TRS65_YEAST
ID TRS65_YEAST Reviewed; 560 AA.
AC P32893; D6VUU9;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Trafficking protein particle complex II-specific subunit 65;
DE Short=TRAPP II-specific subunit 65;
DE AltName: Full=Beta-glucan synthesis-associated protein TRS65;
DE AltName: Full=Killer toxin-resistance protein 11;
DE AltName: Full=Transport protein particle 65 kDa subunit;
GN Name=TRS65; Synonyms=KRE11; OrderedLocusNames=YGR166W;
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].
RX PubMed=8462845; DOI=10.1093/genetics/133.4.837;
RA Brown J.L., Kossaczka Z., Jiang B., Bussey H.;
RT "A mutational analysis of killer toxin resistance in Saccharomyces
RT cerevisiae identifies new genes involved in cell wall (1-->6)-beta-glucan
RT synthesis.";
RL Genetics 133:837-849(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION OF THE TRAPP II COMPLEX, IDENTIFICATION IN THE TRAPP II COMPLEX,
RP AND 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [9]
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TRS120 AND TRS130.
RX PubMed=17475775; DOI=10.1091/mbc.e07-03-0221;
RA Liang Y., Morozova N., Tokarev A.A., Mulholland J.W., Segev N.;
RT "The role of Trs65 in the Ypt/Rab guanine nucleotide exchange factor
RT function of the TRAPP II complex.";
RL Mol. Biol. Cell 18:2533-2541(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393 AND SER-398, AND
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 [13]
RP IDENTIFICATION IN THE TRAP II COMPLEX, AND FUNCTION OF THE TRAP II COMPLEX.
RX PubMed=20972447; DOI=10.1038/nsmb.1914;
RA Yip C.K., Berscheminski J., Walz T.;
RT "Molecular architecture of the TRAPPII complex and implications for vesicle
RT tethering.";
RL Nat. Struct. Mol. Biol. 17:1298-1304(2010).
CC -!- FUNCTION: Specific subunit of the TRAPP II complex, a highly conserved
CC vesicle tethering complex that functions in the late Golgi as a guanine
CC nucleotide exchanger (GEF) for the Golgi YPT1 GTPase. TRS65 plays a
CC role in the YPT GEF activity of TRAPP II in concert with the two other
CC TRAPP II-specific subunits TRS120 and TRS130. Involved in cell wall
CC (1-->6)-beta-glucan synthesis. {ECO:0000269|PubMed:11239471,
CC ECO:0000269|PubMed:17475775, ECO:0000269|PubMed:20972447}.
CC -!- PATHWAY: Glycan metabolism; beta-glucan biosynthesis.
CC -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein particle) II
CC complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65,
CC TRS120 and TRS130. Interacts directly with TRS120 and TRS130.
CC {ECO:0000269|PubMed:11239471, ECO:0000269|PubMed:17475775,
CC ECO:0000269|PubMed:20972447, ECO:0000269|PubMed:9564032}.
CC -!- INTERACTION:
CC P32893; Q03660: TRS130; NbExp=3; IntAct=EBI-9900, EBI-19461;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, cis-Golgi network.
CC -!- MISCELLANEOUS: Present with 1660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L10667; AAA34727.1; -; Genomic_DNA.
DR EMBL; Z72951; CAA97191.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08260.1; -; Genomic_DNA.
DR PIR; S42158; S42158.
DR RefSeq; NP_011682.1; NM_001181295.1.
DR PDB; 7E2C; EM; 4.18 A; K=1-559.
DR PDB; 7E2D; EM; 3.71 A; K=1-560.
DR PDB; 7E8S; EM; 4.36 A; K/V=1-560.
DR PDB; 7E8T; EM; 3.80 A; K=1-560.
DR PDB; 7E93; EM; 6.54 A; K/V=1-560.
DR PDB; 7E94; EM; 4.67 A; K/V=1-560.
DR PDB; 7EA3; EM; 4.31 A; K/X=1-560.
DR PDBsum; 7E2C; -.
DR PDBsum; 7E2D; -.
DR PDBsum; 7E8S; -.
DR PDBsum; 7E8T; -.
DR PDBsum; 7E93; -.
DR PDBsum; 7E94; -.
DR PDBsum; 7EA3; -.
DR AlphaFoldDB; P32893; -.
DR SMR; P32893; -.
DR BioGRID; 33418; 338.
DR ComplexPortal; CPX-1939; TRAPPII protein complex.
DR DIP; DIP-5104N; -.
DR IntAct; P32893; 10.
DR MINT; P32893; -.
DR STRING; 4932.YGR166W; -.
DR iPTMnet; P32893; -.
DR MaxQB; P32893; -.
DR PaxDb; P32893; -.
DR PRIDE; P32893; -.
DR EnsemblFungi; YGR166W_mRNA; YGR166W; YGR166W.
DR GeneID; 853076; -.
DR KEGG; sce:YGR166W; -.
DR SGD; S000003398; TRS65.
DR VEuPathDB; FungiDB:YGR166W; -.
DR eggNOG; ENOG502QSDT; Eukaryota.
DR HOGENOM; CLU_042571_0_0_1; -.
DR InParanoid; P32893; -.
DR OMA; VMNNGYN; -.
DR BioCyc; YEAST:G3O-30864-MON; -.
DR UniPathway; UPA00636; -.
DR PRO; PR:P32893; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32893; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:1990071; C:TRAPPII protein complex; IDA:SGD.
DR GO; GO:0051274; P:beta-glucan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IGI:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IGI:SGD.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IC:ComplexPortal.
DR InterPro; IPR024662; Trs65.
DR PANTHER; PTHR28159; PTHR28159; 1.
DR Pfam; PF12735; Trs65; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Cytoplasm; Golgi apparatus;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..560
FT /note="Trafficking protein particle complex II-specific
FT subunit 65"
FT /id="PRO_0000084328"
FT REGION 164..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 560 AA; 63368 MW; 9039A2CEBB1F8316 CRC64;
MECFVPLRCD LDGSNIEQLR QSHLSRKFII FDEQLNLWLW FQGNSQENKR FVLQNMIILI
NEAQVTRTST IDDYFTQVEN NENLWRLKND CCSKILFKSN VVMNNGYNNQ IKFVFEYKSV
DANFNNQDSL QDPQAKYTLD KYSSEEILPS FEPVYSWSSA ATKSSKNTNN HLEKNNRATH
RVSSKNSEVH EADVSRNPNT FTLKLQYPIF SLLNMRLRNI SLKSEHCILS SLDFQTSKAS
EQLTKKFIYP QEHNSFLKLN FQEISYKLID GTSQIELDPI CPLKVPLTAF SYDSISATFK
LVLLPKSTQP HRVKITLAYE LELHPNLKLP VRTSWETEVT LKRSMPISST SSQYSSNNNN
TNHSASFNGA ANNVNSGGLA NLRLGGVSSS RFSLGAASTT SLVNSKLSNV KFKFINSNIK
VIKGEKFTMR LQIINSSSSP LDLVVYYNNT INPIPSANNV RNSNGINNCG MNNGTIPNSP
LTLENQYQLH NKYRKIAEGI ILLSNDYKIP VVPPRETYFA DLRFIGIMSG YYGTLSGLKV
LDLNTNELIE VGNGASVLIQ
