ELCL_ARATH
ID ELCL_ARATH Reviewed; 368 AA.
AC Q9FFY6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein ELC-like {ECO:0000303|PubMed:17090720};
DE AltName: Full=ESCRT-I complex subunit VPS23 homolog 2 {ECO:0000303|PubMed:17090720};
DE AltName: Full=Protein VACUOLAR PROTEIN SORTING 23B {ECO:0000303|PubMed:25438943};
DE AltName: Full=Vacuolar protein sorting-associated protein 23 homolog 2 {ECO:0000303|PubMed:17090720};
GN Name=ELCL {ECO:0000303|PubMed:17090720};
GN Synonyms=ELCHL {ECO:0000303|PubMed:17090720},
GN VPS23B {ECO:0000303|PubMed:22639582, ECO:0000303|PubMed:25438943};
GN OrderedLocusNames=At5g13860 {ECO:0000312|Araport:AT5G13860};
GN ORFNames=MAC12.18 {ECO:0000312|EMBL:BAB11114.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP IDENTIFICATION, AND NOMENCLATURE.
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 [5]
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 [6]
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 [7]
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).
CC -!- FUNCTION: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I), a regulator of vesicular trafficking
CC process. Required for the sorting of endocytic ubiquitinated cargos
CC into multivesicular bodies (MVBs). {ECO:0000250|UniProtKB:Q9LHG8}.
CC -!- SUBUNIT: Component of the endosomal sorting required for transport
CC complex I (ESCRT-I), composed of ELC, VPS28 and VPS37 (By similarity).
CC Interacts with FREE1 (PubMed:25438943). Interacts with TOL9/TOM1D
CC (PubMed:22639582). {ECO:0000250|UniProtKB:Q9LHG8,
CC ECO:0000269|PubMed:22639582, ECO:0000269|PubMed:25438943}.
CC -!- INTERACTION:
CC Q9FFY6; Q9LHG8: ELC; NbExp=4; IntAct=EBI-3865255, EBI-3865248;
CC Q9FFY6; Q9SCP9: VPS37-1; NbExp=4; IntAct=EBI-3865255, EBI-3865264;
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q9LHG8}.
CC Prevacuolar compartment {ECO:0000269|PubMed:25438943}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000305}.
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DR EMBL; AB005230; BAB11114.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91951.1; -; Genomic_DNA.
DR EMBL; BX832522; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_196890.1; NM_121389.3.
DR AlphaFoldDB; Q9FFY6; -.
DR SMR; Q9FFY6; -.
DR BioGRID; 16510; 13.
DR IntAct; Q9FFY6; 6.
DR STRING; 3702.AT5G13860.1; -.
DR TCDB; 3.A.31.1.2; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR PaxDb; Q9FFY6; -.
DR PRIDE; Q9FFY6; -.
DR ProteomicsDB; 222286; -.
DR EnsemblPlants; AT5G13860.1; AT5G13860.1; AT5G13860.
DR GeneID; 831232; -.
DR Gramene; AT5G13860.1; AT5G13860.1; AT5G13860.
DR KEGG; ath:AT5G13860; -.
DR Araport; AT5G13860; -.
DR TAIR; locus:2159113; AT5G13860.
DR eggNOG; KOG2391; Eukaryota.
DR HOGENOM; CLU_017548_0_0_1; -.
DR InParanoid; Q9FFY6; -.
DR OMA; LQVIAMN; -.
DR OrthoDB; 1435538at2759; -.
DR PhylomeDB; Q9FFY6; -.
DR PRO; PR:Q9FFY6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFY6; baseline and differential.
DR GO; GO:0000813; C:ESCRT I complex; ISS:TAIR.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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.
FT CHAIN 1..368
FT /note="Protein ELC-like"
FT /id="PRO_0000368021"
FT DOMAIN 18..162
FT /note="UEV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00652"
FT DOMAIN 292..360
FT /note="SB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00644"
FT REGION 155..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 234..255
FT /evidence="ECO:0000255"
SQ SEQUENCE 368 AA; 41495 MW; 262F8CDB45BBCD40 CRC64;
MAPPPAKMQE IHQFLSSALT QRGPSALPYA ENTKSLIRQH LLNLISSYTS LDPKTATFTH
NDGRSVILLQ ADGTIPMPFQ GVSYNIPVVI WLLESYPQYP PCVYVNPTRD MIIKRPHSNV
SPSGLVSLPY LQNWIYPSSN LVDLASHLSA AFSRDPPLYS QRRPPPQPSP SIGSGYSRPL
PPRQTDDAAE VYKKNAINRI VEMVHGDIVL MRSAREVETE GLLSLQSDLK RREEEINNGF
KEMVIEKETL EQQLQVIAMN TDVLGSWIRE NQGKAKDLLV DLDVDDSFEC IDSLSKQMLE
CTALDLAIED VVYSMDKSFR DGSLPFDQYL RNVRLLSREQ FFHRATAEKV REIQMDAQVA
SIAARLHS
