TR120_YEAST
ID TR120_YEAST Reviewed; 1289 AA.
AC Q04183; D6VT39; Q05731;
DT 07-FEB-2006, 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 II-specific subunit 120;
DE Short=TRAPP II-specific subunit 120;
DE AltName: Full=Transport protein particle 120 kDa subunit;
GN Name=TRS120; OrderedLocusNames=YDR407C; ORFNames=D9509.25, ESBP10;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-731.
RA Mai B., Lipp M.;
RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION OF THE TRAPP II COMPLEX, IDENTIFICATION IN THE TRAPP II COMPLEX,
RP AND 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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH TRS65.
RX PubMed=17475775; DOI=10.1091/mbc.e07-03-0221;
RA Liang Y., Morozova N., Tokarev A.A., Mulholland J.W., Segev N.;
RT "The role of Trs65 in the Ypt/Rab guanine nucleotide exchange factor
RT function of the TRAPP II complex.";
RL Mol. Biol. Cell 18:2533-2541(2007).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379 AND SER-387, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
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).
CC -!- FUNCTION: Specific subunit of the TRAPP II complex, a highly conserved
CC vesicle tethering complex that functions in the late Golgi as a guanine
CC nucleotide exchanger (GEF) for the Golgi YPT1 GTPase. TRS120 plays a
CC role in the YPT GEF activity of TRAPP II in concert with the two other
CC TRAPP II-specific subunits TRS65 and TRS130.
CC {ECO:0000269|PubMed:11239471, ECO:0000269|PubMed:17475775,
CC ECO:0000269|PubMed:20972447}.
CC -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein particle) II
CC complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65,
CC TRS120 and TRS130. Interacts directly with TRS65.
CC {ECO:0000269|PubMed:11239471, ECO:0000269|PubMed:17475775,
CC ECO:0000269|PubMed:20972447, ECO:0000269|PubMed:9564032}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network
CC {ECO:0000269|PubMed:11239471}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRS120 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA59326.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U32274; AAB64847.1; -; Genomic_DNA.
DR EMBL; X84902; CAA59326.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006938; DAA12249.1; -; Genomic_DNA.
DR PIR; S69689; S69689.
DR RefSeq; NP_010695.1; NM_001180715.1.
DR PDB; 7E2C; EM; 4.18 A; J=1-1289.
DR PDB; 7E2D; EM; 3.71 A; J=1-1289.
DR PDB; 7E8S; EM; 4.36 A; J/U=1-1289.
DR PDB; 7E8T; EM; 3.80 A; J=1-1289.
DR PDB; 7E93; EM; 6.54 A; J/U=1-1289.
DR PDB; 7E94; EM; 4.67 A; J/U=1-1289.
DR PDB; 7EA3; EM; 4.31 A; J/W=1-1289.
DR PDBsum; 7E2C; -.
DR PDBsum; 7E2D; -.
DR PDBsum; 7E8S; -.
DR PDBsum; 7E8T; -.
DR PDBsum; 7E93; -.
DR PDBsum; 7E94; -.
DR PDBsum; 7EA3; -.
DR AlphaFoldDB; Q04183; -.
DR SMR; Q04183; -.
DR BioGRID; 32467; 30.
DR ComplexPortal; CPX-1939; TRAPPII protein complex.
DR DIP; DIP-6461N; -.
DR IntAct; Q04183; 11.
DR MINT; Q04183; -.
DR STRING; 4932.YDR407C; -.
DR iPTMnet; Q04183; -.
DR MaxQB; Q04183; -.
DR PaxDb; Q04183; -.
DR PRIDE; Q04183; -.
DR EnsemblFungi; YDR407C_mRNA; YDR407C; YDR407C.
DR GeneID; 852016; -.
DR KEGG; sce:YDR407C; -.
DR SGD; S000002815; TRS120.
DR VEuPathDB; FungiDB:YDR407C; -.
DR eggNOG; KOG1953; Eukaryota.
DR GeneTree; ENSGT00390000006486; -.
DR HOGENOM; CLU_002231_0_0_1; -.
