DIA2_YEAST
ID DIA2_YEAST Reviewed; 732 AA.
AC Q08496; D6W2E3; O00034; Q7LGN4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protein DIA2;
DE AltName: Full=Digs into agar protein 2;
GN Name=DIA2; OrderedLocusNames=YOR080W; ORFNames=YOR29-31;
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 [GENOMIC DNA].
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
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 [4]
RP DOMAIN, AND FUNCTION.
RX PubMed=10582239; DOI=10.1098/rstb.1999.0497;
RA Willems A.R., Goh T., Taylor L., Chernushevich I., Shevchenko A., Tyers M.;
RT "SCF ubiquitin protein ligases and phosphorylation-dependent proteolysis.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 354:1533-1550(1999).
RN [5]
RP FUNCTION.
RX PubMed=11063681; DOI=10.1093/genetics/156.3.1005;
RA Palecek S.P., Parikh A.S., Kron S.J.;
RT "Genetic analysis reveals that FLO11 upregulation and cell polarization
RT independently regulate invasive growth in Saccharomyces cerevisiae.";
RL Genetics 156:1005-1023(2000).
RN [6]
RP FUNCTION.
RX PubMed=15620357; DOI=10.1016/j.cell.2004.11.052;
RA Bao M.Z., Schwartz M.A., Cantin G.T., Yates J.R. III, Madhani H.D.;
RT "Pheromone-dependent destruction of the Tec1 transcription factor is
RT required for MAP kinase signaling specificity in yeast.";
RL Cell 119:991-1000(2004).
RN [7]
RP FUNCTION.
RX PubMed=15579722; DOI=10.1534/genetics.104.029033;
RA Sarin S., Ross K.E., Boucher L., Green Y., Tyers M., Cohen-Fix O.;
RT "Uncovering novel cell cycle players through the inactivation of securin in
RT budding yeast.";
RL Genetics 168:1763-1771(2004).
RN [8]
RP FUNCTION.
RX PubMed=14993228; DOI=10.1074/jbc.m313746200;
RA Serrano R., Bernal D., Simon E., Arino J.;
RT "Copper and iron are the limiting factors for growth of the yeast
RT Saccharomyces cerevisiae in an alkaline environment.";
RL J. Biol. Chem. 279:19698-19704(2004).
RN [9]
RP INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(DIA2) COMPLEX.
RX PubMed=14747994; DOI=10.1002/prot.10620;
RA Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
RT "Functional interaction of 13 yeast SCF complexes with a set of yeast E2
RT enzymes in vitro.";
RL Proteins 54:455-467(2004).
RN [10]
RP FUNCTION.
RX PubMed=16487579; DOI=10.1016/j.cell.2005.12.036;
RA Pan X., Ye P., Yuan D.S., Wang X., Bader J.S., Boeke J.D.;
RT "A DNA integrity network in the yeast Saccharomyces cerevisiae.";
RL Cell 124:1069-1081(2006).
RN [11]
RP IDENTIFICATION IN THE SCF(DIA2) COMPLEX, AND FUNCTION OF THE SCF(DIA2)
RP COMPLEX.
RX PubMed=16421250; DOI=10.1091/mbc.e05-09-0884;
RA Koepp D.M., Kile A.C., Swaminathan S., Rodriguez-Rivera V.;
RT "The F-box protein Dia2 regulates DNA replication.";
RL Mol. Biol. Cell 17:1540-1548(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP IDENTIFICATION OF INITIATION SITE.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=19913425; DOI=10.1016/j.cub.2009.09.062;
RA Morohashi H., Maculins T., Labib K.;
RT "The amino-terminal TPR domain of Dia2 tethers SCF(Dia2) to the replisome
RT progression complex.";
RL Curr. Biol. 19:1943-1949(2009).
CC -!- FUNCTION: F-box protein component of a SCF (SKP1-CUL1-F-box protein) E3
CC ubiquitin-protein ligase complex which mediates the ubiquitination and
CC subsequent proteasomal degradation of target proteins. Probably
CC recognizes and binds to phosphorylated target proteins (By similarity).
CC The SCF(DIA2) complex is specifically involved in the pheromone induced
CC degradation of phosphorylated TEC1. The SCF(DIA2) complex binds to DNA
CC replication origins. Involved in DNA replication, genome stability, and
CC the control of cell cycle, probably through its association to
CC replication origins to facilitate the ubiquitination of another origin-
CC binding protein. Required for invasive growth and growth under alkaline
CC conditions. {ECO:0000250, ECO:0000269|PubMed:10582239,
CC ECO:0000269|PubMed:11063681, ECO:0000269|PubMed:14993228,
CC ECO:0000269|PubMed:15579722, ECO:0000269|PubMed:15620357,
CC ECO:0000269|PubMed:16421250, ECO:0000269|PubMed:16487579}.
CC -!- SUBUNIT: Component of the SCF(DIA2) complex containing CDC53, SKP1,
CC RBX1 and DIA2. Interacts with SKP1. {ECO:0000269|PubMed:14747994,
CC ECO:0000269|PubMed:16421250}.
