EHD3_RAT
ID EHD3_RAT Reviewed; 535 AA.
AC Q8R491;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=EH domain-containing protein 3 {ECO:0000305};
GN Name=Ehd3 {ECO:0000312|RGD:621762}; Synonyms=Ehd2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Adipose tissue;
RA Park S.Y., Lee W.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH PACSIN1.
RX PubMed=15930129; DOI=10.1091/mbc.e05-01-0076;
RA Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D.,
RA Kessels M.M., Qualmann B.;
RT "EHD proteins associate with syndapin I and II and such interactions play a
RT crucial role in endosomal recycling.";
RL Mol. Biol. Cell 16:3642-3658(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC reorganization/tubulation upon ATP hydrolysis. In vitro causes
CC tubulation of endocytic membranes. Binding to phosphatidic acid induces
CC its membrane tubulation activity. Plays a role in endocytic transport.
CC Involved in early endosome to recycling endosome compartment (ERC),
CC retrograde early endosome to Golgi, and endosome to plasma membrane
CC (rapid recycling) protein transport. Involved in the regulation of
CC Golgi maintenance and morphology. Involved in the recycling of
CC internalized D1 dopamine receptor (By similarity). Plays a role in
CC cardiac protein trafficking probably implicating ANK2. Involved in the
CC ventricular membrane targeting of SLC8A1 and CACNA1C and probably the
CC atrial membrane localization of CACNA1GG and CACNA1H implicated in the
CC regulation of atrial myocyte excitability and cardiac conduction. In
CC conjunction with EHD4 may be involved in endocytic trafficking of
CC KDR/VEGFR2 implicated in control of glomerular function. Involved in
CC the rapid recycling of integrin beta-3 implicated in cell adhesion
CC maintenance. Involved in the unidirectional retrograde dendritic
CC transport of endocytosed BACE1 and in efficient sorting of BACE1 to
CC axons implicating a function in neuronal APP processing. Plays a role
CC in the formation of the ciliary vesicle, an early step in cilium
CC biogenesis; possibly sharing redundant functions with Ehd1.
CC {ECO:0000250|UniProtKB:Q9NZN3, ECO:0000250|UniProtKB:Q9QXY6}.
CC -!- SUBUNIT: Homooligomer, and heterooligomer with EHD1, EHD2 and EHD4,
CC ATP-binding is required for heterooligomerization (By similarity).
CC Interacts with PACSIN1 (By similarity). Interacts with PACSIN2
CC (PubMed:15930129). Interacts (via EH domain) with MICALL1. Interacts
CC (via EH domain) with RAB11FIP2 (By similarity). Interacts with ANK2 (By
CC similarity). Interacts with CACNA1GG and CACNA1H (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZN3, ECO:0000250|UniProtKB:Q9QXY6,
CC ECO:0000269|PubMed:15930129}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9NZN3}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9NZN3}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium
CC membrane {ECO:0000250|UniProtKB:Q9NZN3}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Localizes to the
CC ciliary pocket from where the cilium protrudes. Colocalizes with RAB8A
CC and MYO5B to a cytoplasmic tubular network devoid of RAB11A.
CC Colocalizes with ANK2 in myocyte perinuclear region. Colocalizes with
CC BACE1 in tubulovesicular cytoplasmic membranes. Colocalizes with BACE1
CC and APP amyloid beta proteins in hippocampal mossy fiber terminals.
CC {ECO:0000250|UniProtKB:Q9NZN3, ECO:0000250|UniProtKB:Q9QXY6}.
CC -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target
CC proteins. {ECO:0000250|UniProtKB:Q9WVK4}.
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 ---------------------------------------------------------------------------
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; AF494093; AAM14604.2; -; mRNA.
DR RefSeq; NP_620245.2; NM_138890.2.
DR AlphaFoldDB; Q8R491; -.
DR BMRB; Q8R491; -.
DR SMR; Q8R491; -.
DR BioGRID; 251376; 1.
DR IntAct; Q8R491; 2.
DR MINT; Q8R491; -.
DR STRING; 10116.ENSRNOP00000010419; -.
DR iPTMnet; Q8R491; -.
DR PhosphoSitePlus; Q8R491; -.
DR jPOST; Q8R491; -.
DR PaxDb; Q8R491; -.
DR PRIDE; Q8R491; -.
DR Ensembl; ENSRNOT00000010419; ENSRNOP00000010419; ENSRNOG00000007744.
DR GeneID; 192249; -.
DR KEGG; rno:192249; -.
DR UCSC; RGD:621762; rat.
DR CTD; 30845; -.
DR RGD; 621762; Ehd3.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000159274; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q8R491; -.
DR PhylomeDB; Q8R491; -.
DR TreeFam; TF314429; -.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q8R491; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000007744; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; Q8R491; baseline and differential.
DR Genevisible; Q8R491; RN.
DR GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0034498; P:early endosome to Golgi transport; ISO:RGD.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0090160; P:Golgi to lysosome transport; ISO:RGD.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; ISO:RGD.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0001881; P:receptor recycling; ISO:RGD.
DR GO; GO:1903779; P:regulation of cardiac conduction; ISO:RGD.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; ISO:RGD.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:RGD.
DR GO; GO:1903358; P:regulation of Golgi organization; ISO:RGD.
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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR029951; EHD1/EHD3.
DR InterPro; IPR031692; EHD_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11216:SF67; PTHR11216:SF67; 1.
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; SM00027; EH; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Calcium; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Endosome; Isopeptide bond;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..535
FT /note="EH domain-containing protein 3"
FT /id="PRO_0000322645"
FT DOMAIN 55..286
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 444..532
FT /note="EH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 476..511
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 65..72
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 91..92
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 153..156
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 219..222
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 243
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COILED 198..227
FT /evidence="ECO:0000255"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9NZN3"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 491
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 495
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZN3"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZN3"
FT CROSSLNK 511
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q9NZN3"
SQ SEQUENCE 535 AA; 60791 MW; A719748348CB87D9 CRC64;
MFSWLGNDDR RKKDPEVFQT VSEGLKKLYK TKLLPLEEYY RFHEFHSPAL EDADFDNKPM
VLLVGQYSTG KTTFIRYLLE QDFPGMRIGP EPTTDSFIAV MQGDVEGIIP GNALVVDPKK
PFRKLNAFGN AFLNRFVCAQ LPNAVLESIS VIDTPGILSG EKQRISRGYD FAAVLEWFAE
RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKMRVVLNK ADQIETQQLM RVYGALMWSL
GKIVNTPEVI RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR
ARLAKVHAYI ISSLKKEMPS VFGKDTKKKE LVNNLAEIYG RIEREHQISP GDFPNLKRMQ
DQLQAQDFSK FQPLKSKLLE VVDDMLAHDI AQLMVLVRQE ETQRPVQMVK GGAFEGTLQG
PFGHGYGEGA GEGIDDAEWV VARDKPMYDE IFYTLSPVDG KITGANAKKE MVRSKLPNSV
LGKIWKLADI DKDGMLDDEE FALANHLIKV KLEGHELPSE LPAHLLPPSK RKVAE
