BET3_YEAST
ID BET3_YEAST Reviewed; 193 AA.
AC P36149; D6VXC9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Trafficking protein particle complex subunit BET3;
DE Short=TRAPP subunit BET3;
DE AltName: Full=Transport protein particle 22 kDa subunit;
GN Name=BET3; OrderedLocusNames=YKR068C;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=8590804; DOI=10.1091/mbc.6.12.1769;
RA Rossi G., Kolstad K., Stone S., Palluault F., Ferro-Novick S.;
RT "BET3 encodes a novel hydrophilic protein that acts in conjunction with
RT yeast SNAREs.";
RL Mol. Biol. Cell 6:1769-1780(1995).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE TRAPP II COMPLEX, AND CHARACTERIZATION.
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 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 MUTAGENESIS OF CYS-80, AND PALMITOYLATION AT CYS-80.
RX PubMed=15692564; DOI=10.1038/sj.emboj.7600565;
RA Turnbull A.P., Kummel D., Prinz B., Holz C., Schultchen J., Lang C.,
RA Niesen F.H., Hofmann K.P., Delbruck H., Behlke J., Muller E.C., Jarosch E.,
RA Sommer T., Heinemann U.;
RT "Structure of palmitoylated BET3: insights into TRAPP complex assembly and
RT membrane localization.";
RL EMBO J. 24:875-884(2005).
RN [9]
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).
RN [10]
RP IDENTIFICATION IN THE TRAPP III COMPLEX, SUBCELLULAR LOCATION, AND FUNCTION
RP OF THE TRAPP III COMPLEX.
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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the TRAPP I, TRAPP II and TRAPP III complexes
CC which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP
CC I plays a key role in the late stages of endoplasmic reticulum to Golgi
CC traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III
CC plays a role in autophagosome formation. Required for sporulation. Has
CC a role late in meiosis following DNA replication.
CC {ECO:0000269|PubMed:11239471, ECO:0000269|PubMed:20375281,
CC ECO:0000269|PubMed:20972447, ECO:0000269|PubMed:8590804,
CC ECO:0000269|PubMed:9564032}.
CC -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein particle) I
CC complex composed of BET3, BET5, TRS20, TRS23, TRS31 and TRS33. Part of
CC the multisubunit TRAPP (transport protein particle) II complex composed
CC of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS85, TRS120 and
CC TRS130. Part of the multisubunit TRAPP (transport protein particle) III
CC complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33 and TRS85.
CC {ECO:0000269|PubMed:11239471, ECO:0000269|PubMed:20375281,
CC ECO:0000269|PubMed:20972447, ECO:0000269|PubMed:9564032}.
CC -!- INTERACTION:
CC P36149; Q03630: BET5; NbExp=11; IntAct=EBI-3567, EBI-3580;
CC P36149; P38334: TRS20; NbExp=11; IntAct=EBI-3567, EBI-19468;
CC P36149; Q03784: TRS23; NbExp=11; IntAct=EBI-3567, EBI-19474;
CC P36149; Q03337: TRS31; NbExp=13; IntAct=EBI-3567, EBI-38770;
CC P36149; Q99394: TRS33; NbExp=9; IntAct=EBI-3567, EBI-19480;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network. Endoplasmic
CC reticulum. Preautophagosomal structure.
CC -!- MISCELLANEOUS: Present with 2370 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z28293; CAA82147.1; -; Genomic_DNA.
DR EMBL; AY557896; AAS56222.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09219.1; -; Genomic_DNA.
DR PIR; S38144; S38144.
DR RefSeq; NP_012994.1; NM_001179858.1.
DR PDB; 3CUE; X-ray; 3.70 A; D/E/J/K/P/Q/V/W=1-193.
DR PDB; 7E2C; EM; 4.18 A; C/F=1-193.
DR PDB; 7E2D; EM; 3.71 A; C/F=1-191.
DR PDB; 7E8S; EM; 4.36 A; C/F/N/Q=1-193.
