Adenylate cyclase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P08678 (CYAA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Adenylate cyclase
EC=4.6.1.1

Alternative name(s):
ATP pyrophosphate-lyase
Adenylyl cyclase

Gene names

Name:	CYR1
Synonyms:	CDC35, HSR1, SRA4
Ordered Locus Names:	YJL005W
ORF Names:	J1401

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	2026 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Enzyme regulation	The presence of GTP-bound RAS2 protein is required in order to elicit a magnesium-dependent adenylyl cyclase activity.
Sequence similarities	Belongs to the adenylyl cyclase class-3 family. Contains 1 guanylate cyclase domain. Contains 20 LRR (leucine-rich) repeats. Contains 1 PP2C-like domain. Contains 1 Ras-associating domain.

Ontologies

Keywords
Biological process	cAMP biosynthesis
Domain	Leucine-rich repeat Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	intracellular signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: SGD plasma membrane Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Inferred from direct assay Ref.1. Source: SGD magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2026

2026

Adenylate cyclase

PRO_0000195731

Regions

Domain

676 – 755

Ras-associating

Repeat

815 – 838

LRR 1

Repeat

842 – 862

LRR 2

Repeat

863 – 885

LRR 3

Repeat

886 – 908

LRR 4

Repeat

910 – 931

LRR 5

Repeat

932 – 955

LRR 6

Repeat

957 – 976

LRR 7

Repeat

977 – 999

LRR 8

Repeat

1001 – 1016

LRR 9

Repeat

1017 – 1040

LRR 10

Repeat

1042 – 1062

LRR 11

Repeat

1063 – 1086

LRR 12

Repeat

1088 – 1109

LRR 13

Repeat

1110 – 1132

LRR 14

Repeat

1134 – 1156

LRR 15

Repeat

1188 – 1209

LRR 16

Repeat

1210 – 1232

LRR 17

Repeat

1233 – 1256

LRR 18

Repeat

1258 – 1280

LRR 19

Repeat

1285 – 1308

LRR 20

Domain

1369 – 1625

257

PP2C-like

Domain

1668 – 1805

138

Guanylate cyclase

Sites

Metal binding

1673

Magnesium By similarity

Metal binding

1716

Magnesium By similarity

Amino acid modifications

Modified residue

240

Phosphoserine Ref.10

Modified residue

241

Phosphoserine Ref.9 Ref.11

Modified residue

287

Phosphothreonine Ref.11

Modified residue

288

Phosphoserine Ref.11

Modified residue

292

Phosphoserine Ref.11

Modified residue

371

Phosphothreonine Ref.7 Ref.10 Ref.11

Modified residue

376

Phosphothreonine Ref.8

Modified residue

389

Phosphothreonine Ref.8

Modified residue

433

Phosphoserine Ref.11

Modified residue

435

Phosphoserine Ref.11

Modified residue

486

Phosphoserine Ref.9 Ref.11

Modified residue

487

Phosphoserine Ref.8 Ref.10 Ref.11

Modified residue

527

Phosphoserine Ref.11

Modified residue

559

Phosphoserine Ref.11

Modified residue

562

Phosphoserine Ref.11

Modified residue

1647

Phosphothreonine Ref.10

Experimental info

Mutagenesis

1651

T → D: Attenuation of the response to Ras proteins. Ref.6

Mutagenesis

1651

T → I: Weak Ras-independent activity. Ref.6

Sequence conflict

262

S → L in AAA34549. Ref.1

Sequence conflict

548

S → L in AAA34549. Ref.1

Sequence conflict

592

D → H in AAA34549. Ref.1

Sequence conflict

709

R → I in AAA34549. Ref.1

Sequence conflict

962

L → P in AAA34549. Ref.1

Sequence conflict

1388

L → S in AAA34549. Ref.1

Sequence conflict

1427

E → D in CAA27175. Ref.4

Sequence conflict

1461

A → T in CAA27175. Ref.4

Sequence conflict

1566

A → S in AAA34549. Ref.1

Sequence conflict

1735

V → G in AAA34549. Ref.1

Sequence conflict

1956

I → V in CAA27175. Ref.4

Sequence conflict

1996

C → F in AAA34549. Ref.1

Sequence conflict

2009 – 2026

NVVDE…KDLST → MLLTNFYKWLRTQRIYQLEF CS in CAA27175. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P08678 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: BEAB7419AB6989D0
Show »

FASTA

2,026

227,834

        10         20         30         40         50         60 
MSSKPDTGSE ISGPQRQEEQ EQQIEQSSPT EANDRSIHDE VPKVKKRHEQ NSGHKSRRNS 

        70         80         90        100        110        120 
AYSYYSPRSL SMTKSRESIT PNGMDDVSIS NVEHPRPTEP KIKRGPYLLK KTLSSLSMTS 

