ID   TR130_ARATH             Reviewed;        1259 AA.
AC   F4K0C4; Q9LSR1;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Trafficking protein particle complex II-specific subunit 130 homolog {ECO:0000305};
DE            Short=AtTRS130 {ECO:0000303|PubMed:20713617};
DE            Short=TRAPP II-specific subunit 130 homolog {ECO:0000305};
GN   Name=TRS130 {ECO:0000303|PubMed:20713617};
GN   Synonyms=CLUB {ECO:0000303|PubMed:20609115};
GN   OrderedLocusNames=At5g54440 {ECO:0000312|Araport:AT5G54440};
GN   ORFNames=F24B18.6 {ECO:0000312|EMBL:BAA97517.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20609115; DOI=10.1111/j.1469-8137.2010.03331.x;
RA   Jaber E., Thiele K., Kindzierski V., Loderer C., Rybak K., Jurgens G.,
RA   Mayer U., Sollner R., Wanner G., Assaad F.F.;
RT   "A putative TRAPPII tethering factor is required for cell plate assembly
RT   during cytokinesis in Arabidopsis.";
RL   New Phytol. 187:751-763(2010).
RN   [6]
RP   COMPONENT OF THE TRAPPII COMPLEX.
RX   PubMed=20713617; DOI=10.1104/pp.110.154286;
RA   Thellmann M., Rybak K., Thiele K., Wanner G., Assaad F.F.;
RT   "Tethering factors required for cytokinesis in Arabidopsis.";
RL   Plant Physiol. 154:720-732(2010).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21689172; DOI=10.1111/j.1365-313x.2011.04681.x;
RA   Qi X., Kaneda M., Chen J., Geitmann A., Zheng H.;
RT   "A specific role for Arabidopsis TRAPPII in post-Golgi trafficking that is
RT   crucial for cytokinesis and cell polarity.";
RL   Plant J. 68:234-248(2011).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Specific subunit of the TRAPP II complex, a highly conserved
CC       vesicle tethering complex that is required for the proper transport of
CC       proteins in post-Golgi trafficking pathways to the growing cell plate
CC       in mitotic active cells (PubMed:20609115, PubMed:21689172). Required
CC       for the polarized and selective transport of PIN2, but not PIN1, to the
CC       plasma membrane. Not required for ER-to-Golgi as well as biosynthetic
CC       and endocytic vacuolar transport (PubMed:21689172).
CC       {ECO:0000269|PubMed:20609115, ECO:0000269|PubMed:21689172}.
CC   -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein particle) II
CC       complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65,
CC       TRS85, TRS120 and TRS130. {ECO:0000303|PubMed:20713617}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       {ECO:0000269|PubMed:21689172}. Early endosome
CC       {ECO:0000303|PubMed:21689172}.
CC   -!- DISRUPTION PHENOTYPE: Cytokinesis-defective and seedling-lethal
CC       phenotype. {ECO:0000269|PubMed:20609115, ECO:0000269|PubMed:21689172}.
CC   -!- SIMILARITY: Belongs to the TMEM1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA97517.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB026634; BAA97517.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96496.1; -; Genomic_DNA.
DR   EMBL; AY090975; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_200255.5; NM_124824.7.
DR   AlphaFoldDB; F4K0C4; -.
DR   STRING; 3702.AT5G54440.1; -.
DR   iPTMnet; F4K0C4; -.
DR   PaxDb; F4K0C4; -.
DR   PRIDE; F4K0C4; -.
DR   EnsemblPlants; AT5G54440.1; AT5G54440.1; AT5G54440.
DR   GeneID; 835532; -.
DR   Gramene; AT5G54440.1; AT5G54440.1; AT5G54440.
DR   KEGG; ath:AT5G54440; -.
DR   Araport; AT5G54440; -.
DR   TAIR; locus:2147324; AT5G54440.
DR   eggNOG; KOG1931; Eukaryota.
DR   HOGENOM; CLU_006790_0_0_1; -.
DR   InParanoid; F4K0C4; -.
DR   OrthoDB; 537782at2759; -.
