ADY3_YEAST
ID ADY3_YEAST Reviewed; 790 AA.
AC Q07732; D6VRB7;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Accumulates dyads protein 3;
GN Name=ADY3; OrderedLocusNames=YDL239C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 569.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, COMPOSITION OF A SPB COMPLEX, AND INTERACTION WITH SSP1;
RP NUD1; CNM67 AND MPC54.
RX PubMed=11742972; DOI=10.1093/emboj/20.24.6946;
RA Moreno-Borchart A.C., Strasser K., Finkbeiner M.G., Shevchenko A.,
RA Shevchenko A., Knop M.;
RT "Prospore membrane formation linked to the leading edge protein (LEP) coat
RT assembly.";
RL EMBO J. 20:6946-6957(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPO21; NUD1 AND CNM67.
RX PubMed=11973299; DOI=10.1093/genetics/160.4.1439;
RA Nickas M.E., Neiman A.M.;
RT "Ady3p links spindle pole body function to spore wall synthesis in
RT Saccharomyces cerevisiae.";
RL Genetics 160:1439-1450(2002).
CC -!- FUNCTION: Involved in the pathway that organizes the prospore membrane
CC (PSM) during sporulation. Mediates the assembly of the DON1 ring
CC structure at the leading edge of PSM during meiosis II. May constitute
CC a physical link between SSP1-containing PSM precursors and the spindle
CC pole body (SPB) and may facilitate the recruitment of other factors
CC that are required to promote spore wall formation.
CC {ECO:0000269|PubMed:11742972, ECO:0000269|PubMed:11973299}.
CC -!- SUBUNIT: Interacts directly with SSP1. Probable component of a SPB
CC complex composed of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and
CC CNM67. {ECO:0000269|PubMed:11742972, ECO:0000269|PubMed:11973299}.
CC -!- INTERACTION:
CC Q07732; Q08550: MPC54; NbExp=3; IntAct=EBI-33406, EBI-34513;
CC Q07732; Q12411: SPO21; NbExp=5; IntAct=EBI-33406, EBI-36275;
CC Q07732; P38871: SSP1; NbExp=3; IntAct=EBI-33406, EBI-24852;
CC -!- SUBCELLULAR LOCATION: Prospore membrane. Cytoplasm, cytoskeleton,
CC microtubule organizing center, spindle pole body. Note=Localizes to the
CC leading edge, which cover the ring-shape opening of the PSMs during
CC meiosis II. Colocalizes with DON1 to dots in the cytoplasm and at the
CC SPB. Its localization to the PSMs but not to the SPBs depends on SSP1.
CC -!- DEVELOPMENTAL STAGE: Meiosis-specific. Expressed from 3 to 9 hours
CC after induction of sporulation. Not expressed during mitosis.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:11742972}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z74287; CAA98819.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11627.2; -; Genomic_DNA.
DR PIR; S67803; S67803.
DR RefSeq; NP_010042.2; NM_001180299.2.
DR AlphaFoldDB; Q07732; -.
DR SMR; Q07732; -.
DR BioGRID; 31872; 81.
DR DIP; DIP-1811N; -.
DR IntAct; Q07732; 43.
DR MINT; Q07732; -.
DR STRING; 4932.YDL239C; -.
DR PaxDb; Q07732; -.
DR PRIDE; Q07732; -.
DR EnsemblFungi; YDL239C_mRNA; YDL239C; YDL239C.
DR GeneID; 851359; -.
DR KEGG; sce:YDL239C; -.
DR SGD; S000002398; ADY3.
DR VEuPathDB; FungiDB:YDL239C; -.
DR GeneTree; ENSGT00940000176826; -.
DR HOGENOM; CLU_355332_0_0_1; -.
DR InParanoid; Q07732; -.
DR OMA; NRSESWA; -.
DR BioCyc; YEAST:G3O-29616-MON; -.
DR PRO; PR:Q07732; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07732; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0070056; C:prospore membrane leading edge; IDA:SGD.
DR GO; GO:0005816; C:spindle pole body; IDA:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IMP:SGD.
DR InterPro; IPR021750; Sid4-like.
DR Pfam; PF11778; SID; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Meiosis;
KW Membrane; Phosphoprotein; Reference proteome; Sporulation.
FT CHAIN 1..790
FT /note="Accumulates dyads protein 3"
FT /id="PRO_0000064461"
FT REGION 8..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..328
FT /evidence="ECO:0000255"
FT COILED 361..430
FT /evidence="ECO:0000255"
FT COILED 477..498
FT /evidence="ECO:0000255"
FT COILED 540..658
FT /evidence="ECO:0000255"
FT COMPBIAS 15..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 569
FT /note="E -> G (in Ref. 1; CAA98819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 91812 MW; 46F17474F30FD3D9 CRC64;
MNHWLAFLNK PESLKEQNSD CDQQGEMRHV TDGTLTKSPE SKPFRERRSQ TWIDSEVPTS
TEKSNVQESI SSDIISKLSN RRSRRNRSES WAGSEASSPS GNISTLENAT EKNTLKSPNK
FLQRGGLPTV GIGSQALSPA GKPSTLGNVS PGKFTTYKVH NSIEVNRFSS TPTKLLTNPH
KVAAISNDEH YVVSNESLEE NIEVAHLENV FRSSKTPDEE QSEYMKLGEI RLSSSSYGGS
ISKENSLPKV LDELQSQNEE IKALRQKLEE KDDRIQELEE LNSMNDAKLQ RIEDLQKEFH
NERKAASKRL NIVQDRFRKE IKKIREEKIT DFQNKNASKK EKNEVTSAKT KCKAFSQRNI
LVSELYRKQK QILNLQQEND KFLKDINESN NSIVKLRSEV EILKSNLQLS QDENKKLHDN
GSFYEKRLND VYSYMQNLSL FEKDLGKFIL EEMKCGHSPS MFQNGFAKLY PDFQDIKNLE
NMEQYKQLKG KIELLEKNDR IRLEKIISVF KLINERLHFM QQQHSHKIKY LQKEALTKEQ
QFRLEKRRWH DILNLKEENF QKLKSELKEK LILSEKIQKN AEDKLNDYMN EHQEIVEKLQ
NQALIASRWS TQIQESENTH KKITDELAGK QSEILKLEET ILSLKEDVFQ EKLNLKKLYG
DPSTELNFET VGKSFPHITK EKYDSLGLDI LTDLTYVQSQ NLIKNLLIVL DIPLKTFLKI
VPTIVIQLRC ELTLLTKFAN DLNLKVFGKQ LDFKSRRKVA MNEFLNNHDI AEVKHPLEYD
LQALFKYFFS