       130        140        150        160        170        180 
ANSTHDDNKD HGYALNSSKT HNYTSTHNHH DGHHDHHHVQ FFPNRKPSLA ETLFKRFSGS 

       190        200        210        220        230        240 
NSHDGNKSGK ESKVANLSLS TVNPAPANRK PSKDSTLSNH LADNVPSTLR RKVSSLVRGS 

       250        260        270        280        290        300 
SVHDINNGIA DKQIRPKAVA QSENTLHSSD VPNSKRSHRK SFLLGSTSSS SSRRGSNVSS 

       310        320        330        340        350        360 
MTNSDSASMA TSGSHVLQHN VSNVSPTTKS KDSVNSESAD HTNNKSEKVT PEYNENIPEN 

       370        380        390        400        410        420 
SNSDNKREAT TPTIETPISC KPSLFRLDTN LEDVTDITKT VPPTAVNSTL NSTHGTETAS 

       430        440        450        460        470        480 
PKTVIMPEGP RKSVSMADLS VAAAAPNGEF TSTSNDRSQW VAPQSWDVET KRKKTKPKGR 

       490        500        510        520        530        540 
SKSRRSSIDA DELDPMSPGP PSKKDSRHHH DRKDNESMVT AGDSNSSFVD ICKENVPNDS 

       550        560        570        580        590        600 
KTALDTKSVN RLKSNLAMSP PSIRYAPSNL DGDYDTSSTS SSLPSSSISS EDTSSCSDSS 

       610        620        630        640        650        660 
SYTNAYMEAN REQDNKTPIL NKTKSYTKKF TSSSVNMNSP DGAQSSGLLL QDEKDDEVEC 

       670        680        690        700        710        720 
QLEHYYKDFS DLDPKRHYAI RIFNTDDTFT TLSCTPATTV EEIIPALKRK FNITAQGNFQ 

       730        740        750        760        770        780 
ISLKVGKLSK ILRPTSKPIL IERKLLLLNG YRKSDPLHIM GIEDLSFVFK FLFHPVTPSH 

       790        800        810        820        830        840 
FTPEQEQRIM RSEFVHVDLR NMDLTTPPII FYQHTSEIES LDVSNNANIF LPLEFIESSI 

       850        860        870        880        890        900 
KLLSLRMVNI RASKFPSNIT KAYKLVSLEL QRNFIRKVPN SIMKLSNLTI LNLQCNELES 

       910        920        930        940        950        960 
LPAGFVELKN LQLLDLSSNK FMHYPEVINY CTNLLQIDLS YNKIQSLPQS TKYLVKLAKM 

       970        980        990       1000       1010       1020 
NLSHNKLNFI GDLSEMTDLR TLNLRYNRIS SIKTNASNLQ NLFLTDNRIS NFEDTLPKLR 

      1030       1040       1050       1060       1070       1080 
ALEIQENPIT SISFKDFYPK NMTSLTLNKA QLSSIPGELL TKLSFLEKLE LNQNNLTRLP 

      1090       1100       1110       1120       1130       1140 
QEISKLTKLV FLSVARNKLE YIPPELSQLK SLRTLDLHSN NIRDFVDGME NLELTSLNIS 

      1150       1160       1170       1180       1190       1200 
SNAFGNSSLE NSFYHNMSYG SKLSKSLMFF IAADNQFDDA MWPLFNCFVN LKVLNLSYNN 

      1210       1220       1230       1240       1250       1260 
FSDVSHMKLE SITELYLSGN KLTTLSGDTV LKWSSLKTLM LNSNQMLSLP AELSNLSQLS 

      1270       1280       1290       1300       1310       1320 
VFDVGANQLK YNISNYHYDW NWRNNKELKY LNFSGNRRFE IKSFISHDID ADLSDLTVLP 

      1330       1340       1350       1360       1370       1380 
QLKVLGLMDV TLNTTKVPDE NVNFRLRTTA SIINGMRYGV ADTLGQRDYV SSRDVTFERF 

      1390       1400       1410       1420       1430       1440 
RGNDDECLLC LHDSKNQNAD YGHNISRIVR DIYDKILIRQ LERYGDETDD NIKTALRFSF 

      1450       1460       1470       1480       1490       1500 
LQLNKEINGM LNSVDNGADV ANLSYADLLS GACSTVIYIR GKKLFAANLG DCMAILSKNN 

      1510       1520       1530       1540       1550       1560 
GDYQTLTKQH LPTKREEYER IRISGGYVNN GKLDGVVDVS RAVGFFDLLP HIHASPDISV 

      1570       1580       1590       1600       1610       1620 
VTLTKADEML IVATHKLWEY MDVDTVCDIA RENSTDPLRA AAELKDHAMA YGCTENITIL 

      1630       1640       1650       1660       1670       1680 
CLALYENIQQ QNRFTLNKNS LMTRRSTFED TTLRRLQPEI SPPTGNLAMV FTDIKSSTFL 

