ID   DOP1_YEAST              Reviewed;        1698 AA.
AC   Q03921; D6VSC4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Protein dopey;
GN   Name=DOP1; OrderedLocusNames=YDR141C; ORFNames=YD9302.17C;
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.
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   FUNCTION.
RX   PubMed=10931277; DOI=10.1046/j.1365-2958.2000.01950.x;
RA   Pascon R.C., Miller B.L.;
RT   "Morphogenesis in Aspergillus nidulans requires Dopey (DopA), a member of a
RT   novel family of leucine zipper-like proteins conserved from yeast to
RT   humans.";
RL   Mol. Microbiol. 36:1250-1264(2000).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH MON2.
RX   PubMed=16219684; DOI=10.1242/jcs.02599;
RA   Efe J.A., Plattner F., Hulo N., Kressler D., Emr S.D., Deloche O.;
RT   "Yeast Mon2p is a highly conserved protein that functions in the cytoplasm-
RT   to-vacuole transport pathway and is required for Golgi homeostasis.";
RL   J. Cell Sci. 118:4751-4764(2005).
RN   [7]
RP   INTERACTION WITH MON2, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=16301316; DOI=10.1074/jbc.m510176200;
RA   Gillingham A.K., Whyte J.R.C., Panic B., Munro S.;
RT   "Mon2, a relative of large Arf exchange factors, recruits Dop1 to the Golgi
RT   apparatus.";
RL   J. Biol. Chem. 281:2273-2280(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Involved in cellular morphogenesis. Required for traffic
CC       between late Golgi and early endosomes, and for the normal structure
CC       and organization of the endoplasmic reticulum.
CC       {ECO:0000269|PubMed:10931277, ECO:0000269|PubMed:16301316}.
CC   -!- SUBUNIT: Interacts with MON2. {ECO:0000269|PubMed:16219684,
CC       ECO:0000269|PubMed:16301316}.
CC   -!- INTERACTION:
CC       Q03921; Q03921: DOP1; NbExp=2; IntAct=EBI-34442, EBI-34442;
CC       Q03921; P48563: MON2; NbExp=5; IntAct=EBI-34442, EBI-28333;
CC       Q03921; P40527: NEO1; NbExp=3; IntAct=EBI-34442, EBI-3137;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16219684,
CC       ECO:0000269|PubMed:16301316}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16219684,
CC       ECO:0000269|PubMed:16301316}. Note=Late Golgi.
CC   -!- MISCELLANEOUS: Present with 2700 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the dopey family. {ECO:0000305}.
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DR   EMBL; Z48179; CAA88223.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11984.1; -; Genomic_DNA.
DR   PIR; S51869; S51869.
DR   RefSeq; NP_010425.1; NM_001180448.1.
DR   AlphaFoldDB; Q03921; -.
DR   BioGRID; 32195; 238.
DR   ComplexPortal; CPX-1028; NEO1-MON2-ARL1-DOP1 membrane remodeling complex.
DR   DIP; DIP-2624N; -.
DR   IntAct; Q03921; 18.
DR   MINT; Q03921; -.
DR   STRING; 4932.YDR141C; -.
DR   iPTMnet; Q03921; -.
DR   MaxQB; Q03921; -.
DR   PaxDb; Q03921; -.
DR   PRIDE; Q03921; -.
DR   EnsemblFungi; YDR141C_mRNA; YDR141C; YDR141C.
DR   GeneID; 851719; -.
DR   KEGG; sce:YDR141C; -.
DR   SGD; S000002548; DOP1.
DR   VEuPathDB; FungiDB:YDR141C; -.
DR   eggNOG; KOG3613; Eukaryota.
DR   GeneTree; ENSGT00390000016421; -.
DR   HOGENOM; CLU_001197_1_0_1; -.
DR   InParanoid; Q03921; -.
DR   OMA; LLIMSCC; -.
DR   BioCyc; YEAST:G3O-29738-MON; -.
DR   PRO; PR:Q03921; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03921; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005768; C:endosome; IDA:SGD.
DR   GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR   GO; GO:0000139; C:Golgi membrane; IDA:HGNC-UCL.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:SGD.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IMP:HGNC-UCL.
DR   GO; GO:0006895; P:Golgi to endosome transport; IMP:HGNC-UCL.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR   GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:SGD.
DR   GO; GO:0098629; P:trans-Golgi network membrane organization; IC:ComplexPortal.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR040314; DOP1.
DR   InterPro; IPR007249; Dopey_N.
