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   27-MAR-2024, entry version 159.
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   PDB; 7U05; EM; 3.70 A; J/j=1-283.
DR   PDB; 7U06; EM; 4.20 A; J/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   PDBsum; 7U05; -.
DR   PDBsum; 7U06; -.
DR   AlphaFoldDB; Q03337; -.
DR   EMDB; EMD-22928; -.
DR   EMDB; EMD-26254; -.
DR   EMDB; EMD-26255; -.
DR   EMDB; EMD-30954; -.
DR   EMDB; EMD-30955; -.
DR   EMDB; EMD-31021; -.
DR   EMDB; EMD-31022; -.
DR   EMDB; EMD-31027; -.
DR   EMDB; EMD-31028; -.
DR   EMDB; EMD-31038; -.
DR   SMR; Q03337; -.
DR   BioGRID; 32525; 153.
DR   ComplexPortal; CPX-1383; TRAPPIII protein complex.
DR   ComplexPortal; CPX-1939; TRAPP II complex.
DR   ComplexPortal; CPX-1940; TRAPPI protein complex.
DR   DIP; DIP-1709N; -.
DR   IntAct; Q03337; 10.
DR   MINT; Q03337; -.
DR   STRING; 4932.YDR472W; -.
DR   GlyGen; Q03337; 16 sites, 1 O-linked glycan (16 sites).
DR   iPTMnet; Q03337; -.
DR   MaxQB; Q03337; -.
DR   PaxDb; 4932-YDR472W; -.
DR   PeptideAtlas; Q03337; -.
DR   EnsemblFungi; YDR472W_mRNA; YDR472W; YDR472W.
DR   GeneID; 852083; -.
DR   KEGG; sce:YDR472W; -.
DR   AGR; SGD:S000002880; -.
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; QNRVYTV; -.
DR   OrthoDB; 5471012at2759; -.
DR   BioCyc; YEAST:G3O-29999-MONOMER; -.
DR   Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR   Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   BioGRID-ORCS; 852083; 1 hit in 10 CRISPR screens.
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; NAS: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; NAS:ComplexPortal.
DR   GO; GO:0016236; P:macroautophagy; NAS:ComplexPortal.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; NAS:ComplexPortal.
DR   CDD; cd14943; TRAPPC5_Trs31; 1.
DR   DisProt; DP00835; -.
DR   Gene3D; 3.30.1380.20; Trafficking protein particle complex subunit 3; 1.
DR   InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR   InterPro; IPR016696; TRAPP-I_su5.
DR   InterPro; IPR007194; TRAPP_component.
DR   PANTHER; PTHR20902; 41-2 PROTEIN ANTIGEN-RELATED; 1.
DR   PANTHER; PTHR20902:SF0; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 5; 1.
DR   Pfam; PF04051; TRAPP; 1.
DR   PIRSF; PIRSF017479; TRAPP_I_complex_Trs31; 1.
DR   SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 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
//