      1690       1700       1710       1720       1730       1740 
WELFPNAMRT AIKTHNDIMR RQLRIYGGYE VKTEGDAFMV AFPTPTSGLT WCLSVQLKLL 

      1750       1760       1770       1780       1790       1800 
DAQWPEEITS VQDGCQVTDR NGNIIYQGLS VRMGIHWGCP VPELDLVTQR MDYLGPMVNK 

      1810       1820       1830       1840       1850       1860 
AARVQGVADG GQIAMSSDFY SEFNKIMKYH ERVVKGKESL KEVYGEEIIG EVLEREIAML 

      1870       1880       1890       1900       1910       1920 
ESIGWAFFDF GEHKLKGLET KELVTIAYPK ILASRHEFAS EDEQSKLINE TMLFRLRVIS 

      1930       1940       1950       1960       1970       1980 
NRLESIMSAL SGGFIELDSR TEGSYIKFNP KVENGIMQSI SEKDALLFFD HVITRIESSV 

      1990       2000       2010       2020 
ALLHLRQQRC SGLEICRNDK TSARSNIFNV VDELLQMVKN AKDLST

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence and characterization of the S. cerevisiae gene encoding adenylate cyclase." Kataoka T., Broek D., Wigler M. Cell 43:493-505(1985) [PubMed: 2934138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	de Haan M., Smits P.H.M., Grivell L.A. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Yeast adenylate cyclase catalytic domain is carboxy terminal." Masson P., Lenzen G., Jacquemin J.M., Danchin A. Curr. Genet. 10:343-352(1986) [PubMed: 3327602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1042-2026.
[6]	"Identification of regulatory residues of the yeast adenylyl cyclase." Feger G., de Vendittis E., Vitelli A., Masturzo P., Zahn R., Verrotti A.C., Kavounis C., Pal G.P., Fasano O. EMBO J. 10:349-359(1991) [PubMed: 1991451] [Abstract] Cited for: MUTAGENESIS OF THR-1651.
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-371, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-376; THR-389 AND SER-487, MASS SPECTROMETRY. Strain: ADR376.
[9]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-486, MASS SPECTROMETRY.
[10]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; THR-371; SER-487 AND THR-1647, MASS SPECTROMETRY.
[11]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; THR-287; SER-288; SER-292; THR-371; SER-433; SER-435; SER-486; SER-487; SER-527; SER-559 AND SER-562, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	OYBY. S56776.
RefSeq	NP_012529.1. NM_001181439.1.
3D structure databases
ProteinModelPortal	P08678.
SMR	P08678. Positions 793-1301, 1356-1626, 1662-1896.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2317N.
IntAct	P08678. 19 interactions.
MINT	MINT-364060.
STRING	P08678.
Proteomic databases
PeptideAtlas	P08678.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YJL005W; YJL005W; YJL005W.
GeneID	853452.
KEGG	sce:YJL005W.
NMPDR	fig\|4932.3.peg.3502.
Organism-specific databases
CYGD	YJL005w.
SGD	S000003542. CYR1.
Phylogenomic databases
eggNOG	fuNOG06104.
GeneTree	EFGT00050000002537.
HOGENOM	HBG397746.
OMA	NANIFLP.
OrthoDB	EOG41CB4C.
Gene expression databases
ArrayExpress	P08678.
Genevestigator	P08678.
GermOnline	YJL005W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001054. A/G_cyclase. IPR013716. Adenylate_cyclase_G-a-bd. IPR001611. Leu-rich_rpt. IPR001932. PP2C-like. IPR000159. Ras-assoc. [Graphical view]
Gene3D	G3DSA:3.30.70.1230. A/G_cyclase. 1 hit. G3DSA:3.60.40.10. PP2C-related. 1 hit.
KO	K01768.
Pfam	PF08509. Ad_cyc_g-alpha. 1 hit. PF00211. Guanylate_cyc. 1 hit. PF00560. LRR_1. 2 hits. PF00481. PP2C. 1 hit. PF00788. RA. 1 hit. [Graphical view]
SMART	SM00789. Ad_cyc_g-alpha. 1 hit. SM00044. CYCc. 1 hit. SM00332. PP2Cc. 1 hit. SM00314. RA. 1 hit. [Graphical view]
SUPFAM	SSF55073. A/G_cyclase. 1 hit. SSF81606. PP2C-related. 1 hit.
PROSITE	PS50125. GUANYLATE_CYCLASE_2. 1 hit. PS51450. LRR. 15 hits. PS50200. RA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	974014.

Entry information

Entry name

CYAA_YEAST

Accession

Primary (citable) accession number: P08678
Secondary accession number(s): D6VWH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	November 1, 1995
Last modified:	December 14, 2011
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

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

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents