WDR6_YEAST
ID WDR6_YEAST Reviewed; 1013 AA.
AC Q08924; D6W3I6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Regulator of Ty1 transposition protein 10;
DE AltName: Full=Endosomal recycling protein 2;
DE AltName: Full=tRNA (guanosine(34)-2'-O)-methyltransferase non-catalytic subunit TRM734;
GN Name=RTT10; Synonyms=ERE2, TRM734; OrderedLocusNames=YPL183C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 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 [4]
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 [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=18202368; DOI=10.1534/genetics.107.082602;
RA Nyswaner K.M., Checkley M.A., Yi M., Stephens R.M., Garfinkel D.J.;
RT "Chromatin-associated genes protect the yeast genome from Ty1 insertional
RT mutagenesis.";
RL Genetics 178:197-214(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RRT2.
RX PubMed=21880895; DOI=10.1091/mbc.e11-05-0440;
RA Shi Y., Stefan C.J., Rue S.M., Teis D., Emr S.D.;
RT "Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the
RT retromer-mediated endosomal recycling pathway.";
RL Mol. Biol. Cell 22:4093-4107(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH TRM7.
RX PubMed=22912484; DOI=10.1261/rna.035287.112;
RA Guy M.P., Podyma B.M., Preston M.A., Shaheen H.H., Krivos K.L.,
RA Limbach P.A., Hopper A.K., Phizicky E.M.;
RT "Yeast Trm7 interacts with distinct proteins for critical modifications of
RT the tRNAPhe anticodon loop.";
RL RNA 18:1921-1933(2012).
CC -!- FUNCTION: Involved in regulation of Ty1 transposition. Also plays a
CC role in the regulation of the retromer complex and is required for the
CC recycling from endosomes of plasma membrane proteins like CAN1 and
CC MUP1. Required together with TRM7 for the methylation of the 2'-O-
CC ribose of nucleotides at position 34 of the tRNA anticodon loop of
CC tRNA(Phe) and tRNA(Leu(UAA)). {ECO:0000269|PubMed:18202368,
CC ECO:0000269|PubMed:21880895, ECO:0000269|PubMed:22912484}.
CC -!- SUBUNIT: Interacts with RRT2. Interacts with TRM7; for 2'-O-methylation
CC of position 34 in substrate tRNAs. {ECO:0000269|PubMed:21880895,
CC ECO:0000269|PubMed:22912484}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome. Note=Recruited to endosomes
CC in cells in which increased recycling of internalized plasma membrane
CC proteins occurs.
CC -!- DISRUPTION PHENOTYPE: Increases Ty1 mobility 31-fold.
CC {ECO:0000269|PubMed:18202368}.
CC -!- MISCELLANEOUS: Present with 3450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR6 family. {ECO:0000305}.
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DR EMBL; Z73539; CAA97892.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11252.1; -; Genomic_DNA.
DR PIR; S65195; S65195.
DR RefSeq; NP_015142.1; NM_001183997.1.
DR PDB; 6JP6; X-ray; 2.70 A; A/C=1-1013.
DR PDB; 6JPL; X-ray; 2.32 A; A/C=1-1013.
DR PDBsum; 6JP6; -.
DR PDBsum; 6JPL; -.
DR AlphaFoldDB; Q08924; -.
DR SASBDB; Q08924; -.
DR SMR; Q08924; -.
DR BioGRID; 36000; 191.
DR IntAct; Q08924; 1.
DR MINT; Q08924; -.
DR STRING; 4932.YPL183C; -.
DR iPTMnet; Q08924; -.
DR MaxQB; Q08924; -.
DR PaxDb; Q08924; -.
DR PRIDE; Q08924; -.
DR EnsemblFungi; YPL183C_mRNA; YPL183C; YPL183C.
DR GeneID; 855919; -.
DR KEGG; sce:YPL183C; -.
DR SGD; S000006104; RTT10.
DR VEuPathDB; FungiDB:YPL183C; -.
DR eggNOG; KOG0974; Eukaryota.
DR GeneTree; ENSGT00420000029923; -.
DR HOGENOM; CLU_002615_0_1_1; -.
DR InParanoid; Q08924; -.
DR OMA; HEGSIFY; -.
DR BioCyc; YEAST:G3O-34077-MON; -.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR Reactome; R-SCE-9696273; RND1 GTPase cycle.
DR PRO; PR:Q08924; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08924; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0032456; P:endocytic recycling; IMP:SGD.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002130; P:wobble position ribose methylation; IMP:SGD.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 9.
DR SUPFAM; SSF50978; SSF50978; 3.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endosome; Reference proteome; Repeat;
KW tRNA processing; WD repeat.
