ID WDR59_YEAST Reviewed; 1148 AA.
AC Q03897; D6VSB4;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 183.
DE RecName: Full=Maintenance of telomere capping protein 5;
DE AltName: Full=SEH-associated protein 3;
GN Name=MTC5; Synonyms=SEA3; OrderedLocusNames=YDR128W;
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 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 FUNCTION.
RX PubMed=18845848; DOI=10.1534/genetics.108.092577;
RA Addinall S.G., Downey M., Yu M., Zubko M.K., Dewar J., Leake A.,
RA Hallinan J., Shaw O., James K., Wilkinson D.J., Wipat A., Durocher D.,
RA Lydall D.;
RT "A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied
RT cellular processes influencing telomere capping in Saccharomyces
RT cerevisiae.";
RL Genetics 180:2251-2266(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, 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 [7]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, AND FUNCTION.
RX PubMed=21454883; DOI=10.1074/mcp.m110.006478;
RA Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P.,
RA Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C.,
RA Rout M.P., Dargemont C.;
RT "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically
RT associates with the vacuole in Saccharomyces cerevisiae.";
RL Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011).
CC -!- FUNCTION: Component of the SEA complex which coats the vacuolar
CC membrane and is involved in intracellular trafficking, autophagy,
CC response to nitrogen starvation, and amino acid biogenesis. May be
CC involved in telomere capping. {ECO:0000269|PubMed:18845848,
CC ECO:0000269|PubMed:21454883}.
CC -!- SUBUNIT: Component of the SEA complex composed of at least IML1/SEA1,
CC RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1.
CC {ECO:0000269|PubMed:21454883}.
CC -!- INTERACTION:
CC Q03897; Q04491: SEC13; NbExp=5; IntAct=EBI-32422, EBI-16529;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:21454883}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21454883}.
CC -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat WDR59 family. {ECO:0000305}.
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DR EMBL; Z48179; CAA88209.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11974.1; -; Genomic_DNA.
DR PIR; S51855; S51855.
DR RefSeq; NP_010413.3; NM_001180436.3.
DR PDB; 8ADL; EM; 2.95 A; C/Q=1-1148.
DR PDB; 8AE6; EM; 2.70 A; Q=1-1148.
DR PDBsum; 8ADL; -.
DR PDBsum; 8AE6; -.
DR AlphaFoldDB; Q03897; -.
DR SMR; Q03897; -.
DR BioGRID; 32184; 327.
DR ComplexPortal; CPX-3231; SEA complex.
DR DIP; DIP-1825N; -.
DR IntAct; Q03897; 64.
DR MINT; Q03897; -.
DR STRING; 4932.YDR128W; -.
DR iPTMnet; Q03897; -.
DR MaxQB; Q03897; -.
DR PaxDb; 4932-YDR128W; -.
DR PeptideAtlas; Q03897; -.
DR EnsemblFungi; YDR128W_mRNA; YDR128W; YDR128W.
DR GeneID; 851706; -.
DR KEGG; sce:YDR128W; -.
DR AGR; SGD:S000002535; -.
DR SGD; S000002535; MTC5.
DR VEuPathDB; FungiDB:YDR128W; -.
DR eggNOG; KOG0309; Eukaryota.
DR GeneTree; ENSGT00940000171305; -.
DR HOGENOM; CLU_001497_0_0_1; -.
DR InParanoid; Q03897; -.
DR OMA; HRRETCL; -.
DR OrthoDB; 23438at2759; -.
DR BioCyc; YEAST:G3O-29727-MONOMER; -.
DR BioGRID-ORCS; 851706; 6 hits in 10 CRISPR screens.
DR PRO; PR:Q03897; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03897; Protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0035859; C:Seh1-associated complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903432; P:regulation of TORC1 signaling; IDA:ComplexPortal.
DR CDD; cd16488; mRING-H2-C3H3C2_Mio-like; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR006575; RWD_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR049567; WDR59-like.
DR InterPro; IPR049566; WDR59_RTC1-like_RING_Znf.
DR PANTHER; PTHR46170; GATOR COMPLEX PROTEIN WDR59; 1.
DR PANTHER; PTHR46170:SF1; GATOR COMPLEX PROTEIN WDR59; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF00400; WD40; 2.
DR Pfam; PF17120; zf-RING_16; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50908; RWD; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Vacuole; WD repeat.
