EREL2_ARATH
ID EREL2_ARATH Reviewed; 643 AA.
AC Q8S8D3;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=PX domain-containing protein EREL2 {ECO:0000305};
DE AltName: Full=Protein EREX-like 2 {ECO:0000303|PubMed:27288222};
GN Name=EREL2 {ECO:0000303|PubMed:27288222};
GN OrderedLocusNames=At2g25350 {ECO:0000312|Araport:AT2G25350};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, SUBCELLULAR LOCATION, 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 (By similarity).
CC Involved in vacuolar transport of storage proteins. Regulates membrane
CC trafficking to protein storage vacuoles (PSVs) (Probable). Binds
CC specifically to phosphatidylinositol 3-monophosphate (PtdIns3P) (By
CC similarity). {ECO:0000250|UniProtKB:Q9LSB9,
CC ECO:0000305|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. {ECO:0000269|PubMed:27288222}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:27288222}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007070; AAM15376.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07692.1; -; Genomic_DNA.
DR RefSeq; NP_565591.1; NM_128092.2.
DR AlphaFoldDB; Q8S8D3; -.
DR SMR; Q8S8D3; -.
DR PaxDb; Q8S8D3; -.
DR PRIDE; Q8S8D3; -.
DR EnsemblPlants; AT2G25350.1; AT2G25350.1; AT2G25350.
DR GeneID; 817073; -.
DR Gramene; AT2G25350.1; AT2G25350.1; AT2G25350.
DR KEGG; ath:AT2G25350; -.
DR Araport; AT2G25350; -.
DR TAIR; locus:2040030; AT2G25350.
DR eggNOG; ENOG502QVII; Eukaryota.
DR HOGENOM; CLU_010605_0_0_1; -.
DR InParanoid; Q8S8D3; -.
DR OMA; RYVNSIQ; -.
DR PhylomeDB; Q8S8D3; -.
DR PRO; PR:Q8S8D3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8D3; 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; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..643
FT /note="PX domain-containing protein EREL2"
FT /id="PRO_0000438486"
FT DOMAIN 47..164
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 389..440
FT /evidence="ECO:0000255"
FT COILED 491..543
FT /evidence="ECO:0000255"
FT COMPBIAS 172..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 72823 MW; DA992D70213EF3D4 CRC64;
MQRRSPPKHR HDGASPLPLG MDWSPPPRNW NGRDTIWPHD FRTGWSYCVT IPSWTLLSKS
KNSDPIVFYR VQVSVQSPEG VSTMRGILRR FNDFVKLLAD LKRAFPRKSF PSAPPKGFLR
VKSRDMLEER RCSLEDWMTK LLSDIELARS VVVASFLELE ATARSACQVV DQNASDSNDD
GNSTSLSSLV HPNSGGSSLL SSDYGSDTAY ETSELGSASL GQDDVSETDT GDLTLDEDLT
NPTEKLVKFS MSNIDEGLSM SQTIIEQLED FPKHRVHLGY ANDITETNSY NGKASKGVFR
ANNDLRCRSE SETSHSVMHD RKLSLESADG VSLLAGETST SSILSSIVHS QLDVNHDISV
GNLEIPGNGR IVLPLKMHSK LNRILLTMNE RLLNSKTDME DLIARLNQET AVKEYLNRKV
DDLEVELETT KQRNKENLEQ ALMTERQSVT KMQWDMEELR QKTFEMELKL KSKEDGSSDS
KTSGNSTISE SHELLQEMDA TKQQLEDLSR RYVELEAKSK ADIKVLVREV KSLRRSHMEM
EKELTRSLTE KSDTEKLLQQ ERIIVENTLE ARRRLYSDCE ILHDRLKVNN TNLSMDESSN
NREDLSEVSN ALQDQIEAQL LLGFDETASE DELRKIMADM YED
