ID   TRS33_YEAST             Reviewed;         268 AA.
AC   Q99394; D6W2H4;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 172.
DE   RecName: Full=Trafficking protein particle complex subunit 33;
DE            Short=TRAPP subunit 33;
DE   AltName: Full=Transport protein particle 33 kDa subunit;
GN   Name=TRS33; OrderedLocusNames=YOR115C; ORFNames=O3251, YOR3251C;
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].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8904341;
RX   DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA   Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA   Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT   "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT   Saccharomyces cerevisiae reveals 30 open reading frames.";
RL   Yeast 12:281-288(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9200815;
RX   DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA   Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA   Schwager C., Paces V., Sander C., Ansorge W.;
RT   "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL   Yeast 13:655-672(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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   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).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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}.
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       Q99394; P36149: BET3; NbExp=9; IntAct=EBI-19480, EBI-3567;
CC       Q99394; P15303: SEC23; NbExp=3; IntAct=EBI-19480, EBI-16584;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network. Endoplasmic
CC       reticulum. Preautophagosomal structure.
CC   -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X90518; CAA62124.1; -; Genomic_DNA.
DR   EMBL; X94335; CAA64035.1; -; Genomic_DNA.
DR   EMBL; Z75023; CAA99313.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10890.1; -; Genomic_DNA.
DR   PIR; S61003; S61003.
DR   RefSeq; NP_014758.3; NM_001183534.3.
DR   PDB; 7E2C; EM; 4.18 A; B=1-268.
DR   PDB; 7E2D; EM; 3.71 A; B=1-268.
DR   PDB; 7E8S; EM; 4.36 A; B/M=1-268.
DR   PDB; 7E8T; EM; 3.80 A; B=1-268.
DR   PDB; 7E93; EM; 6.54 A; B/M=1-268.
DR   PDB; 7E94; EM; 4.67 A; B/M=1-268.
DR   PDB; 7EA3; EM; 4.31 A; B/O=1-268.
DR   PDB; 7KMT; EM; 3.70 A; E=1-268.
DR   PDB; 7U05; EM; 3.70 A; E/e=1-268.
DR   PDB; 7U06; EM; 4.20 A; E/e=1-268.
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; Q99394; -.
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; Q99394; -.
DR   BioGRID; 34511; 144.
DR   ComplexPortal; CPX-1383; TRAPPIII protein complex.
DR   ComplexPortal; CPX-1939; TRAPP II complex.
DR   ComplexPortal; CPX-1940; TRAPPI protein complex.
DR   DIP; DIP-1712N; -.
DR   IntAct; Q99394; 11.
DR   MINT; Q99394; -.
DR   STRING; 4932.YOR115C; -.
DR   iPTMnet; Q99394; -.
DR   MaxQB; Q99394; -.
DR   PaxDb; 4932-YOR115C; -.
DR   PeptideAtlas; Q99394; -.
DR   EnsemblFungi; YOR115C_mRNA; YOR115C; YOR115C.
DR   GeneID; 854282; -.
DR   KEGG; sce:YOR115C; -.
DR   AGR; SGD:S000005641; -.
DR   SGD; S000005641; TRS33.
DR   VEuPathDB; FungiDB:YOR115C; -.
DR   eggNOG; KOG3316; Eukaryota.
DR   GeneTree; ENSGT00390000012948; -.
DR   HOGENOM; CLU_076409_2_0_1; -.
DR   InParanoid; Q99394; -.
DR   OMA; PYLEIPC; -.
DR   OrthoDB; 20246at2759; -.
DR   BioCyc; YEAST:G3O-33644-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; 854282; 3 hits in 10 CRISPR screens.
DR   PRO; PR:Q99394; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q99394; Protein.
DR   GO; GO:0005801; C:cis-Golgi network; 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; IDA:SGD.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
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; NAS:ComplexPortal.
DR   GO; GO:0016236; P:macroautophagy; NAS:ComplexPortal.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; IGI:SGD.
DR   GO; GO:0065003; P:protein-containing complex assembly; IGI:SGD.
DR   GO; GO:0031503; P:protein-containing complex localization; IGI:SGD.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; NAS:ComplexPortal.
DR   CDD; cd14944; TRAPPC6A_Trs33; 1.
DR   Gene3D; 3.30.1380.20; Trafficking protein particle complex subunit 3; 1.
DR   InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR   InterPro; IPR007194; TRAPP_component.
DR   InterPro; IPR037992; TRAPPC6/Trs33.
DR   PANTHER; PTHR12817:SF0; GEO08327P1; 1.
DR   PANTHER; PTHR12817; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 6B; 1.
DR   Pfam; PF04051; TRAPP; 1.
DR   SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Autophagy; Endoplasmic reticulum;
KW   ER-Golgi transport; Golgi apparatus; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..268
FT                   /note="Trafficking protein particle complex subunit 33"
FT                   /id="PRO_0000211589"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   268 AA;  30749 MW;  2480F69D7A48D363 CRC64;
     MSSTHSNNVG HPQSSPQGPL TEQQRAQQQY QIFENSLPKV SQSVYQMLLN EMVPLAMGIE
     RQISGDVISS DSNVTSENGN INNMIKRLKI EEHHTVDIIR SHNLIHELYK ADEEEKEKVL
     ARLRNIGFQI GLKLSELLIF SNNPNLKFKE MDLLLIMKFI CRDVWKQIFG KQIDNLKTNH
     RGTFYLLDYD YRPIQSFSLE EDAKNEELKM IEPFLEIPVG IIRGVLSSLG YSSEEVICLA
     SFIDRPTDRP KTAFPKGVSF HVQVTMPQ
//