FT CHAIN 1..1013
FT /note="Regulator of Ty1 transposition protein 10"
FT /id="PRO_0000234366"
FT REPEAT 5..41
FT /note="WD 1"
FT REPEAT 45..84
FT /note="WD 2"
FT REPEAT 132..174
FT /note="WD 3"
FT REPEAT 177..216
FT /note="WD 4"
FT REPEAT 219..258
FT /note="WD 5"
FT REPEAT 269..308
FT /note="WD 6"
FT REPEAT 465..504
FT /note="WD 7"
FT REPEAT 586..625
FT /note="WD 8"
FT REPEAT 652..702
FT /note="WD 9"
FT REPEAT 709..747
FT /note="WD 10"
FT REPEAT 761..804
FT /note="WD 11"
FT REPEAT 811..852
FT /note="WD 12"
FT REPEAT 880..928
FT /note="WD 13"
FT REPEAT 934..973
FT /note="WD 14"
FT REPEAT 975..1013
FT /note="WD 15"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 254..267
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 300..304
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 390..399
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 472..478
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 481..487
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 515..524
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 527..534
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 537..546
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 556..565
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 567..576
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 582..588
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 597..600
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 601..607
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 614..620
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 623..630
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 633..640
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 646..649
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 657..662
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 672..676
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 677..684
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 689..695
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 696..698
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 716..719
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 721..728
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 734..740
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 743..745
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 748..754
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 766..773
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 780..786
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 789..797
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 798..801
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 802..810
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 816..824
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 827..834
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 837..843
FT /evidence="ECO:0007829|PDB:6JPL"
FT HELIX 845..847
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 848..852
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 875..879
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 885..892
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 896..905
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 910..917
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 923..931
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 934..937
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 939..945
FT /evidence="ECO:0007829|PDB:6JPL"
FT TURN 946..949
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 950..955
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 958..966
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 969..977
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 981..990
FT /evidence="ECO:0007829|PDB:6JPL"
FT STRAND 999..1013
FT /evidence="ECO:0007829|PDB:6JPL"
SQ SEQUENCE 1013 AA; 114461 MW; 06E192AE4A0EE35F CRC64;
MKDLSHYGPA LCVKFYNDYV LAGYGPFIHV YDYHSATLIN KCRLFHYNKV HGLSLSSEGK
ILAYGARSVT IVELEDVLKK ESLVDFERIN SDWITGATFS FDNLQIYLLT CYNKVLICDL
NCEVLFRKSL GGERSILYSG IIKVFGPDKV YVNAGTVMGG VIIWDLFSET KIHNLLGHEG
SIFYVNLSNN GRYVASCSDD RSIRLWDLET GKQLSVGWSH TARIWNLMFF DNDSKLISVS
EDCTCRVWNI IESRENVAEL SISNVYEVHL IKSIWGVDVK DDEMIAVTSG NDGRLKLIDL
LQLKRHGDEE TSFSLDDIAK QCGDIFEKNE SIKGFQWFSF GVIAITSLGK ILKYSDVTKQ
WKLLLTNEKF NSYPITNGIQ TQNIAVFSNN KSDILLIKFS KDSADIIETE EFHLDELSKT
NNCLVTEYDD DSFLLTLQSP NPREKFVCLE ISLQNLKIKS KHCFNKPENF SSSCLTSFRN
HILVGSRFST LVIYNLLDES EEPFIIRRLS PGDTTTSIEF VEDKDNSAVF SVTNRDGYYV
FIELTKNSLE EGPYRLSYKV LHSNKMMKGF LEGAFFNSKG EYITYGFKSS LFYLYNETNC
YELASEVCGG SHRLWNLAKI TDGHVLMYIK ASRFHLRKIY NSIVPETLEN GVHGREIRDI
SICPVSNTNT NDNFKDGHIF CTASEDTTIK LGYFNNRTGK VQNFWTQRKH VSGLQRCQFI
NHKLMISSSA REELFLWELN DKYNKRPYMT IRQALPVSTN NSDLRIMDFD VKFISQSGDF
LLVTVYSDST IKIWHYRENQ NKFDLIMQGR YKTCCLFNVV FIALKEELLV VISPTDGHLV
VYNITEYVPF SVDPISGDLV DHKLDATISN LPAPVAQLPV HQSGVKSLDY VANATRTSAT
ILTGGDDNGL GLSNLKLDDS NKVTLKTSDF IAAAASSTIT SGMLINGGKE VITTSVDQVI
RAWEITAGKL SLVDKKRTTV ADTGSLEIIS NDEDADSEKT LLIGGVGLSI WKK
