EREL1_ARATH
ID EREL1_ARATH Reviewed; 723 AA.
AC F4JTJ2; O49376; Q93YV8;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=PX domain-containing protein EREL1 {ECO:0000305};
DE AltName: Full=Protein EREX-like 1 {ECO:0000303|PubMed:27288222};
GN Name=EREL1 {ECO:0000303|PubMed:27288222};
GN OrderedLocusNames=At4g32160 {ECO:0000312|Araport:AT4G32160};
GN ORFNames=F10N7.30 {ECO:0000312|EMBL:CAA16573.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 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) (PubMed:27288222). Binds
CC specifically to phosphatidylinositol 3-monophosphate (PtdIns3P) (By
CC similarity). {ECO:0000250|UniProtKB:Q9LSB9,
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. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL24093.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA16573.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79934.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021636; CAA16573.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161580; CAB79934.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86012.1; -; Genomic_DNA.
DR EMBL; AY059745; AAL24093.1; ALT_FRAME; mRNA.
DR PIR; T04629; T04629.
DR RefSeq; NP_567888.2; NM_119368.3.
DR AlphaFoldDB; F4JTJ2; -.
DR SMR; F4JTJ2; -.
DR STRING; 3702.AT4G32160.1; -.
DR PaxDb; F4JTJ2; -.
DR PRIDE; F4JTJ2; -.
DR ProteomicsDB; 221806; -.
DR EnsemblPlants; AT4G32160.1; AT4G32160.1; AT4G32160.
DR GeneID; 829348; -.
DR Gramene; AT4G32160.1; AT4G32160.1; AT4G32160.
DR KEGG; ath:AT4G32160; -.
DR Araport; AT4G32160; -.
DR TAIR; locus:2116687; AT4G32160.
DR eggNOG; ENOG502QVII; Eukaryota.
DR HOGENOM; CLU_010605_0_0_1; -.
DR InParanoid; F4JTJ2; -.
DR OMA; YCVIIPS; -.
DR OrthoDB; 413978at2759; -.
DR PRO; PR:F4JTJ2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JTJ2; 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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Endosome; Lipid-binding; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..723
FT /note="PX domain-containing protein EREL1"
FT /id="PRO_0000438485"
FT DOMAIN 48..165
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 169..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 401..474
FT /evidence="ECO:0000255"
FT COILED 503..555
FT /evidence="ECO:0000255"
FT COMPBIAS 209..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 646
FT /note="N -> K (in Ref. 3; AAL24093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 81811 MW; 533DB0561BDCB6D6 CRC64;
MMQRRSPPKH RHDGTSPLPL GMDWSPPPRK WNGRDTVWPH DPRTGWSYCV TIPSWIVLPK
SRNSDPVVFY RVQVSVQSPE GITTMRGVLR RFNDFLKLLT DLKRTFPRKG FPSAPPKGLL
RMKSRAVLEE RRCSLEEWIT KLLSDIELAR SVVVASFLEL EAAARSACQD VDQNASDSNN
DRSSTSSSPM VHPSLSLFHA GGSTLTSDYG SDTAYETSEV GSPSVGQDDI SEIGTEDLTL
DEDLTLTNPI EKLVNFSMSN IDEGLSMSET ILEQLEDFPK HKVRSRYVNN ILGKDVYNGN
ASKGVFLANN GSRLLSEPEP STHSVMHDRN DSAERFALHT GQTSTSGLLI SSRDSHLDLR
QGPGVSLGTG LVCNPERQGS AQIVLPLELR NKLNRILLAT NERLVNAKTD MEDLIARLNQ
EIAVKDYLNK KVNDLEGELE TTKQRSKENL EQAIMSERER FNQMQWDMEE LRQKSYEMEM
KLKSREDGSS HAEPTVQSTI SEKHVLSKEL DARKQQLEDL SRRYEELEAK SKADMKVLVK
EVKSLRRSHV ELEKELTHSL TDKTNAEKLL QEERKLLENT VAARKKLLSD CRILHDRLKE
YNLNLSMDGN GNFVDDSTTI SDVLRLLSIS DDQIEEAQLL SGFDENAAAE DIDKTLSMDT
ETRIMEDELR KILANIFVEN AKLRKQVNSA MLRALQKDVK TTEDVNEENS DEKDEASRET
LKR