CC -!- INTERACTION:
CC Q08496; Q01454: CTF4; NbExp=5; IntAct=EBI-31943, EBI-5209;
CC Q08496; P29469: MCM2; NbExp=4; IntAct=EBI-31943, EBI-10533;
CC Q08496; P25588: MRC1; NbExp=11; IntAct=EBI-31943, EBI-412442;
CC Q08496; P52286: SKP1; NbExp=4; IntAct=EBI-31943, EBI-4090;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DIA2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA94565.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA99273.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA99275.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z70678; CAA94565.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74988; CAA99273.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74989; CAA99275.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006948; DAA10859.2; -; Genomic_DNA.
DR PIR; S66963; S66963.
DR RefSeq; NP_014723.2; NM_001183499.1.
DR PDB; 7PMK; EM; 3.20 A; L=1-732.
DR PDB; 7PMN; EM; 3.20 A; L=1-732.
DR PDBsum; 7PMK; -.
DR PDBsum; 7PMN; -.
DR AlphaFoldDB; Q08496; -.
DR SMR; Q08496; -.
DR BioGRID; 34479; 675.
DR ComplexPortal; CPX-3250; SCF-Dia2 ubiquitin ligase complex.
DR DIP; DIP-6496N; -.
DR IntAct; Q08496; 46.
DR MINT; Q08496; -.
DR STRING; 4932.YOR080W; -.
DR iPTMnet; Q08496; -.
DR PaxDb; Q08496; -.
DR PRIDE; Q08496; -.
DR EnsemblFungi; YOR080W_mRNA; YOR080W; YOR080W.
DR GeneID; 854247; -.
DR KEGG; sce:YOR080W; -.
DR SGD; S000005606; DIA2.
DR VEuPathDB; FungiDB:YOR080W; -.
DR eggNOG; ENOG502QRSD; Eukaryota.
DR HOGENOM; CLU_023422_0_0_1; -.
DR InParanoid; Q08496; -.
DR OMA; ISCKGYL; -.
DR BioCyc; YEAST:G3O-33617-MON; -.
DR PRO; PR:Q08496; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08496; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IGI:SGD.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IC:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IMP:SGD.
DR GO; GO:0032984; P:protein-containing complex disassembly; IMP:SGD.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:SGD.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IDA:ComplexPortal.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF00560; LRR_1; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Leucine-rich repeat; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..732
FT /note="Protein DIA2"
FT /id="PRO_0000233003"
FT REPEAT 15..48
FT /note="TPR 1"
FT REPEAT 78..111
FT /note="TPR 2"
FT REPEAT 113..145
FT /note="TPR 3"
FT DOMAIN 204..251
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 425..449
FT /note="LRR 1"
FT REPEAT 480..505
FT /note="LRR 2"
FT REPEAT 509..532
FT /note="LRR 3"
FT REPEAT 550..574
FT /note="LRR 4"
FT REPEAT 579..602
FT /note="LRR 5"
FT REPEAT 616..637
FT /note="LRR 6"
FT REPEAT 645..669
FT /note="LRR 7"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 280..290
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 356..363
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 369..377
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 485..489
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 496..505
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 546..550
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 554..557
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 565..573
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 579..581
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 599..601
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 609..615
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 632..640
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 661..671
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 684..688
FT /evidence="ECO:0007829|PDB:7PMK"
FT HELIX 697..705
FT /evidence="ECO:0007829|PDB:7PMK"
FT STRAND 708..713
FT /evidence="ECO:0007829|PDB:7PMK"
FT TURN 725..727
FT /evidence="ECO:0007829|PDB:7PMK"
SQ SEQUENCE 732 AA; 85070 MW; 98B610994BA2F803 CRC64;
MSSPGNSGVA IDSTVLKAIE LGTRLFKSGE YLQAKRIFTN ALRVCDSYSQ EQIMRIRNAY
QLDTARPDNK RLYHPRYIKI LDNICACYEK LNDLKSCLDV SQRLLKLEPG NIKCYIRCTR
TLIKLKDWKR AYKTCSRGLQ LCNNDSNHLR QQKQFIKNNM VQKQDGKRSY IDPLEETKIA
KKKKNNNVLE SLPKKKIKGS TKKTDLVGNL PIEILPIIFQ RFTTKELVTL SLVCNKWRDK
ILYHLDCFQE FNLAPINFKN FVKFMDFLQQ NFTRTYRKYI LSQVKVSSRI TSEELRITQL
LFSKMPKCIN IERLILSMPT LTTTQIFKLM VRGGTDFFTR LLELSLMITY RPDKQHELEI
LQTCPLLKKI ELIFVNSLVP IFDGNNSVGR DGSFNVMARH TNMQISTADN DEQGIVEEKV
IYSELEKITL ICDKKKIKNF PLCRALLRGQ FPLLQKLTIT GVTFPMNNQD IMNFQWLLNF
PDLKELWIED NDNCELSKFL QLLKFSNVWK NLEKLTFREN KLYPIVNLDE DQPVTNDDEV
PSMLFYKENL QNLEKLDLMG TSISGSALTR LCEQEYLDGR KLRSLNIGNC PNIQFPNNHA
HTARMILDVN AVLKRLSKLE EINLSHLSSL NDSTMKSFII NVPFLENLKR LDISHNFEIT
GISIYEFLKK FQMDHDNEAG GQPLAYLNID GCSQVSHITV NMIRAQNLVT QVDCVYERDV
WRKFGINSYS YS
