TRS85_YEAST
ID TRS85_YEAST Reviewed; 698 AA.
AC P46944; D6VS94; Q04563;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Trafficking protein particle complex III-specific subunit 85;
DE Short=TRAPP III-specific subunit 85;
DE AltName: Full=Muddled meiosis protein 1;
DE AltName: Full=Sporulation protein GSG1;
DE AltName: Full=Transport protein particle 85 kDa subunit;
GN Name=TRS85; Synonyms=GSG1, MUM1; OrderedLocusNames=YDR108W;
GN ORFNames=YD9727.04;
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], AND FUNCTION.
RX PubMed=8619313; DOI=10.1002/yea.320111205;
RA Kaytor M.D., Livingston D.M.;
RT "GSG1, a yeast gene required for sporulation.";
RL Yeast 11:1147-1155(1995).
RN [2]
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 [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 IDENTIFICATION IN THE TRAPP II COMPLEX.
RX PubMed=9564032; DOI=10.1093/emboj/17.9.2494;
RA Sacher M., Jiang Y., Barrowman J., Scarpa A., Burston J., Zhang L.,
RA Schieltz D., Yates J.R. III, Abeliovich H., Ferro-Novick S.;
RT "TRAPP, a highly conserved novel complex on the cis-Golgi that mediates
RT vesicle docking and fusion.";
RL EMBO J. 17:2494-2503(1998).
RN [5]
RP FUNCTION.
RX PubMed=10727015; DOI=10.1078/s0171-9335(04)70009-6;
RA Sacher M., Barrowman J., Schieltz D., Yates J.R. III, Ferro-Novick S.;
RT "Identification and characterization of five new subunits of TRAPP.";
RL Eur. J. Cell Biol. 79:71-80(2000).
RN [6]
RP FUNCTION OF THE TRAPP II COMPLEX, IDENTIFICATION IN THE TRAPP II COMPLEX,
RP FUNCTION OF THE TRAPP I COMPLEX, IDENTIFICATION IN THE TRAPP I COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11239471; DOI=10.1016/s1097-2765(01)00190-3;
RA Sacher M., Barrowman J., Wang W., Horecka J., Zhang Y., Pypaert M.,
RA Ferro-Novick S.;
RT "TRAPP I implicated in the specificity of tethering in ER-to-Golgi
RT transport.";
RL Mol. Cell 7:433-442(2001).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=16874038; DOI=10.4161/auto.1.1.1512;
RA Nazarko T.Y., Huang J., Nicaud J.M., Klionsky D.J., Sibirny A.A.;
RT "Trs85 is required for macroautophagy, pexophagy and cytoplasm to vacuole
RT targeting in Yarrowia lipolytica and Saccharomyces cerevisiae.";
RL Autophagy 1:37-45(2005).
RN [9]
RP FUNCTION.
RX PubMed=16079147; DOI=10.1074/jbc.m501701200;
RA Meiling-Wesse K., Epple U.D., Krick R., Barth H., Appelles A., Voss C.,
RA Eskelinen E.L., Thumm M.;
RT "Trs85 (Gsg1), a component of the TRAPP complexes, is required for the
RT organization of the preautophagosomal structure during selective autophagy
RT via the Cvt pathway.";
RL J. Biol. Chem. 280:33669-33678(2005).
RN [10]
RP IDENTIFICATION BY 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).
RN [11]
RP IDENTIFICATION IN THE TRAPP III COMPLEX, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=20375281; DOI=10.1073/pnas.1000063107;
RA Lynch-Day M.A., Bhandari D., Menon S., Huang J., Cai H., Bartholomew C.R.,
RA Brumell J.H., Ferro-Novick S., Klionsky D.J.;
RT "Trs85 directs a Ypt1 GEF, TRAPPIII, to the phagophore to promote
RT autophagy.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7811-7816(2010).
CC -!- FUNCTION: Specific subunit of the TRAPP III complex that acts as an
CC autophagy-specific guanine nucleotide exchange factor (GEF) for YPT1.
CC TRS85 directs the TRAPP III complex to the phagophore assembly site
CC (PAS) that is involved in autophagosome formation. Required for
CC membrane expansion during autophagy and the CVT pathway. Required for
CC sporulation. Has a role late in meiosis following DNA replication.
CC {ECO:0000269|PubMed:10727015, ECO:0000269|PubMed:11239471,
CC ECO:0000269|PubMed:16079147, ECO:0000269|PubMed:16874038,
CC ECO:0000269|PubMed:20375281, ECO:0000269|PubMed:8619313}.
