EHD2_ARATH
ID EHD2_ARATH Reviewed; 546 AA.
AC B3LF48; F4JGH2; Q9S9W1;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=EH domain-containing protein 2 {ECO:0000303|PubMed:18547399};
DE Short=AtEHD2 {ECO:0000303|PubMed:18547399};
DE EC=3.6.5.2 {ECO:0000255|PROSITE-ProRule:PRU00758};
GN Name=EHD2 {ECO:0000303|PubMed:18547399};
GN OrderedLocusNames=At4g05520 {ECO:0000312|Araport:AT4G05520};
GN ORFNames=T1J24.10 {ECO:0000312|EMBL:AAD48968.1};
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:ACE79044.1};
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;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBUNIT, 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 [5]
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 [6]
RP FUNCTION, MUTAGENESIS OF GLY-37; GLY-204 AND 488-GLU--ASN-546, DOMAIN
RP COILED COIL, SUBCELLULAR LOCATION, AND INTERACTION WITH AT2G19790.
RX PubMed=19936242; DOI=10.1371/journal.pone.0007973;
RA Bar M., Sharfman M., Schuster S., Avni A.;
RT "The coiled-coil domain of EHD2 mediates inhibition of LeEix2 endocytosis
RT and signaling.";
RL PLoS ONE 4:E7973-E7973(2009).
CC -!- FUNCTION: Involved in endocytosis negative regulation, probably by
CC influencing actin organization. Acts in early endocytic membrane fusion
CC and membrane trafficking of recycling endosomes. Exhibits an inhibitory
CC effect on endocytosis when over-expressed.
CC {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}.
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 EHD1 (PubMed:18547399).
CC Interacts with AP-4 complex subunit sigma (At2g19790)
CC (PubMed:19936242). {ECO:0000269|PubMed:18547399,
CC ECO:0000269|PubMed:19936242}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q641Z6};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q641Z6}. Cell
CC membrane {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242};
CC Peripheral membrane protein {ECO:0000269|PubMed:18547399,
CC ECO:0000269|PubMed:19936242}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9WVK4}. Nucleus {ECO:0000255|PROSITE-
CC ProRule:PRU00768, ECO:0000269|PubMed:18547399,
CC ECO:0000269|PubMed:19936242}. Cytoplasm {ECO:0000269|PubMed:18547399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B3LF48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B3LF48-2; Sequence=VSP_057385;
CC -!- DOMAIN: The coiled coil domain (488-546) is required to inhibit
CC endocytosis. {ECO:0000269|PubMed:19936242}.
CC -!- DISRUPTION PHENOTYPE: Early flowering in short-day growth conditions.
CC {ECO:0000269|PubMed:18547399}.
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=AAD48968.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF147263; AAD48968.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161503; CAB81094.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82529.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82530.1; -; Genomic_DNA.
DR EMBL; BT033036; ACE79044.1; -; mRNA.
DR PIR; D85069; D85069.
DR RefSeq; NP_567299.2; NM_116790.3. [B3LF48-1]
DR RefSeq; NP_974517.1; NM_202788.1. [B3LF48-2]
DR AlphaFoldDB; B3LF48; -.
DR SMR; B3LF48; -.
DR STRING; 3702.AT4G05520.1; -.
DR iPTMnet; B3LF48; -.
DR PaxDb; B3LF48; -.
DR PRIDE; B3LF48; -.
DR ProteomicsDB; 221848; -. [B3LF48-1]
DR EnsemblPlants; AT4G05520.1; AT4G05520.1; AT4G05520. [B3LF48-1]
DR EnsemblPlants; AT4G05520.2; AT4G05520.2; AT4G05520. [B3LF48-2]
DR GeneID; 825902; -.
DR Gramene; AT4G05520.1; AT4G05520.1; AT4G05520. [B3LF48-1]
DR Gramene; AT4G05520.2; AT4G05520.2; AT4G05520. [B3LF48-2]
DR KEGG; ath:AT4G05520; -.
DR Araport; AT4G05520; -.
DR TAIR; locus:2135462; AT4G05520.
DR eggNOG; KOG1954; Eukaryota.
DR InParanoid; B3LF48; -.
DR OMA; CDNDGML; -.
DR OrthoDB; 377342at2759; -.
DR PhylomeDB; B3LF48; -.
DR PRO; PR:B3LF48; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; B3LF48; baseline and differential.
DR Genevisible; B3LF48; AT.
DR GO; GO:0005737; C:cytoplasm; 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:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP: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 Alternative splicing; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW Endocytosis; Endosome; GTP-binding; Hydrolase; Membrane; Metal-binding;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..546
FT /note="EH domain-containing protein 2"
FT /id="PRO_0000431806"
FT DOMAIN 15..50
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 16..94
FT /note="EH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 51..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 194..430
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 MOTIF 429..436
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT BINDING 28
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 73
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 292..296
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 VAR_SEQ 132
FT /note="Missing (in isoform 2)"
FT /id="VSP_057385"
FT MUTAGEN 37
FT /note="G->R: Slighty increased nuclear subcellular
FT localization."
FT /evidence="ECO:0000269|PubMed:19936242"
FT MUTAGEN 204
FT /note="G->R: Loss of negative effect on endocytosis."
FT /evidence="ECO:0000269|PubMed:19936242"
FT MUTAGEN 488..546
FT /note="Missing: Loss of negative effect on endocytosis."
FT /evidence="ECO:0000269|PubMed:19936242"
SQ SEQUENCE 546 AA; 61383 MW; B78F38337D934B6E CRC64;
METSSTISIG SCLKEHQKIY KEWFNIADSD GDGRVSGNDA TKFFAMSKLS RQELKQVWAV
ADSKRQGFLG LSEFITAMKL VSLAQEGHEI TSDLLKGSID MKSVELPVLE GLENVVSKQK
VSKTNVDVED NVVTKPQVTA KTPWFKSKSI IKPQVNVVTI VDGLKRLYTE KLKPLEVTYR
FNDFASPVLT SSDFDAKPMV MLLGQYSTGK TTFIKHLLGC DYPGAHIGPE PTTDRFVVAM
SGPDERTIPG NTMAVQADMP FNGLTSFGGA FLSKFECSQM PHPVLDQITL VDTPGVLSGE
KQRMQRSYDF TGVISWFASK CDMILLLFDP HKLDISDEFK RVITSLRGNE DKIRVVLNKA
DQVDTQQLMR VYGALMWSLG KVLNTPEVVR VYIGSFNDKP INEVAVGPIG KELFEKEQND
LLADLMDVPK KACDRKINEF VKRARSAKIN AYIMSHLKKE MPAMMGKSKA QQRLMDNLEE
EFGKVQREFH LPAGDFPSVE HFREVLGGYN IDKFEKLKPK MIQAVDDMLG YDIPDLLKKF
RNPYDN
