ID   TR130_YEAST             Reviewed;        1102 AA.
AC   Q03660; D6W043;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Trafficking protein particle complex II-specific subunit 130;
DE            Short=TRAPP II-specific subunit 130;
DE   AltName: Full=Transport protein particle 130 kDa subunit;
GN   Name=TRS130; OrderedLocusNames=YMR218C; ORFNames=YM8261.12C;
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   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.
RX   PubMed=10727015; DOI=10.1078/s0171-9335(04)70009-6;
RA   Sacher M., Barrowman J., Schieltz D., Yates J.R. III, Ferro-Novick S.;
RT   "Identification and characterization of five new subunits of TRAPP.";
RL   Eur. J. Cell Biol. 79:71-80(2000).
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   FUNCTION, AND INTERACTION WITH YPT31 AND YPT32.
RX   PubMed=12478387; DOI=10.1007/s00294-002-0336-5;
RA   Yamamoto K., Jigami Y.;
RT   "Mutation of TRS130, which encodes a component of the TRAPP II complex,
RT   activates transcription of OCH1 in Saccharomyces cerevisiae.";
RL   Curr. Genet. 42:85-93(2002).
RN   [7]
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   [8]
RP   FUNCTION.
RX   PubMed=16314430; DOI=10.1083/jcb.200505145;
RA   Cai H., Zhang Y., Pypaert M., Walker L., Ferro-Novick S.;
RT   "Mutants in trs120 disrupt traffic from the early endosome to the late
RT   Golgi.";
RL   J. Cell Biol. 171:823-833(2005).
RN   [9]
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   [10]
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   [11]
RP   FUNCTION.
RX   PubMed=23078654; DOI=10.1111/tra.12024;
RA   Zou S., Chen Y., Liu Y., Segev N., Yu S., Liu Y., Min G., Ye M., Zeng Y.,
RA   Zhu X., Hong B., Bjorn L.O., Liang Y., Li S., Xie Z.;
RT   "Trs130 participates in autophagy through GTPases Ypt31/32 in Saccharomyces
RT   cerevisiae.";
RL   Traffic 14:233-246(2013).
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 exchange factor (GEF) for the Golgi YPT1 GTPase. TRS130
CC       plays a role in the YPT GEF activity of TRAPP II in concert with the
CC       two other TRAPP II-specific subunits TRS65 and TRS120. Required for
CC       both the cytoplasm-to-vacuole targeting (Cvt) pathway and starvation-
CC       induced autophagy through its role in ATG8 and ATG9 trafficking.
CC       {ECO:0000269|PubMed:10727015, ECO:0000269|PubMed:11239471,
CC       ECO:0000269|PubMed:12478387, ECO:0000269|PubMed:16314430,
CC       ECO:0000269|PubMed:17475775, ECO:0000269|PubMed:20972447,
CC       ECO:0000269|PubMed:23078654}.
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 with YPT31 and YPT32.
CC       {ECO:0000269|PubMed:11239471, ECO:0000269|PubMed:12478387,
CC       ECO:0000269|PubMed:17475775, ECO:0000269|PubMed:20972447,
CC       ECO:0000269|PubMed:9564032}.
CC   -!- INTERACTION:
CC       Q03660; P32613: TCA17; NbExp=7; IntAct=EBI-19461, EBI-22370;
CC       Q03660; P38334: TRS20; NbExp=2; IntAct=EBI-19461, EBI-19468;
CC       Q03660; P32893: TRS65; NbExp=3; IntAct=EBI-19461, EBI-9900;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000305|PubMed:11239471}.
CC   -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TMEM1 family. {ECO:0000305}.
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DR   EMBL; Z49809; CAA89933.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10117.1; -; Genomic_DNA.
DR   PIR; S55100; S55100.
DR   RefSeq; NP_013945.1; NM_001182725.1.
DR   PDB; 7E2C; EM; 4.18 A; I=1-1102.
DR   PDB; 7E2D; EM; 3.71 A; I=1-1102.
DR   PDB; 7E8S; EM; 4.36 A; I/T=1-1102.
DR   PDB; 7E8T; EM; 3.80 A; I=1-1102.
DR   PDB; 7E93; EM; 6.54 A; I/T=1-1102.
DR   PDB; 7E94; EM; 4.67 A; I/T=1-1102.
DR   PDB; 7EA3; EM; 4.31 A; I/V=1-1102.
DR   PDB; 7U05; EM; 3.70 A; B/b=1-1102.
DR   PDB; 7U06; EM; 4.20 A; B/b=1-1102.
DR   PDBsum; 7E2C; -.
DR   PDBsum; 7E2D; -.
DR   PDBsum; 7E8S; -.
DR   PDBsum; 7E8T; -.
DR   PDBsum; 7E93; -.
DR   PDBsum; 7E94; -.
DR   PDBsum; 7EA3; -.
DR   PDBsum; 7U05; -.
