ELC_ARATH
ID ELC_ARATH Reviewed; 398 AA.
AC Q9LHG8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein ELC {ECO:0000303|PubMed:17090720};
DE Short=AtELC {ECO:0000303|PubMed:17090720};
DE AltName: Full=ESCRT-I complex subunit VPS23 homolog 1 {ECO:0000303|PubMed:17090720};
DE AltName: Full=Protein VACUOLAR PROTEIN SORTING 23A {ECO:0000303|PubMed:25438943};
DE AltName: Full=Vacuolar protein-sorting-associated protein 23 homolog 1 {ECO:0000303|PubMed:16488176};
GN Name=ELC {ECO:0000303|PubMed:17090720};
GN Synonyms=ELCH {ECO:0000303|PubMed:17090720},
GN VPS23A {ECO:0000303|PubMed:22639582, ECO:0000303|PubMed:25438943};
GN OrderedLocusNames=At3g12400 {ECO:0000312|Araport:AT3G12400};
GN ORFNames=MQC3.22 {ECO:0000312|EMBL:BAB03147.1},
GN T2E22.28 {ECO:0000312|EMBL:AAG51025.1};
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;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH VPS28; VPS37 AND UBIQUITIN,
RP DISRUPTION PHENOTYPE, NOMENCLATURE, AND SUBCELLULAR LOCATION.
RX PubMed=17090720; DOI=10.1242/dev.02654;
RA Spitzer C., Schellmann S., Sabovljevic A., Shahriari M., Keshavaiah C.,
RA Bechtold N., Herzog M., Mueller S., Hanisch F.-G., Huelskamp M.;
RT "The Arabidopsis elch mutant reveals functions of an ESCRT component in
RT cytokinesis.";
RL Development 133:4679-4689(2006).
RN [7]
RP IDENTIFICATION.
RX PubMed=16488176; DOI=10.1016/j.tplants.2006.01.008;
RA Winter V., Hauser M.-T.;
RT "Exploring the ESCRTing machinery in eukaryotes.";
RL Trends Plant Sci. 11:115-123(2006).
RN [8]
RP INTERACTION WITH TOL9.
RX PubMed=22639582; DOI=10.3389/fpls.2011.00020;
RA Richardson L.G., Howard A.S., Khuu N., Gidda S.K., McCartney A.,
RA Morphy B.J., Mullen R.T.;
RT "Protein-protein interaction network and subcellular localization of the
RT Arabidopsis thaliana ESCRT machinery.";
RL Front. Plant Sci. 2:20-20(2011).
RN [9]
RP INTERACTION WITH FREE1, AND SUBCELLULAR LOCATION.
RX PubMed=25438943; DOI=10.1016/j.cub.2014.09.014;
RA Gao C., Luo M., Zhao Q., Yang R., Cui Y., Zeng Y., Xia J., Jiang L.;
RT "A unique plant ESCRT component, FREE1, regulates multivesicular body
RT protein sorting and plant growth.";
RL Curr. Biol. 24:2556-2563(2014).
RN [10]
RP INTERACTION WITH BRO1.
RX PubMed=26902184; DOI=10.1016/j.molp.2016.02.005;
RA Shen J., Gao C., Zhao Q., Lin Y., Wang X., Zhuang X., Jiang L.;
RT "AtBRO1 functions in ESCRT-I complex to regulate multivesicular body
RT protein sorting.";
RL Mol. Plant 9:760-763(2016).
RN [11]
RP INTERACTION WITH SINAT1; SINAT2; SINAT3 AND SINAT4, AND UBIQUITINATION.
RX PubMed=32753431; DOI=10.1105/tpc.20.00267;
RA Xia F.N., Zeng B., Liu H.S., Qi H., Xie L.J., Yu L.J., Chen Q.F., Li J.F.,
RA Chen Y.Q., Jiang L., Xiao S.;
RT "SINAT E3 ubiquitin ligases mediate FREE1 and VPS23A degradation to
RT modulate abscisic acid signaling.";
RL Plant Cell 32:3290-3310(2020).
CC -!- FUNCTION: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I), a regulator of vesicular trafficking process
CC (PubMed:17090720). Required for the sorting of endocytic ubiquitinated
CC cargos into multivesicular bodies (MVBs) (PubMed:17090720). May control
CC nuclear division through the microtubule cytoskeleton
CC (PubMed:17090720). {ECO:0000269|PubMed:17090720}.
CC -!- SUBUNIT: Component of the endosomal sorting required for transport
CC complex I (ESCRT-I), composed of ELC, VPS28 and VPS37
CC (PubMed:17090720). Interacts with VPS28 and VPS37 (PubMed:17090720).
CC Binds ubiquitin in vitro (PubMed:17090720). Interacts with FREE1
CC (PubMed:25438943). Interacts with TOL9/TOM1D (PubMed:22639582).
