WDR59_YEAST
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 03-AUG-2022, entry version 175.
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}.
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; 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 AlphaFoldDB; Q03897; -.
DR SMR; Q03897; -.
DR BioGRID; 32184; 320.
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; Q03897; -.
DR PRIDE; Q03897; -.
DR EnsemblFungi; YDR128W_mRNA; YDR128W; YDR128W.
DR GeneID; 851706; -.
DR KEGG; sce:YDR128W; -.
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; HDACIPF; -.
DR BioCyc; YEAST:G3O-29727-MON; -.
DR PRO; PR:Q03897; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03897; protein.
DR GO; GO:0097042; C:extrinsic component of fungal-type vacuolar membrane; IDA:SGD.
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 Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR006575; RWD-domain.
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 SMART; SM00591; RWD; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 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 Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW 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"
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
