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Protein

Adenylate cyclase

Gene

CYR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Enzyme regulationi

The presence of GTP-bound RAS2 protein is required in order to elicit a magnesium-dependent adenylyl cyclase activity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1673MagnesiumBy similarity1
Metal bindingi1716MagnesiumBy similarity1

GO - Molecular functioni

  • adenylate cyclase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • magnesium ion binding Source: InterPro

GO - Biological processi

  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: SGD
  • Ras protein signal transduction Source: SGD
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

BioCyciYEAST:YJL005W-MONOMER.
ReactomeiR-SCE-199418. Negative regulation of the PI3K/AKT network.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase (EC:4.6.1.1)
Alternative name(s):
ATP pyrophosphate-lyase
Adenylyl cyclase
Gene namesi
Name:CYR1
Synonyms:CDC35, HSR1, SRA4
Ordered Locus Names:YJL005W
ORF Names:J1401
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL005W.
SGDiS000003542. CYR1.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: SGD
  • mitochondrion Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1651T → D: Attenuation of the response to Ras proteins. 1 Publication1
Mutagenesisi1651T → I: Weak Ras-independent activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001957312 – 2026Adenylate cyclaseAdd BLAST2025

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei376PhosphothreonineCombined sources1
Modified residuei389PhosphothreonineCombined sources1
Modified residuei433PhosphoserineCombined sources1
Modified residuei487PhosphoserineCombined sources1
Modified residuei497PhosphoserineCombined sources1
Modified residuei562PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP08678.
PRIDEiP08678.

PTM databases

iPTMnetiP08678.

Interactioni

Protein-protein interaction databases

BioGridi33752. 66 interactors.
DIPiDIP-2317N.
IntActiP08678. 15 interactors.
MINTiMINT-364060.

Structurei

3D structure databases

ProteinModelPortaliP08678.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini676 – 755Ras-associatingPROSITE-ProRule annotationAdd BLAST80
Repeati815 – 838LRR 1Add BLAST24
Repeati842 – 862LRR 2Add BLAST21
Repeati863 – 885LRR 3Add BLAST23
Repeati886 – 908LRR 4Add BLAST23
Repeati910 – 931LRR 5Add BLAST22
Repeati932 – 955LRR 6Add BLAST24
Repeati957 – 976LRR 7Add BLAST20
Repeati977 – 999LRR 8Add BLAST23
Repeati1001 – 1016LRR 9Add BLAST16
Repeati1017 – 1040LRR 10Add BLAST24
Repeati1042 – 1062LRR 11Add BLAST21
Repeati1063 – 1086LRR 12Add BLAST24
Repeati1088 – 1109LRR 13Add BLAST22
Repeati1110 – 1132LRR 14Add BLAST23
Repeati1134 – 1156LRR 15Add BLAST23
Repeati1188 – 1209LRR 16Add BLAST22
Repeati1210 – 1232LRR 17Add BLAST23
Repeati1233 – 1256LRR 18Add BLAST24
Repeati1258 – 1280LRR 19Add BLAST23
Repeati1285 – 1308LRR 20Add BLAST24
Domaini1357 – 1624PPM-type phosphatasePROSITE-ProRule annotationAdd BLAST268
Domaini1668 – 1805Guanylate cyclasePROSITE-ProRule annotationAdd BLAST138

Sequence similaritiesi

Belongs to the adenylyl cyclase class-3 family.Curated
Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation
Contains 20 LRR (leucine-rich) repeats.Curated
Contains 1 PPM-type phosphatase domain.PROSITE-ProRule annotation
Contains 1 Ras-associating domain.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

