EHD1_ARATH
ID EHD1_ARATH Reviewed; 545 AA.
AC Q94CF0; Q9LTR4;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=EH domain-containing protein 1 {ECO:0000303|PubMed:18547399};
DE Short=AtEHD1 {ECO:0000303|PubMed:18547399};
DE EC=3.6.5.2 {ECO:0000255|PROSITE-ProRule:PRU00758};
GN Name=EHD1 {ECO:0000303|PubMed:18547399};
GN OrderedLocusNames=At3g20290 {ECO:0000312|Araport:AT3G20290};
GN ORFNames=MQC12.3 {ECO:0000312|EMBL:BAB02809.1};
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 {ECO:0000312|EMBL:AAK59418.1};
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;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH19984.1};
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, GENE FAMILY,
RP AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=18547399; DOI=10.1111/j.1365-313x.2008.03571.x;
RA Bar M., Aharon M., Benjamin S., Rotblat B., Horowitz M., Avni A.;
RT "AtEHDs, novel Arabidopsis EH-domain-containing proteins involved in
RT endocytosis.";
RL Plant J. 55:1025-1038(2008).
RN [6]
RP REVIEW.
RX PubMed=19704436; DOI=10.4161/psb.6708;
RA Bar M., Benjamin S., Horowitz M., Avni A.;
RT "AtEHDs in endocytosis.";
RL Plant Signal. Behav. 3:1008-1010(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY SALINITY STRESS, MUTAGENESIS
RP OF 1-MET--VAL-93, SUBCELLULAR LOCATION, AND DOMAIN EH.
RX PubMed=23342166; DOI=10.1371/journal.pone.0054533;
RA Bar M., Leibman M., Schuster S., Pitzhadza H., Avni A.;
RT "EHD1 functions in endosomal recycling and confers salt tolerance.";
RL PLoS ONE 8:E54533-E54533(2013).
CC -!- FUNCTION: Involved in endocytosis positive regulation. Acts in early
CC endocytic membrane fusion and membrane trafficking of recycling
CC endosomes (PubMed:18547399, PubMed:23342166). Confers salt tolerance
CC (PubMed:23342166). {ECO:0000269|PubMed:18547399,
CC ECO:0000269|PubMed:23342166}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00758};
CC -!- SUBUNIT: Homooligomer, and heterooligomer with EHD2.
CC {ECO:0000269|PubMed:18547399}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:18547399,
CC ECO:0000269|PubMed:23342166}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18547399}. Cell membrane
CC {ECO:0000269|PubMed:18547399}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18547399}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9WVK4}. Cytoplasm.
CC -!- INDUCTION: By salinity stress. {ECO:0000269|PubMed:23342166}.
CC -!- DOMAIN: The EH domain (1-93) is critical for vesicular localization.
CC {ECO:0000269|PubMed:23342166}.
CC -!- DISRUPTION PHENOTYPE: Early flowering in short-day growth conditions
CC (PubMed:18547399). Slightly slower endocytosis with delayed
CC internalization (PubMed:18547399, PubMed:23342166). Reduced Brefeldin A
CC sensitivity (PubMed:23342166). {ECO:0000269|PubMed:18547399,
CC ECO:0000269|PubMed:23342166}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. EHD subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02809.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024036; BAB02809.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76359.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76360.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65913.1; -; Genomic_DNA.
DR EMBL; AY034911; AAK59418.1; -; mRNA.
DR EMBL; BT004414; AAO42408.1; -; mRNA.
DR EMBL; AK317308; BAH19984.1; -; mRNA.
DR RefSeq; NP_001030731.1; NM_001035654.2.
DR RefSeq; NP_001327849.1; NM_001338474.1.
DR RefSeq; NP_566657.1; NM_112920.4.
DR AlphaFoldDB; Q94CF0; -.
DR SMR; Q94CF0; -.
DR IntAct; Q94CF0; 1.
DR STRING; 3702.AT3G20290.1; -.
DR PaxDb; Q94CF0; -.
DR PRIDE; Q94CF0; -.
DR ProteomicsDB; 221936; -.
DR EnsemblPlants; AT3G20290.1; AT3G20290.1; AT3G20290.
DR EnsemblPlants; AT3G20290.2; AT3G20290.2; AT3G20290.
DR EnsemblPlants; AT3G20290.3; AT3G20290.3; AT3G20290.
DR GeneID; 821573; -.
DR Gramene; AT3G20290.1; AT3G20290.1; AT3G20290.
DR Gramene; AT3G20290.2; AT3G20290.2; AT3G20290.
DR Gramene; AT3G20290.3; AT3G20290.3; AT3G20290.
DR KEGG; ath:AT3G20290; -.
DR Araport; AT3G20290; -.
DR TAIR; locus:2092419; AT3G20290.
DR eggNOG; KOG1954; Eukaryota.
DR HOGENOM; CLU_017595_2_0_1; -.
DR InParanoid; Q94CF0; -.
DR OMA; KDMPSMF; -.
DR OrthoDB; 377342at2759; -.
DR PhylomeDB; Q94CF0; -.
DR PRO; PR:Q94CF0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94CF0; baseline and differential.
DR Genevisible; Q94CF0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0032456; P:endocytic recycling; IMP:TAIR.
DR GO; GO:0006897; P:endocytosis; IMP:TAIR.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR CDD; cd00052; EH; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR040990; DUF5600.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR031692; EHD_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF18150; DUF5600; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF12763; EF-hand_4; 1.
DR Pfam; PF16880; EHD_N; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Coiled coil; Cytoplasm; Endocytosis; Endosome;
KW GTP-binding; Hydrolase; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..545
FT /note="EH domain-containing protein 1"
FT /id="PRO_0000431805"
FT DOMAIN 14..49
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 15..93
FT /note="EH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 50..83
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 194..429
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 204..211
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 230..231
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 292..295
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 358..361
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 382
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 467..490
FT /evidence="ECO:0000255"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 204..211
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 309..313
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT BINDING 395..398
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT MUTAGEN 1..93
FT /note="Missing: Impaired endosomal subcellular location and
FT delayed internalization."
FT /evidence="ECO:0000269|PubMed:23342166"
SQ SEQUENCE 545 AA; 61230 MW; 0E5B907504D70117 CRC64;
MEIESVAAGS CSKENQMIYK EWFEFSDSDG DGRITGNDAI KFFTMSNLPR PELKQIWAIA
DSKRQGYLGF KEFIVAMQLV SLAQTGHEIS HEVLISDVDF KNINPPTMEG LGVLMAKKKH
SSKSSDPNMN GSPAADTSLT AHWFSSKSSK KISLSSVTSI VDGLKRLYIQ KLKPLEVAYR
FNDFVSPLLT NSDFDAKPMV MLLGQYSTGK TTFIKHLLKS TYPGAHIGPE PTTDRFVVVM
SGPDERSIPG NTVAVQADMP FSGLTTFGTA FLSKFECSQM PHPLLEHVTF VDTPGVLSGE
KQRTQRAYDF TGVTSWFASK CDLILLLFDP HKLDVSDEFK RVISSLRGHD DKIRVVLNKA
DQVDTQQLMR VYGALMWSLG KVLNTPEVSR VYIGSFSDKP INEAATGPIG RELFEKEQDD
LLADLKDIPK KACDRRINEF VKRARAAKIH AYIISHLKKE MPAIMGKAKA QQKLIDNLED
EFGKVQREHH LPKGDFPNVD HFREVLSGYN IDKFEKLKPK MLQTVDDMLG YDIPELLKNF
KNPYD