CC Interacts with BRO1/ALIX (PubMed:26902184, PubMed:17090720,
CC PubMed:22639582, PubMed:25438943). Interacts with SINAT1, SINAT2,
CC SINAT3 and SINAT4 (PubMed:32753431). {ECO:0000269|PubMed:17090720,
CC ECO:0000269|PubMed:22639582, ECO:0000269|PubMed:25438943,
CC ECO:0000269|PubMed:26902184, ECO:0000269|PubMed:32753431}.
CC -!- INTERACTION:
CC Q9LHG8; Q9FFY6: ELCL; NbExp=4; IntAct=EBI-3865248, EBI-3865255;
CC Q9LHG8; Q9FF81: VPS36; NbExp=3; IntAct=EBI-3865248, EBI-3865302;
CC Q9LHG8; Q9SCP9: VPS37-1; NbExp=4; IntAct=EBI-3865248, EBI-3865264;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:17090720}.
CC Late endosome {ECO:0000269|PubMed:17090720}. Prevacuolar compartment
CC {ECO:0000269|PubMed:25438943}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers.
CC {ECO:0000269|PubMed:17090720}.
CC -!- PTM: Ubiquitinated by SINAT1, SINAT2, SINAT3 and SINAT4 for subsequent
CC proteasomal degradation. {ECO:0000269|PubMed:32753431}.
CC -!- DISRUPTION PHENOTYPE: Clustered trichomes and multinucleated cells.
CC {ECO:0000269|PubMed:17090720}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000305}.
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DR EMBL; AP002047; BAB03147.1; -; Genomic_DNA.
DR EMBL; AC069474; AAG51025.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75193.1; -; Genomic_DNA.
DR EMBL; AY056283; AAL07132.1; -; mRNA.
DR EMBL; AY133779; AAM91713.1; -; mRNA.
DR EMBL; AY087782; AAM65318.1; -; mRNA.
DR RefSeq; NP_566423.1; NM_112075.3.
DR AlphaFoldDB; Q9LHG8; -.
DR SMR; Q9LHG8; -.
DR BioGRID; 5753; 14.
DR IntAct; Q9LHG8; 8.
DR STRING; 3702.AT3G12400.1; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; Q9LHG8; -.
DR PRIDE; Q9LHG8; -.
DR ProteomicsDB; 220759; -.
DR EnsemblPlants; AT3G12400.1; AT3G12400.1; AT3G12400.
DR GeneID; 820419; -.
DR Gramene; AT3G12400.1; AT3G12400.1; AT3G12400.
DR KEGG; ath:AT3G12400; -.
DR Araport; AT3G12400; -.
DR TAIR; locus:2092477; AT3G12400.
DR eggNOG; KOG2391; Eukaryota.
DR HOGENOM; CLU_017548_0_0_1; -.
DR InParanoid; Q9LHG8; -.
DR PhylomeDB; Q9LHG8; -.
DR PRO; PR:Q9LHG8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHG8; baseline and differential.
DR Genevisible; Q9LHG8; AT.
DR GO; GO:0005769; C:early endosome; IDA:TAIR.
DR GO; GO:0000813; C:ESCRT I complex; ISS:TAIR.
DR GO; GO:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IDA:TAIR.
DR GO; GO:0043130; F:ubiquitin binding; IDA:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR017916; SB_dom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR008883; UEV_N.
DR Pfam; PF05743; UEV; 1.
DR Pfam; PF09454; Vps23_core; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS51312; SB; 1.
DR PROSITE; PS51322; UEV; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endosome; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT CHAIN 1..398
FT /note="Protein ELC"
FT /id="PRO_0000368020"
FT DOMAIN 18..162
FT /note="UEV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00652"
FT DOMAIN 322..390
FT /note="SB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00644"
FT REGION 157..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 247..291
FT /evidence="ECO:0000255"
FT COMPBIAS 160..176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 44716 MW; 659996F9784FDC20 CRC64;
MVPPPSNPQQ VQQFLSSALS QRGPSSVPYE ESNKWLIRQH LLNLISSYPS LEPKTASFMH
NDGRSVNLLQ ADGTIPMPFH GVTYNIPVII WLLESYPRHP PCVYVNPTAD MIIKRPHAHV
TPSGLVSLPY LQNWVYPSSN LVDLVSDLSA AFARDPPLYS RRRPQPPPPS PPTVYDSSLS
RPPSADQSLP RPFPPSPYGG GVSRVQVQHV HHQQQSDDAA EVFKRNAINK MVEMVHSDLV
SMRRAREAEA EELLSLQAGL KRREDELNIG LKEMVEEKET LEQQLQIISM NTDILDSWVR
ENQGKTKNLV DLDVDNAFEC GDTLSKQMLE CTALDLAIED AIYSLDKSFQ DGVVPFDQYL
RNVRLLSREQ FFHRATGSKV RAAQMEVQVA AIAGRLHS