GeneTreeiENSGT00440000037833.
HOGENOMiHOG000112124.
InParanoidiP08678.
KOiK01768.
OMAiLRDYAIC.
OrthoDBiEOG092C02M0.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
3.60.40.10. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR013716. Adenylate_cyclase_G-a-bd.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR029787. Nucleotide_cyclase.
IPR001932. PPM-type_phosphatase_dom.
IPR000159. RA_dom.
[Graphical view]
PfamiPF08509. Ad_cyc_g-alpha. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF13855. LRR_8. 4 hits.
PF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00789. Ad_cyc_g-alpha. 1 hit.
SM00044. CYCc. 1 hit.
SM00369. LRR_TYP. 11 hits.
SM00332. PP2Cc. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 3 hits.
SSF55073. SSF55073. 2 hits.
SSF81606. SSF81606. 1 hit.
PROSITEiPS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS51450. LRR. 15 hits.
PS51746. PPM_2. 1 hit.
PS50200. RA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08678-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSKPDTGSE ISGPQRQEEQ EQQIEQSSPT EANDRSIHDE VPKVKKRHEQ
60 70 80 90 100
NSGHKSRRNS AYSYYSPRSL SMTKSRESIT PNGMDDVSIS NVEHPRPTEP
110 120 130 140 150
KIKRGPYLLK KTLSSLSMTS ANSTHDDNKD HGYALNSSKT HNYTSTHNHH
160 170 180 190 200
DGHHDHHHVQ FFPNRKPSLA ETLFKRFSGS NSHDGNKSGK ESKVANLSLS
210 220 230 240 250
TVNPAPANRK PSKDSTLSNH LADNVPSTLR RKVSSLVRGS SVHDINNGIA
260 270 280 290 300
DKQIRPKAVA QSENTLHSSD VPNSKRSHRK SFLLGSTSSS SSRRGSNVSS
310 320 330 340 350
MTNSDSASMA TSGSHVLQHN VSNVSPTTKS KDSVNSESAD HTNNKSEKVT
360 370 380 390 400
PEYNENIPEN SNSDNKREAT TPTIETPISC KPSLFRLDTN LEDVTDITKT
410 420 430 440 450
VPPTAVNSTL NSTHGTETAS PKTVIMPEGP RKSVSMADLS VAAAAPNGEF
460 470 480 490 500
TSTSNDRSQW VAPQSWDVET KRKKTKPKGR SKSRRSSIDA DELDPMSPGP
510 520 530 540 550
PSKKDSRHHH DRKDNESMVT AGDSNSSFVD ICKENVPNDS KTALDTKSVN
560 570 580 590 600
RLKSNLAMSP PSIRYAPSNL DGDYDTSSTS SSLPSSSISS EDTSSCSDSS
610 620 630 640 650
SYTNAYMEAN REQDNKTPIL NKTKSYTKKF TSSSVNMNSP DGAQSSGLLL
660 670 680 690 700
QDEKDDEVEC QLEHYYKDFS DLDPKRHYAI RIFNTDDTFT TLSCTPATTV
710 720 730 740 750
EEIIPALKRK FNITAQGNFQ ISLKVGKLSK ILRPTSKPIL IERKLLLLNG
760 770 780 790 800
YRKSDPLHIM GIEDLSFVFK FLFHPVTPSH FTPEQEQRIM RSEFVHVDLR
810 820 830 840 850
NMDLTTPPII FYQHTSEIES LDVSNNANIF LPLEFIESSI KLLSLRMVNI
860 870 880 890 900
RASKFPSNIT KAYKLVSLEL QRNFIRKVPN SIMKLSNLTI LNLQCNELES
910 920 930 940 950
LPAGFVELKN LQLLDLSSNK FMHYPEVINY CTNLLQIDLS YNKIQSLPQS
960 970 980 990 1000
TKYLVKLAKM NLSHNKLNFI GDLSEMTDLR TLNLRYNRIS SIKTNASNLQ
1010 1020 1030 1040 1050
NLFLTDNRIS NFEDTLPKLR ALEIQENPIT SISFKDFYPK NMTSLTLNKA
1060 1070 1080 1090 1100
QLSSIPGELL TKLSFLEKLE LNQNNLTRLP QEISKLTKLV FLSVARNKLE
1110 1120 1130 1140 1150
YIPPELSQLK SLRTLDLHSN NIRDFVDGME NLELTSLNIS SNAFGNSSLE
1160 1170 1180 1190 1200
NSFYHNMSYG SKLSKSLMFF IAADNQFDDA MWPLFNCFVN LKVLNLSYNN
1210 1220 1230 1240 1250
FSDVSHMKLE SITELYLSGN KLTTLSGDTV LKWSSLKTLM LNSNQMLSLP
1260 1270 1280 1290 1300
AELSNLSQLS VFDVGANQLK YNISNYHYDW NWRNNKELKY LNFSGNRRFE
1310 1320 1330 1340 1350
IKSFISHDID ADLSDLTVLP QLKVLGLMDV TLNTTKVPDE NVNFRLRTTA
1360 1370 1380 1390 1400
SIINGMRYGV ADTLGQRDYV SSRDVTFERF RGNDDECLLC LHDSKNQNAD
1410 1420 1430 1440 1450
YGHNISRIVR DIYDKILIRQ LERYGDETDD NIKTALRFSF LQLNKEINGM
1460 1470 1480 1490 1500
LNSVDNGADV ANLSYADLLS GACSTVIYIR GKKLFAANLG DCMAILSKNN
1510 1520 1530 1540 1550
GDYQTLTKQH LPTKREEYER IRISGGYVNN GKLDGVVDVS RAVGFFDLLP
1560 1570 1580 1590 1600
HIHASPDISV VTLTKADEML IVATHKLWEY MDVDTVCDIA RENSTDPLRA
1610 1620 1630 1640 1650
AAELKDHAMA YGCTENITIL CLALYENIQQ QNRFTLNKNS LMTRRSTFED
1660 1670 1680 1690 1700
TTLRRLQPEI SPPTGNLAMV FTDIKSSTFL WELFPNAMRT AIKTHNDIMR
1710 1720 1730 1740 1750
RQLRIYGGYE VKTEGDAFMV AFPTPTSGLT WCLSVQLKLL DAQWPEEITS
1760 1770 1780 1790 1800
VQDGCQVTDR NGNIIYQGLS VRMGIHWGCP VPELDLVTQR MDYLGPMVNK
1810 1820 1830 1840 1850
AARVQGVADG GQIAMSSDFY SEFNKIMKYH ERVVKGKESL KEVYGEEIIG
1860 1870 1880 1890 1900
EVLEREIAML ESIGWAFFDF GEHKLKGLET KELVTIAYPK ILASRHEFAS
1910 1920 1930 1940 1950
EDEQSKLINE TMLFRLRVIS NRLESIMSAL SGGFIELDSR TEGSYIKFNP
1960 1970 1980 1990 2000
KVENGIMQSI SEKDALLFFD HVITRIESSV ALLHLRQQRC SGLEICRNDK
2010 2020
TSARSNIFNV VDELLQMVKN AKDLST
Length:2,026
Mass (Da):227,834
Last modified:November 1, 1995 - v2
Checksum:iBEAB7419AB6989D0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti262S → L in AAA34549 (PubMed:2934138).Curated1
Sequence conflicti548S → L in AAA34549 (PubMed:2934138).Curated1
Sequence conflicti592D → H in AAA34549 (PubMed:2934138).Curated1
Sequence conflicti709R → I in AAA34549 (PubMed:2934138).Curated1
Sequence conflicti962L → P in AAA34549 (PubMed:2934138).Curated1
Sequence conflicti1388L → S in AAA34549 (PubMed:2934138).Curated1
Sequence conflicti1427E → D in CAA27175 (Ref. 4) Curated1
Sequence conflicti1461A → T in CAA27175 (Ref. 4) Curated1
Sequence conflicti1566A → S in AAA34549 (PubMed:2934138).Curated1
Sequence conflicti1735V → G in AAA34549 (PubMed:2934138).Curated1
Sequence conflicti1956I → V in CAA27175 (Ref. 4) Curated1
Sequence conflicti1996C → F in AAA34549 (PubMed:2934138).Curated1
Sequence conflicti2009 – 2026NVVDE…KDLST → MLLTNFYKWLRTQRIYQLEF CS in CAA27175 (Ref. 4) CuratedAdd BLAST18