CC -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein particle)
CC III complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33 and
CC TRS85. {ECO:0000269|PubMed:11239471, ECO:0000269|PubMed:20375281,
CC ECO:0000269|PubMed:9564032}.
CC -!- INTERACTION:
CC P46944; P38334: TRS20; NbExp=6; IntAct=EBI-19492, EBI-19468;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000269|PubMed:11239471, ECO:0000269|PubMed:20375281}.
CC -!- MISCELLANEOUS: Present with 8760 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRS85 family. {ECO:0000305}.
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DR EMBL; U26674; AAB03360.1; -; Genomic_DNA.
DR EMBL; Z48758; CAA88662.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11954.1; -; Genomic_DNA.
DR PIR; S52674; S52674.
DR RefSeq; NP_010393.3; NM_001180416.3.
DR PDB; 7KMT; EM; 3.70 A; B=1-698.
DR PDBsum; 7KMT; -.
DR AlphaFoldDB; P46944; -.
DR SMR; P46944; -.
DR BioGRID; 32166; 494.
DR ComplexPortal; CPX-1383; TRAPPIII protein complex.
DR DIP; DIP-1354N; -.
DR IntAct; P46944; 9.
DR MINT; P46944; -.
DR STRING; 4932.YDR108W; -.
DR iPTMnet; P46944; -.
DR MaxQB; P46944; -.
DR PaxDb; P46944; -.
DR PRIDE; P46944; -.
DR EnsemblFungi; YDR108W_mRNA; YDR108W; YDR108W.
DR GeneID; 851686; -.
DR KEGG; sce:YDR108W; -.
DR SGD; S000002515; TRS85.
DR VEuPathDB; FungiDB:YDR108W; -.
DR eggNOG; KOG1938; Eukaryota.
DR GeneTree; ENSGT00390000000568; -.
DR HOGENOM; CLU_015504_0_0_1; -.
DR InParanoid; P46944; -.
DR OMA; KLADWSM; -.
DR BioCyc; YEAST:G3O-29710-MON; -.
DR PRO; PR:P46944; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P46944; protein.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000407; C:phagophore assembly site; IDA:SGD.
DR GO; GO:1990072; C:TRAPPIII protein complex; IDA:SGD.
DR GO; GO:0000045; P:autophagosome assembly; IMP:SGD.
DR GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR GO; GO:0071255; P:Cvt vesicle assembly; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IMP:SGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR024420; TRAPP_III_complex_Trs85.
DR PANTHER; PTHR12975; PTHR12975; 1.
DR Pfam; PF12739; TRAPPC-Trs85; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Meiosis; Reference proteome; Sporulation;
KW Transport.
FT CHAIN 1..698
FT /note="Trafficking protein particle complex III-specific
FT subunit 85"
FT /id="PRO_0000065642"
FT REGION 82..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 277
FT /note="A -> R (in Ref. 1; AAB03360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 80495 MW; 31652762E1CD55D9 CRC64;
MVFSYEHYMN LLFHLDNSKE TVPPEIAKRI ISNAIAPVIT VTSTPLFDKH IQETYKVDSL
YMLLRFFGGC VSDRDQANEA KVGQHEHEVC DASDSTDSIP KNKNLEVPNL SKKGSRSRSN
SLFQRDSTQS QYIRFTRPLG DLIETRDAND MLFNYHSLEV FLDNYLKLVA ANTDEMVPHN
LLKKSIYHSF FSLAISSTNN LSPYETFNHP ILSLIALDIS NGEVYEDARD LLVNFKNLNH
NTENFPIFMN TNEMLPVFLL CYNDDSQEEF EKCQALAKKL KKQLFVESIL LALWKDSFIY
DENSVIQLHQ PVMSSLEEIL FFLQAPTQTT LSLALINSIY DMLDYLVYDL MIPFMKRKVS
FWEETILQPR KSLFNGAKFF KKFMNKNPVN GNHQHNSLTR DSQGNEYFAS SSSEFLMRKL
ADWSMMLSDF KTAYSTYESL MDDLDAFPKY LASCIEWCAV SLLMGAQSIV TVKMIKNDIN
PLIERALATY ENCSRIQRGK GKESNSLDVT EPVRSYETRC MILASELFLS LSNTWTSTPY
AIQYLETILD ECKLGPCSQI MVWERLSDCY NLRVDPRIKH RVGAMKKDAK DTEDLRGEHK
YSTDHFTDED ILSEGLTRRR KAAFFRLIAA KKWAEQKQWR QVSWCLKDIE STYSEIKFLH
GNGLILSKLK NQLNLKDVDS APRPSEKNLT RTSVSFIG