DR PDB; 7E8T; EM; 3.80 A; C/F=1-193.
DR PDB; 7E93; EM; 6.54 A; C/F/N/Q=1-193.
DR PDB; 7E94; EM; 4.67 A; C/F/N/Q=1-193.
DR PDB; 7EA3; EM; 4.31 A; C/F/P/S=1-193.
DR PDB; 7KMT; EM; 3.70 A; F/I=1-193.
DR PDBsum; 3CUE; -.
DR PDBsum; 7E2C; -.
DR PDBsum; 7E2D; -.
DR PDBsum; 7E8S; -.
DR PDBsum; 7E8T; -.
DR PDBsum; 7E93; -.
DR PDBsum; 7E94; -.
DR PDBsum; 7EA3; -.
DR PDBsum; 7KMT; -.
DR AlphaFoldDB; P36149; -.
DR SMR; P36149; -.
DR BioGRID; 34199; 494.
DR ComplexPortal; CPX-1383; TRAPPIII protein complex.
DR ComplexPortal; CPX-1939; TRAPPII protein complex.
DR ComplexPortal; CPX-1940; TRAPPI protein complex.
DR DIP; DIP-1710N; -.
DR IntAct; P36149; 27.
DR MINT; P36149; -.
DR STRING; 4932.YKR068C; -.
DR iPTMnet; P36149; -.
DR SwissPalm; P36149; -.
DR MaxQB; P36149; -.
DR PaxDb; P36149; -.
DR PRIDE; P36149; -.
DR EnsemblFungi; YKR068C_mRNA; YKR068C; YKR068C.
DR GeneID; 853942; -.
DR KEGG; sce:YKR068C; -.
DR SGD; S000001776; BET3.
DR VEuPathDB; FungiDB:YKR068C; -.
DR eggNOG; KOG3330; Eukaryota.
DR GeneTree; ENSGT00390000003880; -.
DR HOGENOM; CLU_087110_0_0_1; -.
DR InParanoid; P36149; -.
DR OMA; WTSDNKQ; -.
DR BioCyc; YEAST:G3O-32034-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR EvolutionaryTrace; P36149; -.
DR PRO; PR:P36149; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36149; protein.
DR GO; GO:0033106; C:cis-Golgi network membrane; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; IC:ComplexPortal.
DR GO; GO:0030008; C:TRAPP complex; IBA:GO_Central.
DR GO; GO:1990070; C:TRAPPI protein complex; IDA:SGD.
DR GO; GO:1990071; C:TRAPPII protein complex; IDA:SGD.
DR GO; GO:1990072; C:TRAPPIII protein complex; IDA: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; IDA:ComplexPortal.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP: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 CDD; cd14942; TRAPPC3_bet3; 1.
DR InterPro; IPR016721; Bet3.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR007194; TRAPP_component.
DR PANTHER; PTHR13048; PTHR13048; 1.
DR Pfam; PF04051; TRAPP; 1.
DR PIRSF; PIRSF018293; TRAPP_I_complex_Bet3; 1.
DR SUPFAM; SSF111126; SSF111126; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Lipoprotein; Palmitate; Reference proteome; Transport.
FT CHAIN 1..193
FT /note="Trafficking protein particle complex subunit BET3"
FT /id="PRO_0000211578"
FT LIPID 80
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:15692564"
FT MUTAGEN 80
FT /note="C->S: Loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:15692564"
SQ SEQUENCE 193 AA; 22129 MW; C802D8A3563DE82B CRC64;
MVSTTQSRSL KAMGEEIWKN KTEKINTELF TLTYGSIVAQ LCQDYERDFN KVNDHLYSMG
YNIGCRLIED FLARTALPRC ENLVKTSEVL SKCAFKIFLN ITPNITNWSH NKDTFSLILD
ENPLADFVEL PMDAMKSLWY SNILCGVLKG SLEMVQLDCD VWFVSDILRG DSQTEIKVKL
NRILKDEIPI GED
