1_MOUSE
AccessioniPrimary (citable) accession number: O88444
Secondary accession number(s): Q5SS89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: April 12, 2005
Last modified: October 29, 2014
This is version 113 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