Reviewed, UniProtKB/Swiss-Prot Q07732 (ADY3_YEAST)

Names and origin

Protein names

Recommended name:
    Accumulates dyads protein 3

Gene names

Name:	ADY3
Ordered Locus Names:	YDL239C

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	790 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the pathway that organizes the prospore membrane (PSM) during sporulation. Mediates the assembly of the DON1 ring structure at the leading edge of PSM during meiosis II. May constitute a physical link between SSP1-containing PSM precursors and the spindle pole body (SPB) and may facilitate the recruitment of other factors that are required to promote spore wall formation. Ref.2 Ref.3
Subunit structure	Interacts directly with SSP1. Probable component of a SPB complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67. Ref.2 Ref.3
Subcellular location	Prospore membrane. Cytoplasm › cytoskeleton › spindle pole body. Note: Localizes to the leading edge, which cover the ring-shape opening of the PSMs during meiosis II. Colocalizes with DON1 to dots in the cytoplasm and at the SPB. Its localization to the PSMs but not to the SPBs depends on SSP1. Ref.2 Ref.3
Developmental stage	Meiosis-specific. Expressed from 3 to 9 hours after induction of sporulation. Not expressed during mitosis.
Post-translational modification	Phosphorylated. Ref.2

Ontologies

Keywords
Biological process	Cell cycle Cell division Meiosis Sporulation
Cellular component	Cytoplasm Cytoskeleton Membrane Nucleus
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ascospore wall assembly Ref.3 Inferred from mutant phenotype. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW meiosis Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion inheritance Inferred from genetic interaction. Source: SGD protein complex assembly Ref.3 Inferred from mutant phenotype. Source: SGD
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-KW prospore membrane Ref.2 Ref.3 Inferred from direct assay. Source: SGD spindle pole body Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Ref.2 Ref.3 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P40325	1	EBI-33406,EBI-23614
	Q08001	1	EBI-33406,EBI-30998
APE1	P14904	1	EBI-33406,EBI-2571
ATG17	Q06410	1	EBI-33406,EBI-30856
BBP1	Q12365	1	EBI-33406,EBI-3448
CAT2	P32796	1	EBI-33406,EBI-3935
CHA4	P43634	2	EBI-33406,EBI-4566
CNM67	P53865	2	EBI-33406,EBI-29172
DON1	Q05610	1	EBI-33406,EBI-31191
FRT1	Q99332	1	EBI-33406,EBI-35986
FRT2	P39734	1	EBI-33406,EBI-20631
HSP26	P15992	1	EBI-33406,EBI-8555
KGD2	P19262	1	EBI-33406,EBI-12464
MPC54	Q08550	1	EBI-33406,EBI-34513
MUK1	Q02866	1	EBI-33406,EBI-32646
NGG1	P32494	1	EBI-33406,EBI-2192
NIP29	P33419	1	EBI-33406,EBI-12041
NUD1	P32336	2	EBI-33406,EBI-12361
SPO21	Q12411	3	EBI-33406,EBI-36275
SSP1	P38871	3	EBI-33406,EBI-24852

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 790	790	Accumulates dyads protein 3		PRO_0000064461
Regions
	Coiled coil	241 – 328	88	Potential
	Coiled coil	361 – 430	70	Potential
	Coiled coil	477 – 498	22	Potential
	Coiled coil	540 – 658	119	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q07732-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 6F8D43B78F38928F	FASTA	790	91,740
	10 20 30 40 50 60 MNHWLAFLNK PESLKEQNSD CDQQGEMRHV TDGTLTKSPE SKPFRERRSQ TWIDSEVPTS 70 80 90 100 110 120 TEKSNVQESI SSDIISKLSN RRSRRNRSES WAGSEASSPS GNISTLENAT EKNTLKSPNK 130 140 150 160 170 180 FLQRGGLPTV GIGSQALSPA GKPSTLGNVS PGKFTTYKVH NSIEVNRFSS TPTKLLTNPH 190 200 210 220 230 240 KVAAISNDEH YVVSNESLEE NIEVAHLENV FRSSKTPDEE QSEYMKLGEI RLSSSSYGGS 250 260 270 280 290 300 ISKENSLPKV LDELQSQNEE IKALRQKLEE KDDRIQELEE LNSMNDAKLQ RIEDLQKEFH 310 320 330 340 350 360 NERKAASKRL NIVQDRFRKE IKKIREEKIT DFQNKNASKK EKNEVTSAKT KCKAFSQRNI 370 380 390 400 410 420 LVSELYRKQK QILNLQQEND KFLKDINESN NSIVKLRSEV EILKSNLQLS QDENKKLHDN 430 440 450 460 470 480 GSFYEKRLND VYSYMQNLSL FEKDLGKFIL EEMKCGHSPS MFQNGFAKLY PDFQDIKNLE 490 500 510 520 530 540 NMEQYKQLKG KIELLEKNDR IRLEKIISVF KLINERLHFM QQQHSHKIKY LQKEALTKEQ 550 560 570 580 590 600 QFRLEKRRWH DILNLKEENF QKLKSELKGK LILSEKIQKN AEDKLNDYMN EHQEIVEKLQ 610 620 630 640 650 660 NQALIASRWS TQIQESENTH KKITDELAGK QSEILKLEET ILSLKEDVFQ EKLNLKKLYG 670 680 690 700 710 720 DPSTELNFET VGKSFPHITK EKYDSLGLDI LTDLTYVQSQ NLIKNLLIVL DIPLKTFLKI 730 740 750 760 770 780 VPTIVIQLRC ELTLLTKFAN DLNLKVFGKQ LDFKSRRKVA MNEFLNNHDI AEVKHPLEYD 790 LQALFKYFFS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Prospore membrane formation linked to the leading edge protein (LEP) coat assembly." Moreno-Borchart A.C., Strasser K., Finkbeiner M.G., Shevchenko A., Shevchenko A., Knop M. EMBO J. 20:6946-6957(2001) [PubMed: 11742972] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, COMPOSITION OF A SPB COMPLEX, INTERACTION WITH SSP1; NUD1; CNM67 AND MPC54.
[3]	"Ady3p links spindle pole body function to spore wall synthesis in Saccharomyces cerevisiae." Nickas M.E., Neiman A.M. Genetics 160:1439-1450(2002) [PubMed: 11973299] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPO21; NUD1 AND CNM67.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z74287 Genomic DNA. Translation: CAA98819.1.
PIR	S67803.
RefSeq	NP_010042.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1811N.
IntAct	Q07732. 46 interactions.
STRING	Q07732.
Genome annotation databases
Ensembl	YDL239C; YDL239C; YDL239C; Saccharomyces cerevisiae. [Genome view]
GeneID	851359.
KEGG	sce:YDL239C.
NMPDR	fig|4932.3.peg.775.
Organism-specific databases
CYGD	YDL239c.
SGD	S000002398. ADY3.
Phylogenomic databases
OMA	EEKFDYT
OrthoDB	EOG9RR81M
Gene expression databases
ArrayExpress	Q07732.
Genevestigator	Q07732.
GermOnline	YDL239C. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other Resources
NextBio	968459.

Entry information

Entry name

ADY3_YEAST

Accession

Primary (citable) accession number: Q07732

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	November 1, 1996
Last modified:	November 24, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)