BET5_YEAST
ID BET5_YEAST Reviewed; 159 AA.
AC Q03630; D6W0K6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Trafficking protein particle complex subunit BET5;
DE Short=TRAPP subunit BET5;
DE AltName: Full=Transport protein particle 18 kDa subunit;
GN Name=BET5; OrderedLocusNames=YML077W;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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=9611195; DOI=10.1093/genetics/149.2.833;
RA Jiang Y., Scarpa A., Zhang L., Stone S., Feliciano E., Ferro-Novick S.;
RT "A high copy suppressor screen reveals genetic interactions between BET3
RT and a new gene. Evidence for a novel complex in ER-to-Golgi transport.";
RL Genetics 149:833-841(1998).
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 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 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 [8]
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).
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:9611195}.
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 Q03630; P36149: BET3; NbExp=11; IntAct=EBI-3580, EBI-3567;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network. Endoplasmic
CC reticulum. Preautophagosomal structure.
CC -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET5 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z46373; CAA86501.1; -; Genomic_DNA.
DR EMBL; AY557760; AAS56086.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09820.1; -; Genomic_DNA.
DR PIR; S48820; S48820.
DR RefSeq; NP_013634.1; NM_001182436.1.
DR PDB; 3CUE; X-ray; 3.70 A; C/I/O/U=1-159.
DR PDB; 7E2C; EM; 4.18 A; D=1-159.
DR PDB; 7E2D; EM; 3.71 A; D=1-159.
DR PDB; 7E8S; EM; 4.36 A; D/O=1-159.
DR PDB; 7E8T; EM; 3.80 A; D=1-159.
DR PDB; 7E93; EM; 6.54 A; D/O=1-159.
DR PDB; 7E94; EM; 4.67 A; D/O=1-159.
DR PDB; 7EA3; EM; 4.31 A; D/Q=1-159.
DR PDB; 7KMT; EM; 3.70 A; G=1-159.
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; Q03630; -.
DR SMR; Q03630; -.
DR BioGRID; 35064; 452.
DR ComplexPortal; CPX-1383; TRAPPIII protein complex.
DR ComplexPortal; CPX-1939; TRAPPII protein complex.
DR ComplexPortal; CPX-1940; TRAPPI protein complex.
DR DIP; DIP-4528N; -.
DR IntAct; Q03630; 7.
DR STRING; 4932.YML077W; -.
DR MaxQB; Q03630; -.
DR PaxDb; Q03630; -.
DR PRIDE; Q03630; -.
DR EnsemblFungi; YML077W_mRNA; YML077W; YML077W.
DR GeneID; 854898; -.
DR KEGG; sce:YML077W; -.
DR SGD; S000004542; BET5.
DR VEuPathDB; FungiDB:YML077W; -.
DR eggNOG; KOG3368; Eukaryota.
DR GeneTree; ENSGT00940000153761; -.
DR HOGENOM; CLU_053380_4_0_1; -.
DR InParanoid; Q03630; -.
DR OMA; HYFETPT; -.
DR BioCyc; YEAST:G3O-32669-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR EvolutionaryTrace; Q03630; -.
DR PRO; PR:Q03630; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03630; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:ComplexPortal.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IC:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; IC:ComplexPortal.
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; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR007233; TRAPPC.
DR PANTHER; PTHR23249; PTHR23249; 1.
DR Pfam; PF04099; Sybindin; 1.
DR SMART; SM01399; Sybindin; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Reference proteome; Transport.
FT CHAIN 1..159
FT /note="Trafficking protein particle complex subunit BET5"
FT /id="PRO_0000211565"
SQ SEQUENCE 159 AA; 18434 MW; 4821217270F516E9 CRC64;
MGIYSFWIFD RHCNCIFDRE WTLASNSASG TINSKQNEED AKLLYGMIFS LRSITQKLSK
GSVKNDIRSI STGKYRVHTY CTASGLWFVL LSDFKQQSYT QVLQYIYSHI YVKYVSNNLL
SPYDFAENEN EMRGQGTRKI TNRNFISVLE SFLAPMVNQ