DR   PDBsum; 7U06; -.
DR   AlphaFoldDB; Q03660; -.
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; Q03660; -.
DR   BioGRID; 35396; 121.
DR   ComplexPortal; CPX-1939; TRAPP II complex.
DR   DIP; DIP-6482N; -.
DR   IntAct; Q03660; 12.
DR   STRING; 4932.YMR218C; -.
DR   iPTMnet; Q03660; -.
DR   MaxQB; Q03660; -.
DR   PaxDb; 4932-YMR218C; -.
DR   PeptideAtlas; Q03660; -.
DR   EnsemblFungi; YMR218C_mRNA; YMR218C; YMR218C.
DR   GeneID; 855258; -.
DR   KEGG; sce:YMR218C; -.
DR   AGR; SGD:S000004831; -.
DR   SGD; S000004831; TRS130.
DR   VEuPathDB; FungiDB:YMR218C; -.
DR   eggNOG; KOG1931; Eukaryota.
DR   GeneTree; ENSGT00390000003873; -.
DR   HOGENOM; CLU_009596_0_0_1; -.
DR   InParanoid; Q03660; -.
DR   OMA; DYLNAYE; -.
DR   OrthoDB; 593347at2759; -.
DR   BioCyc; YEAST:G3O-32900-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; 855258; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q03660; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03660; 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:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP: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:0016236; P:macroautophagy; IMP:SGD.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; NAS:ComplexPortal.
DR   InterPro; IPR022233; TRAPP_II_complex_TRAPPC10_C.
DR   InterPro; IPR045126; TRAPPC10/Trs130.
DR   PANTHER; PTHR13251; EPILEPSY HOLOPROSENCEPHALY CANDIDATE 1/TMEM1; 1.
DR   PANTHER; PTHR13251:SF3; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 10; 1.
DR   Pfam; PF12584; TRAPPC10; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Autophagy; Golgi apparatus; Reference proteome; Transport.
FT   CHAIN           1..1102
FT                   /note="Trafficking protein particle complex II-specific
FT                   subunit 130"
FT                   /id="PRO_0000193512"
SQ   SEQUENCE   1102 AA;  128131 MW;  110EA9D95620E727 CRC64;
     MDKEIYCGSV PVSYFDPFDL FESLRPEFQQ ILPLDNIHWK AFDGTVRTVN RLPIELIPEG
     RGEADKSNDE QPFIRFLIVN CISIDQYRAK VRPLVRQWLP NLESVSSSTG EKMIYKPIIL
     LYANSEVVDS NLFKSVSLME KFGKDFPHVQ TLEVRSVYRS PKERQEFWNQ FSQKIKASVL
     SIFQKRLTHL QHSLANLQKG NNFEEQLLTR EKLYELYVVF NILEDASLEL QKIKKEILRR
     NMNMPDGKLQ VPFESSSKSD ESLGSIIIEG TLDKFQLHKY FFIRRLRLLK LEDQTLTAFV
     GAFQLIKNFI ESISIEYRKS VRLLEFKHYF ITSMLSYFEF ENVSNPLLCE IKAELLMLKR
     DNWVQGVMAT SGYRLMDKNY PNSDVKYKFD LLKETFVDET VFQENFLTLT KEILSLFNKC
     EGKRQRIVDI LSIEIGLLYY QGKKYEEAVS LFLSCYEYYT QTNWNSIGLK ILQVFIDSLS
     HCPKLDVLQI DGESVSASAV LTNAFLNILK LCKDNDSKEI WWKKFMDLQM KNNIHLMYPL
     DGLFEVTLNS KVHLARANVS AIEVNLKSYG FPEDISTKTM RLSLKNMGGD VIVFGASDFL
     LKKGENKLIL ECRDIMYGEF SLLSFEIIVE GITFVKEFPE NQDEFIVVPE IYCKESTKVL
     VKQAHNLNLG EYALELKSVQ SDALESLQVE VEVQKNIGNM KNLPVSFSMD EIQARKRYNT
     PFENVRLEYY LLDQITAFDL IIKTSFTKKN DQGTFGETKK VRIQCYLQLS VSVEDIFKKD
     IFFFKFLLNS SVREEPVILY SSELSAPDTR NDYNIRGDYI ATTPALITFD GNESFINCYE
     ITANNNFDSK DIFNLKVRYN TLKEQLDCFI TDAVLIEGDV EWFILFEKWK TFWELEILKK
     LKYDYDAFKE NRIIRLLKTS IDLNKTKSKI RNLCIEKAVL DKILICLNKV SRGIAVCNTD
     MDEYVRNLVP KQLTVPVQLP GFEQFFHVQF EQMETSHDAL HDTIATIGNS LSYTVIVENL
     SGQWGQDVID DGGYIFEILS SNEWLIHGQK RCAIKEKRKE FEVHLIPLKK GYLNFPRVEI
     TNINGKSCRV DHSNAFESIL IF
//