EHD1_RAT
ID EHD1_RAT Reviewed; 534 AA.
AC Q641Z6; B1H289;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=EH domain-containing protein 1 {ECO:0000305};
GN Name=Ehd1 {ECO:0000312|RGD:1309017};
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 [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Kidney, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP INTERACTION WITH PACSIN1 AND PACSIN2.
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 IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP 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).
RN [5]
RP FUNCTION IN NEURITE OUTGROWTH, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP MICALL1 AND RAB35.
RX PubMed=23572513; DOI=10.1242/jcs.117846;
RA Kobayashi H., Fukuda M.;
RT "Rab35 establishes the EHD1-association site by coordinating two distinct
RT effectors during neurite outgrowth.";
RL J. Cell Sci. 126:2424-2435(2013).
CC -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC reorganization/tubulation upon ATP hydrolysis. In vitro causes
CC vesiculation of endocytic membranes (By similarity). Acts in early
CC endocytic membrane fusion and membrane trafficking of recycling
CC endosomes (By similarity). Recruited to endosomal membranes upon nerve
CC growth factor stimulation, indirectly regulates neurite outgrowth
CC (PubMed:23572513). Plays a role in myoblast fusion (By similarity).
CC Involved in the unidirectional retrograde dendritic transport of
CC endocytosed BACE1 and in efficient sorting of BACE1 to axons
CC implicating a function in neuronal APP processing (By similarity).
CC Plays a role in the formation of the ciliary vesicle (CV), an early
CC step in cilium biogenesis. Proposed to be required for the fusion of
CC distal appendage vesicles (DAVs) to form the CV by recruiting SNARE
CC complex component SNAP29. Is required for recruitment of transition
CC zone proteins CEP290, RPGRIP1L, TMEM67 and B9D2, and of IFT20 following
CC DAV reorganization before Rab8-dependent ciliary membrane extension.
CC Required for the loss of CCP110 form the mother centriole essential for
CC the maturation of the basal body during ciliogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000250|UniProtKB:Q9WVK4,
CC ECO:0000269|PubMed:23572513}.
CC -!- SUBUNIT: Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4,
CC ATP-binding is required for heterooligomerization (By similarity).
CC Interacts (via EH domain) with MICALL1 (via NPF1 motif); the
CC interaction is direct and recruits EHD1 to membranes (PubMed:23572513).
CC Interacts with RAB35; the interaction is indirect through MICALL1 and
CC recruits EHD1 to membranes (PubMed:23572513). Interacts (via EH domain)
CC with PACSIN2 (via NPF motifs); regulates localization to tubular
CC recycling endosome membranes (PubMed:15930129). Interacts with PACSIN1
CC (PubMed:15930129). Interacts with RAB8A (By similarity). Interacts with
CC FER1L5 (via second C2 domain) (By similarity). Interacts with MYOF (By
CC similarity). Interacts with ZFYVE20 (By similarity). Interacts (via EH
CC domain) with RAB11FIP2 (By similarity). {ECO:0000250|UniProtKB:Q9H4M9,
CC ECO:0000250|UniProtKB:Q9WVK4, ECO:0000269|PubMed:15930129,
CC ECO:0000269|PubMed:23572513}.
CC -!- INTERACTION:
CC Q641Z6; Q9QY17: Pacsin2; NbExp=2; IntAct=EBI-492911, EBI-491201;
CC Q641Z6; Q9Z2P6: Snap29; NbExp=2; IntAct=EBI-492911, EBI-492883;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:23572513}; Peripheral membrane protein
CC {ECO:0000269|PubMed:23572513}; Cytoplasmic side {ECO:0000305}. Early
CC endosome membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane
CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium
CC membrane {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Preferentially
CC associates with tubular recycling endosomes (By similarity).
CC Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes
CC (By similarity). Localizes to the ciliary pocket from where the cilium
CC protrudes (By similarity). Colocalizes with BACE1 in tubulovesicular
CC cytoplasmic membranes. Colocalizes with BACE1 and APP amyloid beta
CC proteins in hippocampal mossy fiber terminals (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000250|UniProtKB:Q9WVK4}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAI60908.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC082030; AAH82030.1; -; mRNA.
DR EMBL; BC160908; AAI60908.1; ALT_INIT; mRNA.
DR RefSeq; NP_001011939.1; NM_001011939.2.
DR AlphaFoldDB; Q641Z6; -.
DR BMRB; Q641Z6; -.
DR SMR; Q641Z6; -.
DR BioGRID; 254403; 4.
DR IntAct; Q641Z6; 2.
DR STRING; 10116.ENSRNOP00000051714; -.
DR iPTMnet; Q641Z6; -.
DR PhosphoSitePlus; Q641Z6; -.
DR jPOST; Q641Z6; -.
DR PaxDb; Q641Z6; -.
DR PRIDE; Q641Z6; -.
DR Ensembl; ENSRNOT00000054830; ENSRNOP00000051714; ENSRNOG00000043503.
DR GeneID; 293692; -.
DR KEGG; rno:293692; -.
DR UCSC; RGD:1309017; rat.
DR CTD; 10938; -.
DR RGD; 1309017; Ehd1.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000158249; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q641Z6; -.
DR OMA; WYEETIL; -.
DR OrthoDB; 377342at2759; -.
DR PhylomeDB; Q641Z6; -.
DR TreeFam; TF314429; -.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q641Z6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000043503; Expressed in heart and 19 other tissues.
DR Genevisible; Q641Z6; RN.
DR GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0031095; C:platelet dense tubular network membrane; 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:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0016197; P:endosomal transport; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISO:RGD.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; ISS:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
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:SF127; PTHR11216:SF127; 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; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..534
FT /note="EH domain-containing protein 1"
FT /id="PRO_0000306858"
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:Q9H4M9"
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 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:Q9H4M9"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4M9"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 534 AA; 60603 MW; 35502055BC6164F7 CRC64;
MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL EDADFDNKPM
VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV MHGPTEGVVP GNALVVDPRR
PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS IIDTPGILSG EKQRISRGYD FAAVLEWFAE
RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL
GKIINTPEVV RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR
ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISS GDFPSLRKMQ
ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQAVK GGAFDGTMNG
PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV
LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLIPPSK RRHE