FT CHAIN 1..1148
FT /note="Maintenance of telomere capping protein 5"
FT /id="PRO_0000253807"
FT REPEAT 63..106
FT /note="WD 1"
FT REPEAT 112..152
FT /note="WD 2"
FT REPEAT 156..195
FT /note="WD 3"
FT REPEAT 199..239
FT /note="WD 4"
FT REPEAT 299..348
FT /note="WD 5"
FT DOMAIN 432..543
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT REGION 963..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:8AE6"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 255..266
FT /evidence="ECO:0007829|PDB:8AE6"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 304..312
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:8AE6"
FT HELIX 342..347
FT /evidence="ECO:0007829|PDB:8AE6"
FT HELIX 401..406
FT /evidence="ECO:0007829|PDB:8AE6"
FT HELIX 430..440
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 442..450
FT /evidence="ECO:0007829|PDB:8AE6"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 455..463
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:8AE6"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:8AE6"
FT HELIX 504..522
FT /evidence="ECO:0007829|PDB:8AE6"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:8AE6"
FT HELIX 530..536
FT /evidence="ECO:0007829|PDB:8AE6"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:8ADL"
FT STRAND 631..637
FT /evidence="ECO:0007829|PDB:8ADL"
FT STRAND 774..779
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 781..783
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 788..791
FT /evidence="ECO:0007829|PDB:8ADL"
FT STRAND 796..799
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 801..814
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 818..830
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 839..845
FT /evidence="ECO:0007829|PDB:8ADL"
FT TURN 848..851
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 852..864
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 868..880
FT /evidence="ECO:0007829|PDB:8ADL"
FT STRAND 998..1001
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 1005..1010
FT /evidence="ECO:0007829|PDB:8ADL"
FT TURN 1020..1022
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 1026..1039
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 1043..1060
FT /evidence="ECO:0007829|PDB:8ADL"
FT STRAND 1080..1082
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 1091..1095
FT /evidence="ECO:0007829|PDB:8ADL"
FT TURN 1099..1101
FT /evidence="ECO:0007829|PDB:8ADL"
FT STRAND 1107..1111
FT /evidence="ECO:0007829|PDB:8ADL"
FT STRAND 1113..1115
FT /evidence="ECO:0007829|PDB:8ADL"
FT STRAND 1118..1120
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 1121..1127
FT /evidence="ECO:0007829|PDB:8ADL"
FT TURN 1128..1130
FT /evidence="ECO:0007829|PDB:8ADL"
FT HELIX 1142..1145
FT /evidence="ECO:0007829|PDB:8ADL"
SQ SEQUENCE 1148 AA; 130946 MW; D6A137FB0FDE2816 CRC64;
MCSSINEGPY NSPTFGKSLS LKVDGGFNAV SINPSGRDIV LASRQGLYII DLDDPFTPPR
WLHHITPWQV ADVQWSPHPA KPYWIVSTSN QKAIIWNLAK SSSNAIEFVL HGHSRAITDI
NFNPQHPDVL ATCSVDTYVH AWDMRSPHRP FYSTSSWRSA ASQVKWNYKD PNVLASSHGN
DIFVWDLRKG STPLCSLKGH VSSVNSIDFN RFKYSEIMSS SNDGTVKFWD YSKSTTESKR
TVTTNFPIWR GRYLPFGEGY CIMPMVGGNN AVYLINLCDD DDSEQNKKTK LQPIYAFKGH
SDRVIDFLWR SRHTCDGDYD DREFQLVTWS KDCDLKLWPI SDSIYGKVNF DRGKRLEEKL
PDYDYCSYNK EPENRENVQK NEFRRLRENF VTTSGLKKNK TNHITWLSGI RMNSATSQED
LFNETKIQNL GEEVSAIGHK FPKVVFEKIS VSTRELCLTL NGPWSEENPD DYIFLRISIN
FPLNYPNKGD PPKFTIEENS NLTMSKRQEI LSNLATIGQK YTDSNLYCLE PCIRFVLGEK
VSLEDIEEGQ EPLLNFDIAD HIDFEELSSL DSSYSDSQNP ENLSSQSDIE SYKEALVFPD
TSNQGLDFGR NLALDTTPVP NGCGSCWTAT GELFCFFANE KKPEKKQNAI IKLSQKEAGV
EKHPFKIEPQ VLYDKEVDSS VITAADELKA RPKRYVDTLG LGGGTNGDSR TYFDDETSSD
DSFDSVADDW DDILRNDIIV RTKIPILRGN FKAFSSVHSE SGKTVESTKK NKNLVISKNF
SSLLSDRKEL ALEYLFMDAT PEGFARNNAL VAEKFDLDEI SHCWQILSDM LIDQSDYDPY
TTIWNNHPMG IKWFIKEAIV YFERQQNLQM LAMLCCVILS ARRKKIPARY YGQELENMEG
TIVFNDNESQ NTSFWKGSDA FSTRSRSSTV TPNFYGNHLR GKNIHGGDNS SIRSDDHHAR
LRTHNTLNGS SKFTEPAQKQ GSRAISSSPF HSRMPDIKVE LLHDDIIEAY EQEDLLHLEV
SDIPKFQTYI YQYSKLLFRW GLPLERVKIL KVSTDFRSSY SSQGIPPNNN KKSPYNGVLT
HWIENNEFGE EKFLARNCNY CDLRVTRSSF ICGNCQHVLH SSCARIWWEI GDECPSGCGC
NCPEMFDA
//