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12057 Genomic DNA. Translation: AAA34549.1.
Z49280 Genomic DNA. Translation: CAA89295.1.
X87611 Genomic DNA. Translation: CAA60917.1.
X03449 Genomic DNA. Translation: CAA27175.1.
BK006943 Genomic DNA. Translation: DAA08786.1.
PIRiS56776. OYBY.
RefSeqiNP_012529.3. NM_001181439.3.

Genome annotation databases

EnsemblFungiiYJL005W; YJL005W; YJL005W.
GeneIDi853452.
KEGGisce:YJL005W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12057 Genomic DNA. Translation: AAA34549.1.
Z49280 Genomic DNA. Translation: CAA89295.1.
X87611 Genomic DNA. Translation: CAA60917.1.
X03449 Genomic DNA. Translation: CAA27175.1.
BK006943 Genomic DNA. Translation: DAA08786.1.
PIRiS56776. OYBY.
RefSeqiNP_012529.3. NM_001181439.3.

3D structure databases

ProteinModelPortaliP08678.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33752. 66 interactors.
DIPiDIP-2317N.
IntActiP08678. 15 interactors.
MINTiMINT-364060.

PTM databases

iPTMnetiP08678.

Proteomic databases

MaxQBiP08678.
PRIDEiP08678.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL005W; YJL005W; YJL005W.
GeneIDi853452.
KEGGisce:YJL005W.

Organism-specific databases

EuPathDBiFungiDB:YJL005W.
SGDiS000003542. CYR1.

Phylogenomic databases

GeneTreeiENSGT00440000037833.
HOGENOMiHOG000112124.
InParanoidiP08678.
KOiK01768.
OMAiLRDYAIC.
OrthoDBiEOG092C02M0.

Enzyme and pathway databases

BioCyciYEAST:YJL005W-MONOMER.
ReactomeiR-SCE-199418. Negative regulation of the PI3K/AKT network.

Miscellaneous databases

PROiP08678.

Family and domain databases

Gene3Di3.30.70.1230. 1 hit.
3.60.40.10. 1 hit.
3.80.10.10. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR013716. Adenylate_cyclase_G-a-bd.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR029787. Nucleotide_cyclase.
IPR001932. PPM-type_phosphatase_dom.
IPR000159. RA_dom.
[Graphical view]
PfamiPF08509. Ad_cyc_g-alpha. 1 hit.
PF00211. Guanylate_cyc. 1 hit.
PF13855. LRR_8. 4 hits.
PF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00789. Ad_cyc_g-alpha. 1 hit.
SM00044. CYCc. 1 hit.
SM00369. LRR_TYP. 11 hits.
SM00332. PP2Cc. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 3 hits.
SSF55073. SSF55073. 2 hits.
SSF81606. SSF81606. 1 hit.
PROSITEiPS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS51450. LRR. 15 hits.
PS51746. PPM_2. 1 hit.
PS50200. RA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYAA_YEAST
AccessioniPrimary (citable) accession number: P08678
Secondary accession number(s): D6VWH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1995
Last modified: October 5, 2016
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

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.