TRS31_YEAST
ID TRS31_YEAST Reviewed; 283 AA.
AC Q03337; D6VT96;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Trafficking protein particle complex subunit 31;
DE Short=TRAPP subunit 31;
DE AltName: Full=Transport protein particle 31 kDa subunit;
GN Name=TRS31; OrderedLocusNames=YDR472W;
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 FUNCTION, AND 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 [4]
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 [5]
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 [6]
RP IDENTIFICATION BY 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 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. {ECO:0000269|PubMed:11239471,
CC ECO:0000269|PubMed:20375281, ECO:0000269|PubMed:20972447,
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 Q03337; P36149: BET3; NbExp=13; IntAct=EBI-38770, EBI-3567;
CC Q03337; P38334: TRS20; NbExp=4; IntAct=EBI-38770, EBI-19468;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network. Endoplasmic
CC reticulum. Preautophagosomal structure.
CC -!- MISCELLANEOUS: Present with 8350 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; U33050; AAB64914.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12306.1; -; Genomic_DNA.
DR PIR; S69639; S69639.
DR RefSeq; NP_010760.3; NM_001180780.3.
DR PDB; 3CUE; X-ray; 3.70 A; B/H/N/T=1-283.
DR PDB; 7E2C; EM; 4.18 A; G=1-283.
DR PDB; 7E2D; EM; 3.71 A; G=1-283.
DR PDB; 7E8S; EM; 4.36 A; G/R=1-283.
DR PDB; 7E8T; EM; 3.80 A; G=1-283.
DR PDB; 7E93; EM; 6.54 A; G/R=1-283.
DR PDB; 7E94; EM; 4.67 A; G/R=1-283.
DR PDB; 7EA3; EM; 4.31 A; G/T=1-283.
DR PDB; 7KMT; EM; 3.70 A; J=1-283.
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; Q03337; -.
DR SMR; Q03337; -.
DR BioGRID; 32525; 147.
DR ComplexPortal; CPX-1383; TRAPPIII protein complex.
DR ComplexPortal; CPX-1939; TRAPPII protein complex.
DR ComplexPortal; CPX-1940; TRAPPI protein complex.
DR DIP; DIP-1709N; -.
DR IntAct; Q03337; 10.
DR MINT; Q03337; -.
DR STRING; 4932.YDR472W; -.
DR iPTMnet; Q03337; -.
DR MaxQB; Q03337; -.
DR PaxDb; Q03337; -.
DR PRIDE; Q03337; -.
DR EnsemblFungi; YDR472W_mRNA; YDR472W; YDR472W.
DR GeneID; 852083; -.
DR KEGG; sce:YDR472W; -.
DR SGD; S000002880; TRS31.
DR VEuPathDB; FungiDB:YDR472W; -.
DR eggNOG; KOG3315; Eukaryota.
DR GeneTree; ENSGT00390000000976; -.
DR HOGENOM; CLU_073154_0_0_1; -.
DR InParanoid; Q03337; -.
DR OMA; VPELQNK; -.
DR BioCyc; YEAST:G3O-29999-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; Q03337; -.
DR PRO; PR:Q03337; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03337; protein.
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: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 CDD; cd14943; TRAPPC5_Trs31; 1.
DR DisProt; DP00835; -.
DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR InterPro; IPR016696; TRAPP-I_su5.
DR InterPro; IPR007194; TRAPP_component.
DR PANTHER; PTHR20902; PTHR20902; 1.
DR Pfam; PF04051; TRAPP; 1.
DR PIRSF; PIRSF017479; TRAPP_I_complex_Trs31; 1.
DR SUPFAM; SSF111126; SSF111126; 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..283
FT /note="Trafficking protein particle complex subunit 31"
FT /id="PRO_0000211585"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 283 AA; 31722 MW; 857BBA3E03423D42 CRC64;
MSQRIIQPSA SDQQFPGKSD GYEYTVGPKQ AITSEASTTY IPSRIYSESL LFKRQEASLS
AMAFLFQEMI SQLHRTCKTA GDFETKLSDY GHNIGIRLLE LLNFRASVSP SSLPRASAFL
SQNESSSKLS NASNSPGMLA NSSTATSASA NERLQEKQTE SLSNYITKMR RRDLKILDIL
QFIHGTLWSY LFNHVSDDLV KSSERDNEYM IVDNFPTLTQ FIPGENVSCE YFVCGIIKGF
LFNAGFPCGV TAHRMPQGGH SQRTVYLIQF DRQVLDREGL RFG
