ID EHD1_PONAB Reviewed; 534 AA.
AC Q5RBP4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=EH domain-containing protein 1 {ECO:0000305};
GN Name=EHD1 {ECO:0000250|UniProtKB:Q9H4M9};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC reorganization/tubulation upon ATP hydrolysis. Acts in early endocytic
CC membrane fusion and membrane trafficking of recycling endosomes.
CC Recruited to endosomal membranes upon nerve growth factor stimulation,
CC indirectly regulates neurite outgrowth. Plays a role in myoblast
CC fusion. Involved in the unidirectional retrograde dendritic transport
CC of endocytosed BACE1 and in efficient sorting of BACE1 to axons
CC implicating a function in neuronal APP processing. Plays a role in the
CC formation of the ciliary vesicle (CV), an early step in cilium
CC biogenesis. Proposed to be required for the fusion of distal appendage
CC vesicles (DAVs) to form the CV by recruiting SNARE complex component
CC SNAP29. Is required for recruitment of transition zone proteins CEP290,
CC RPGRIP1L, TMEM67 and B9D2, and of IFT20 following DAV reorganization
CC before Rab8-dependent ciliary membrane extension. Required for the loss
CC of CCP110 form the mother centriole essential for the maturation of the
CC basal body during ciliogenesis. {ECO:0000250|UniProtKB:Q641Z6,
CC ECO:0000250|UniProtKB:Q9H4M9, ECO:0000250|UniProtKB:Q9WVK4}.
CC -!- SUBUNIT: Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4,
CC ATP-binding is required for heterooligomerization. Interacts (via EH
CC domain) with MICALL1 (via NPF1 motif); the interaction is direct and
CC recruits EHD1 to membranes. Interacts with RAB35; the interaction is
CC indirect through MICALL1 and recruits EHD1 to membranes. Interacts (via
CC EH domain) with PACSIN2 (via NPF motifs); regulates localization to
CC tubular recycling endosome membranes. Interacts with PACSIN1. Interacts
CC with RAB8A. Interacts with FER1L5 (via second C2 domain). Interacts
CC with MYOF. Interacts with ZFYVE20. Interacts (via EH domain) with
CC RAB11FIP2. {ECO:0000250|UniProtKB:Q9H4M9,
CC ECO:0000250|UniProtKB:Q9WVK4}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC {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}.
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DR EMBL; CR858594; CAH90816.1; -; mRNA.
DR RefSeq; NP_001125465.1; NM_001131993.1.
DR AlphaFoldDB; Q5RBP4; -.
DR BMRB; Q5RBP4; -.
DR SMR; Q5RBP4; -.
DR STRING; 9601.ENSPPYP00000003578; -.
DR Ensembl; ENSPPYT00000003705.3; ENSPPYP00000003578.2; ENSPPYG00000003093.3.
DR GeneID; 100172373; -.
DR KEGG; pon:100172373; -.
DR CTD; 10938; -.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000158249; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q5RBP4; -.
DR OrthoDB; 12127at2759; -.
DR TreeFam; TF314429; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
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:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
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:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR CDD; cd00052; EH; 1.
DR CDD; cd09913; EHD; 1.
DR Gene3D; 1.10.268.20; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR031692; EHD_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
DR PANTHER; PTHR11216:SF161; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE CLONE 15, ISOFORM A; 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; EF-hand; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 2: Evidence at transcript 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_0000306857"
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:0000250|UniProtKB:Q9H4M9"
SQ SEQUENCE 534 AA; 60627 MW; 3330218772A26CE4 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 KIEREHQISP GDFPSLRKMQ
ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQVVK GGAFDGTMNG
PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV
LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLVPPSK RRHE
//
