Reviewed, UniProtKB/Swiss-Prot P08678 (CYAA_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	2026 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 21 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
Gene Ontology (GO)
Biological process	G-protein signaling, coupled to cAMP nucleotide second messenger Ref.1 Inferred from genetic interaction. Source: SGD Ras protein signal transduction Ref.1 Inferred from genetic interaction. Source: SGD cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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 Ref.1 Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-5364,EBI-5364

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	80	Ras-associating
	Repeat	815 – 838	24	LRR 1
	Repeat	842 – 862	21	LRR 2
	Repeat	863 – 885	23	LRR 3
	Repeat	886 – 908	23	LRR 4
	Repeat	910 – 931	22	LRR 5
	Repeat	932 – 955	24	LRR 6
	Repeat	957 – 976	20	LRR 7
	Repeat	977 – 999	23	LRR 8
	Repeat	1001 – 1016	16	LRR 9
	Repeat	1017 – 1040	24	LRR 10
	Repeat	1042 – 1062	21	LRR 11
	Repeat	1063 – 1086	24	LRR 12
	Repeat	1088 – 1109	22	LRR 13
	Repeat	1110 – 1132	23	LRR 14
	Repeat	1134 – 1156	23	LRR 15
	Repeat	1188 – 1209	22	LRR 16
	Repeat	1210 – 1232	23	LRR 17
	Repeat	1233 – 1256	24	LRR 18
	Repeat	1258 – 1280	23	LRR 19
	Repeat	1285 – 1308	24	LRR 20
	Repeat	1319 – 1344	26	LRR 21
	Domain	1369 – 1625	257	PP2C-like
	Domain	1668 – 1805	138	Guanylate cyclase
Sites
	Metal binding	1673	1	Magnesium By similarity
	Metal binding	1716	1	Magnesium By similarity
Amino acid modifications
	Modified residue	240	1	Phosphoserine Ref.9
	Modified residue	241	1	Phosphoserine Ref.8 Ref.10
	Modified residue	287	1	Phosphothreonine Ref.10
	Modified residue	288	1	Phosphoserine Ref.10
	Modified residue	292	1	Phosphoserine Ref.10
	Modified residue	371	1	Phosphothreonine Ref.9 Ref.10 Ref.6
	Modified residue	376	1	Phosphothreonine Ref.7
	Modified residue	389	1	Phosphothreonine Ref.7
	Modified residue	433	1	Phosphoserine Ref.10
	Modified residue	435	1	Phosphoserine Ref.10
	Modified residue	486	1	Phosphoserine Ref.8 Ref.10
	Modified residue	487	1	Phosphoserine Ref.9 Ref.10 Ref.7
	Modified residue	527	1	Phosphoserine Ref.10
	Modified residue	559	1	Phosphoserine Ref.10
	Modified residue	562	1	Phosphoserine Ref.10
	Modified residue	1647	1	Phosphothreonine Ref.9
Experimental info
	Mutagenesis	1651	1	T → D: Attenuation of the response to Ras proteins. Ref.5
	Mutagenesis	1651	1	T → I: Weak Ras-independent activity. Ref.5
	Sequence conflict	262	1	S → L in AAA34549. Ref.1
	Sequence conflict	548	1	S → L in AAA34549. Ref.1
	Sequence conflict	592	1	D → H in AAA34549. Ref.1
	Sequence conflict	709	1	R → I in AAA34549. Ref.1
	Sequence conflict	962	1	L → P in AAA34549. Ref.1
	Sequence conflict	1388	1	L → S in AAA34549. Ref.1
	Sequence conflict	1427	1	E → D in CAA27175. Ref.3
	Sequence conflict	1461	1	A → T in CAA27175. Ref.3
	Sequence conflict	1566	1	A → S in AAA34549. Ref.1
	Sequence conflict	1735	1	V → G in AAA34549. Ref.1
	Sequence conflict	1956	1	I → V in CAA27175. Ref.3
	Sequence conflict	1996	1	C → F in AAA34549. Ref.1
	Sequence conflict	2009 – 2026	18	NVVDE…KDLST → MLLTNFYKWLRTQRIYQLEF CS in CAA27175. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P08678-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: BEAB7419AB6989D0	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

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. , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., 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]	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.
[4]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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
EMBLGenBankDDBJ	M12057 Genomic DNA. Translation: AAA34549.1. Z49280 Genomic DNA. Translation: CAA89295.1. X87611 Genomic DNA. Translation: CAA60917.1. X03449 Genomic DNA. Translation: CAA27175.1.
PIR	OYBY. S56776.
RefSeq	NP_012529.1.
3D structure databases
HSSP	HSSP built from PDB template 1FX2 based on UniProtKB Q99279.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2317N.
IntAct	P08678. 13 interactions.
STRING	P08678.
Proteomic databases
PeptideAtlas	P08678.
PRIDE	P08678.
Genome annotation databases
Ensembl	YJL005W; YJL005W; YJL005W; Saccharomyces cerevisiae. [Genome view]
GeneID	853452.
GenomeReviews	Gene locus YJL005W in contig Y13136_GR.
KEGG	sce:YJL005W.
NMPDR	fig|4932.3.peg.3502.
Organism-specific databases
CYGD	YJL005w.
SGD	S000003542. CYR1.
Phylogenomic databases
HOGENOM	P08678.
OMA	NANIFLP.
Enzyme and pathway databases
BRENDA	4.6.1.1. 250.
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-related. IPR014045. PP2C_N. 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.
Pfam	PF08509. Ad_cyc_g-alpha. 1 hit. PF00211. Guanylate_cyc. 1 hit. PF00560. LRR_1. 6 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]
PROSITE	PS50125. GUANYLATE_CYCLASE_2. 1 hit. PS50200. RA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	974014.

Entry information

Entry name

CYAA_YEAST

Accession

Primary (citable) accession number: P08678

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)