DR   PRO; PR:F4K0C4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4K0C4; baseline and differential.
DR   Genevisible; F4K0C4; AT.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:1990071; C:TRAPPII protein complex; IBA:GO_Central.
DR   GO; GO:0000919; P:cell plate assembly; IMP:TAIR.
DR   GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR   GO; GO:0034498; P:early endosome to Golgi transport; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   InterPro; IPR022233; TRAPP_II_complex_TRAPPC10_C.
DR   InterPro; IPR045126; TRAPPC10/Trs130.
DR   PANTHER; PTHR13251; PTHR13251; 1.
DR   Pfam; PF12584; TRAPPC10; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endosome; Golgi apparatus; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..1259
FT                   /note="Trafficking protein particle complex II-specific
FT                   subunit 130 homolog"
FT                   /id="PRO_0000431450"
FT   REGION          479..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   1259 AA;  140681 MW;  194BD6B2D4F4AD17 CRC64;
     MANYLAQFQT IKNSCDRLVA AVEDVCDLWP TVKGLFEEHQ PLKRAFLTNK TRNPVFVENL
     PVEFILTTDA RLRSRFPQEQ YLFWFREPYA TIVLVTCEDL DEFKNILKPR LKLIVQNDER
     EWFIVFVSKA HPSNDQATKN VKKVYAKLEV DFSSKKRERC CKLDVHGPEG NFWEDLELKI
     TECIRNTLDR RAQFYEDEIR KLSEQRFMPI WNFCNFFILK ESLAFIFEMA HLHEDALREY
     DELELCYLET VNMPGKQRDF GGFDGEDDQA VLLKPGSKPL TQIVQDDSFR EFEFRQYLFA
     CQSRLLFKLN RPFEVASRGY SFVISFAKAL TLHESVLPFC MREVWVITAC LALIEATASH
     HHDGVVAPDI EKEFFRLQGD LYSLSRVKFM RLGYLIGYGT DIEKSPLNSA CLSMLPWPKP
     AVWPSLPQDA SSEVLEKEKT ILQATSRTKH FGIQRKALPL EPSVLLRVAN RRRASLSTGN
     IPEMFDGRPS FTEGSGLEAS PRTPSSLKVQ APPMSRTNSS PGNFESPLDR PMRLAEIFVA
     AEHALRLTIS DHDLLKTLSS IQDFENKYLN LTKGAAENYH RSWWKRHGVV LDGEIAAVCF
     KHGKYDLAAN SYEKVCALYA GEGWQDLLAE VLPNLAQCQK ILDDQAGYMS SCVRLLSLDK
     GLFSSKERQA FQSEVVTLAH SEMKNPVPLD VSSLITFSGN TGPPLQLCDG DPGNLSVTVW
     SGFPDDITLD SLSLTLVATN NTDEGGQALK SSAATVLNPG RNTITFALPP QKPGSYVLGV
     VTGQIGRLRF RSHSFSKGGP ADSDDFMSYE KPTRPILKVS KPRALVDLAA AVSSALLINE
     AQWIGIIVRP IAYSLKGAIL HIDTGPGLKI EDSYGIEMER YMDADCDTGA SKAEVFVEDS
     PVSSKRDSEV LNLCDGKIVF SDWASNVSSI LWVPVRALSE KLARGSSSVT PLKQDILEGM
     RTVALKLEFG VHHNQIFERT IAAHFTDPFD VTTRVANKCN DGTLVLQVML HSLVKANLIV
     LDVWLDLQDG FIHGQNDGRP TSTFFPLVVS PGSRAAVVFS ICLDKSMSSE GKDLQLPESI
     LNIKYGIHGD RAAGAHRPVD ADHSETDTEG RDLVFKSAIV LQRPVLDPCL TVGFLPLPSD
     GLRVGKLITM QWRVERLKEL KESEAVEQQH DEVLYEVNAN SENWMIAGRK RGHVSLSEEQ
     GSRVVISILC VPLVAGYVRP PQLGLPNVEE ANVSSNPSGP HLVCVLPPLL SSSYCLPVK