DR   PANTHER; PTHR14042; PTHR14042; 1.
DR   Pfam; PF04118; Dopey_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..1698
FT                   /note="Protein dopey"
FT                   /id="PRO_0000190976"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   1698 AA;  194688 MW;  119459CD3785526C CRC64;
     MSLPLKPLTI DSNNKQLDSK QKKFRANVER ALERFDSVTE WADYIASLGT LLKALQSWSP
     KFQNVRYYVP SPYQVSRRLT SSLSPALPAG VHQKTLEVYT YIFEHIGLET LATECNIWIP
     GILPLMTYAS MSVRSHLIEL YDNYILLLPQ TTLRLLIRPL ISSLLPGIDD ESNDFLPLTL
     KLIETLQENL DDDSLFWQTL FLVMTANKGR RLGGLTWLTR KFPSLNAVPH LVNKIKMEAE
     ENPSETETND SHLDRKKRKE EAFKVLLPAA KDLVTPEPGL LIRCLVGCLE DENDILIKRS
     VLDLLLQRLR LDSPVLNVLI TSEDKKLLIM SCCRTTLSKD MSLNRRIWNW LLGPTAGGML
     NNNGGNSMEY TTSVKSANEE SNVYFTKYGL SALLEGLSDL LSEEESVLTA FRISMAVMDR
     WEIGSLVIPE LFIPLLYSSE KFKQNEQIMK TARTFFDNTE TNIIWGKLFQ ELEDIKNLKI
     LDFVLTNFNI GNDEEIIVRH LPLILLTLLA LPSNDKDFDN IYKLQKFSLY NKLLNYIPER
     ALLPLSHSKL KHDDEVSCEE LLAKIRGFYT NVSNPSSILE KENIAERLPP FTTEDLTFLI
     ADLIQKKLLS SLWDLENINE SSKLFIAIFE KIPESEELKG RSHISWSDKK ITQSIFEAIP
     RLCESNNDAK SEEIVGIVEI FGNYLYSRME FIESMKLLKV VMMAVWKSLK DPRHQILGVK
     NLKTLNRFIP SKFIESALVY TFVEEEDISE RLSVLDLLWT QLDSDSNLIR RPLELILGEL
     FDDQNPFYLT VSKWILSILN SGSASRLFYI LTDNILKVNR LEKERLDERD DLDMLTYEFQ
     MLAYVLKTNN GRTRKVFSTE LTSIKSSTIW KNEDVSTYKS LLLVTLMRFL NIKSNTHAKS
     IRSALILLDI LLDGTEQNFK DIVIFLLQMS SKYIAEEGIE PELIAVSLLD IVSKVLRLSH
     DNGIKLDIFD DNAAHLKYID FLVTSVSNMK SPLIVTAYVK LLSESIVYFE NSIFRMILPL
     SASLVQCVQR LFLLEKREGG YYQPIALLLG GLEELLEISH GYLVTEEREG YFSGSNLKGD
     FIQSVVSNVF SSDSSNEESK IQGERDVILQ SFRQVISCCL DIWYWAHNIS CKSNDDSSLD
     ATNHNSYKFK FRSKKLLETL FLLEPLELLE NLISIRSDNT TVTLVHVLDG NKPAITIPHL
     LYGVIIRYNR TASVKFSNRD GSRSSTTKLT KGEPSMLKRL SGESIIAFLF NYVDSVENSA
     MEEFYGDFLL FFREVATNYN LYSDVSLSIL KLVALISGKV SKTQFGEQKR VRREISDVFF
     KYLPNAFINF TNLYRGHPDS FKDLEFVVWR VQYIVNDQIG GDKFNTTLAT IVNQCLTPYI
     KPKSEKTIPG YVLELAAVVS HLGSKVKSWR LLIAELFQND KKLSVIGSDQ TWEKIIYEWS
     IYPENKSKIL NDLLLEIGSK RSSVTPTLIT FNLGSDSEVE YKCQNLLKIS YLLMVSPNDA
     YLLHFSSLIS CIFHYLVSKD IKLKGSCWIL LRVLLLRFSE SHFNDYWSMI SYCLQTNLQE
     FYESLQIQSE VDPQTILQVC KTLDLLLLLN MEGFTSTNEW IFVIDTINCV YKTNSFVALV
     DEIAEFKDYE ITKTDDLELP TTLKDGLPLL RGIHKIERHT QLRSFFQNLS YLHYEKVYGL
     GSVDLYGCGE DLKKDILS