EREX_ARATH
ID EREX_ARATH Reviewed; 755 AA.
AC Q9LSB9; Q680J3;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=PX domain-containing protein EREX {ECO:0000305};
DE AltName: Full=Protein ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN {ECO:0000303|PubMed:27288222};
GN Name=EREX {ECO:0000303|PubMed:27288222};
GN OrderedLocusNames=At3g15920 {ECO:0000312|Araport:AT3G15920};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH RABF2A AND RABF2B, SUBCELLULAR LOCATION, DOMAIN,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=27288222; DOI=10.1105/tpc.16.00326;
RA Sakurai H.T., Inoue T., Nakano A., Ueda T.;
RT "ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an interacting partner of RAB5
RT GTPases, regulates membrane trafficking to protein storage vacuoles in
RT Arabidopsis.";
RL Plant Cell 28:1490-1503(2016).
CC -!- FUNCTION: Acts as an effector of RABF2A and RABF2B. Involved in
CC vacuolar transport of storage proteins. Regulates membrane trafficking
CC to protein storage vacuoles (PSVs). Binds specifically to
CC phosphatidylinositol 3-monophosphate (PtdIns3P).
CC {ECO:0000269|PubMed:27288222}.
CC -!- SUBUNIT: Interacts (via PX domain) with RABF2A and RABF2B.
CC {ECO:0000269|PubMed:27288222}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:27288222}.
CC Endosome membrane {ECO:0000269|PubMed:27288222}; Peripheral membrane
CC protein {ECO:0000305}. Note=The endosomal localization depends on the
CC active state of RABF2B. Binding of phosphatidylinositol 3-monophosphate
CC via the PX domain is required for the endosomal localization.
CC {ECO:0000269|PubMed:27288222}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutant plants erex and erel1 exhibit severe
CC growth retardation at a juvenile stage. {ECO:0000269|PubMed:27288222}.
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DR EMBL; AB026653; BAB02876.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75747.1; -; Genomic_DNA.
DR EMBL; BT012581; AAS99725.1; -; mRNA.
DR EMBL; AK175543; BAD43306.1; -; mRNA.
DR EMBL; AK175874; BAD43637.1; -; mRNA.
DR EMBL; AK176000; BAD43763.1; -; mRNA.
DR RefSeq; NP_188213.1; NM_112462.6.
DR AlphaFoldDB; Q9LSB9; -.
DR SMR; Q9LSB9; -.
DR iPTMnet; Q9LSB9; -.
DR PaxDb; Q9LSB9; -.
DR PRIDE; Q9LSB9; -.
DR ProteomicsDB; 221807; -.
DR EnsemblPlants; AT3G15920.1; AT3G15920.1; AT3G15920.
DR GeneID; 820835; -.
DR Gramene; AT3G15920.1; AT3G15920.1; AT3G15920.
DR KEGG; ath:AT3G15920; -.
DR Araport; AT3G15920; -.
DR TAIR; locus:2093915; AT3G15920.
DR eggNOG; ENOG502QVII; Eukaryota.
DR HOGENOM; CLU_010605_0_0_1; -.
DR InParanoid; Q9LSB9; -.
DR OMA; LHECAIL; -.
DR OrthoDB; 413978at2759; -.
DR PhylomeDB; Q9LSB9; -.
DR PRO; PR:Q9LSB9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSB9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR044588; EREX-like.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR46856; PTHR46856; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..755
FT /note="PX domain-containing protein EREX"
FT /id="PRO_0000438484"
FT DOMAIN 107..224
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 36..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 420..585
FT /evidence="ECO:0000255"
FT COMPBIAS 55..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 191
FT /note="R -> G (in Ref. 4; BAD43637)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 755 AA; 85631 MW; D12656461BE4E9B0 CRC64;
MNLYAHDLSL LDFNYNVSGP FGEPLSHRFL SPGPFFQGEE DDYRRNTSYS HDGANGREPD
TDSRASPPHR HDGRSPLPLG MDWSSPPRHL EGRDTVWPHD HRTGWSYCVT VPSWVDLPKS
SVSDPAVFYR VQVAIQSPEG ITSARLVLRR FNDFLELYSS IKKEFVKKSL PQAPPKKILR
MRNQTLLEER RCSLEDWMNR LLSDIDISRS ALIATFLELE AAVRSYFNDE YQETEDTSGD
IPSLLPTTIS DVPGSSSVTI DHDNDSADET SNASTMKHDE ANLKNLFSRN STAVDNVTDW
HELITEYGLL DQSSFQEKVE RLSSTNGDAA TGTVTRGGIS SGVGIQRLDG SDRKFQELTI
ESIKKTHVSD FEASTAVEPD LVNQGAMDIH GEAHGNMYGA VGGDTETQKD LAIVFQSEER
HKLKRVIDTL KQRLETAKAD TEDLISRLNQ ELAVRQFLST KVRDLEVELE TTRESCKQGM
EKTVLDEKER FTQIQWDMEE LRKQCMEMES FLNSIKDEKT HIETANESLV QENQMLLQQI
NDIRENFENF HKEHEELEVK AKAELKVLVK EVKSLRTTQS DLRQELSGIM KEKLEMERIV
QREKDREETA KNADKKLLHE CDVLQNRLQE CNVKFDIEEE GKLIMDSSSL SEAIELLATS
DNRIGLLIAE TQLLSEEVEK LKLTSGGHRG TDDLVRKMLT EVLIDNARLR KQVNSVLRCS
LSGHGISVRE AGTEVDDEEG SIDLARTVMS KILEK