DR InParanoid; Q04183; -.
DR OMA; DYIWHAK; -.
DR BioCyc; YEAST:G3O-29951-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:Q04183; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04183; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:1990071; C:TRAPPII protein complex; IDA:SGD.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:SGD.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:SGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IC:ComplexPortal.
DR InterPro; IPR013935; TRAPP_II_complex_Trs120.
DR PANTHER; PTHR21512; PTHR21512; 1.
DR Pfam; PF08626; TRAPPC9-Trs120; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Golgi apparatus; Phosphoprotein; Reference proteome;
KW Transport.
FT CHAIN 1..1289
FT /note="Trafficking protein particle complex II-specific
FT subunit 120"
FT /id="PRO_0000076355"
FT REGION 354..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 435
FT /note="A -> C (in Ref. 3; CAA59326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1289 AA; 147662 MW; A1B01959A5875E29 CRC64;
MNILKHFPSY VGPSKIRTLV IPIGHWTRKE FNNAVQKLSE FNEIHLSDVT PIDSPIFTPQ
GFPHGKLFFD FLTIDHDDAL ELFLYDFEPF RKTFVIIGLV NDYSDPLTNL NFMKEKYPTL
ISPNLVYASS TPTKELEQTI DTMENVFASS PDMQKNIETI MCDIARNFLT ALNSYYSSYK
HVTLRSPGAI GGNAVLKTTL IRQNSYTSSS SSTPMSAVQS SVSSSSKAGS VTTASKRLSS
FEMTTNSLKR SASLKLATTL STSENRSQQK SLGRQMKILG NFQLLAGRYV DALNSFVDAI
TTLYKVRDYL WLGSALDGIS ICFLLLSYLG LSYQIPQIVS LICPVEKLNF ESSSTGISPV
DSNSKATAST TASSTPRNSI SIAAMQSPRN SIMSLSAPAL NIDVENINLP LLIKCISDKV
LYYYDLSLMH NSEYAPQVVY CEFLLKTLTF MTSCYKSSEF SKDVLDNIVK NQHRALSDIP
NSPMFPRFEV YFYSNKLFEL QLKEMQVEAQ IKIYSTMAEV YRLLGYKRKQ LFVLRLLMVA
LLATPNKIAW HPDYRTLIDT IIELLNINES EAKINVDDPS QSTWLILQKK ILQLCIKVSR
KINDFEYVAK FSSILITKYT HLLNQSEQDA LFKEYIQPSI TNESITSYWD PFILREVVIN
RILDSDPTSN EIPLESDVSS LESLENRQKT QDINPQEVFN PFKRVQPTSF VSNNSTKVPI
LVFLVGDKAE FTCRVQNPFK FDFTINDIQL DEEISEFCEI DRKAVSYSGP YNVKAESIRS
ITLPLIIKKP TYKKIYEISC LKISILKLPL QKFDIINDSR RSNPVEEEAE YSKCIYGKLK
IKILPEQPQL ELLSTSKMTR NSWMMLDGTK TDFHITVRNK SLSCAINHIK IIPMNNIEQM
LKPDYWKKMP PDDLYIMEKQ LDWLSKSCVR IIKLPTVIKP NETITFDLEL DNTAVPFNFT
GFDLLIEYGM SATDESCIYL KKLSIPYEVT LRRTIEVPSM DIIPLNELFS SQVENVDWIE
YVMSKIRAES NLHSRDFILL LLDFRNSWID GIKLNVQFED FTSNEYHVEA SHTSRIIVPI
KKIDYKKYNF ENTPIPRIYP GRQFIQSGLN EEQTIEMRQK FWCREHIISK LKCNWKLTTD
QSVTGSVDFN KFIEKFDHKM VYTIYPGRLF YGVQLLLDEP KVKVGEIINL KIITEPTSTC
RRKQNSTVNF LDIVIFDSKT SKILPRSNRR ILYNGSLTKP ISTTKVSEIN LEIIPIEKGR
YEFSVCISKS NNQDGIIQFD SENVILSVI
