EHD2_RAT
ID EHD2_RAT Reviewed; 543 AA.
AC Q4V8H8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=EH domain-containing protein 2 {ECO:0000305};
GN Name=Ehd2 {ECO:0000312|RGD:1560856};
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 TISSUE=Placenta;
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 SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14676205; DOI=10.1074/jbc.m307702200;
RA Guilherme A., Soriano N.A., Bose S., Holik J., Bose A., Pomerleau D.P.,
RA Furcinitti P., Leszyk J., Corvera S., Czech M.P.;
RT "EHD2 and the novel EH domain binding protein EHBP1 couple endocytosis to
RT the actin cytoskeleton.";
RL J. Biol. Chem. 279:10593-10605(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-438; SER-470 AND
RP SER-493, AND 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. Plays a role in membrane
CC trafficking between the plasma membrane and endosomes. Important for
CC the internalization of GLUT4. Required for fusion of myoblasts to
CC skeletal muscle myotubes. Required for normal translocation of FER1L5
CC to the plasma membrane. Regulates the equilibrium between cell surface-
CC associated and cell surface-dissociated caveolae by constraining
CC caveolae at the cell membrane. {ECO:0000250|UniProtKB:Q8BH64,
CC ECO:0000250|UniProtKB:Q9NZN4}.
CC -!- ACTIVITY REGULATION: The very low intrinsic ATPase activity is
CC increased upon interaction with liposomes.
CC {ECO:0000250|UniProtKB:Q8BH64}.
CC -!- SUBUNIT: Homodimer and homooligomer. Interacts with EHD1. May also
CC interact with EHD3 and EHD4. Interacts with MYOF. Interacts with EHBP1.
CC Interacts with FER1L5 (via second C2 domain). Interacts with CAV1 in a
CC cholesterol-dependent manner. Interacts (via EH domain) with PACSIN2
CC (via NPF motifs); this interaction probably stabilizes the caveolae (By
CC similarity). {ECO:0000250|UniProtKB:Q8BH64,
CC ECO:0000250|UniProtKB:Q9NZN4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14676205};
CC Peripheral membrane protein {ECO:0000269|PubMed:14676205}; Cytoplasmic
CC side {ECO:0000269|PubMed:14676205}. Membrane, caveola
CC {ECO:0000250|UniProtKB:Q8BH64}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8BH64}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8BH64}. Endosome membrane
CC {ECO:0000269|PubMed:14676205}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14676205}; Cytoplasmic side
CC {ECO:0000269|PubMed:14676205}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:14676205}. Note=Colocalizes with GLUT4 in
CC intracellular tubulovesicular structures that are associated with
CC cortical F-actin (PubMed:14676205). Colocalizes with FER1L5 at plasma
CC membrane in myoblasts and myotubes (By similarity).
CC {ECO:0000250|UniProtKB:Q8BH64, ECO:0000269|PubMed:14676205}.
CC -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target
CC proteins. {ECO:0000250|UniProtKB:Q8BH64}.
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; BC097385; AAH97385.1; -; mRNA.
DR RefSeq; NP_001020068.1; NM_001024897.1.
DR AlphaFoldDB; Q4V8H8; -.
DR SMR; Q4V8H8; -.
DR BioGRID; 262737; 3.
DR STRING; 10116.ENSRNOP00000017353; -.
DR iPTMnet; Q4V8H8; -.
DR PhosphoSitePlus; Q4V8H8; -.
DR jPOST; Q4V8H8; -.
DR PaxDb; Q4V8H8; -.
DR PRIDE; Q4V8H8; -.
DR Ensembl; ENSRNOT00000017353; ENSRNOP00000017353; ENSRNOG00000011346.
DR GeneID; 361512; -.
DR KEGG; rno:361512; -.
DR UCSC; RGD:1560856; rat.
DR CTD; 30846; -.
DR RGD; 1560856; Ehd2.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000159256; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q4V8H8; -.
DR OMA; CEKMQEL; -.
DR OrthoDB; 377342at2759; -.
DR PhylomeDB; Q4V8H8; -.
DR TreeFam; TF314429; -.
DR Reactome; R-RNO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q4V8H8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000011346; Expressed in lung and 18 other tissues.
DR Genevisible; Q4V8H8; RN.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0097320; P:plasma membrane tubulation; 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:0072659; P:protein localization to plasma membrane; ISS: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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR029945; EHD2.
DR InterPro; IPR031692; EHD_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11216:SF62; PTHR11216:SF62; 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 ATP-binding; Calcium; Cell membrane; Cytoplasm; Endosome; Hydrolase;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..543
FT /note="EH domain-containing protein 2"
FT /id="PRO_0000322644"
FT DOMAIN 55..286
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 449..537
FT /note="EH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 481..516
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 REGION 320..340
FT /note="Mediates membrane-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT REGION 521..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
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 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 498
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 BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZN4"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZN4"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 543 AA; 61237 MW; 91585F8842D1DEF4 CRC64;
MFSWLKKGGA RGQRSEAIRT VTSSLKELYR TKLLPLEEHY RFGSFHSPAL EDADFDGKPM
VLVAGQYSTG KTSFIQYLLE QEVPGSRVGP EPTTDCFVAV MHGETEGTVP GNALVVDPEK
PFRKLNPFGN TFLNRFMCAQ LPNQVLESIS IIDTPGILSG AKQRVSRGYD FPAVLRWFAE
RVDLIILLFD AHKLEISDEF SEAIGALRGH EDKIRVVLNK ADMVETQQLM RVYGALMWAL
GKVVGTPEVL RVYIGSFWSQ PLLVPDNRRL FELEEQDLFR DIQGLPRHAA LRKLNDLVKR
ARLVRVHAYI ISYLKKEMPS VFGKENKKKQ LIFKLPVIFA KIQLEHHISP GDFPDCQKMQ
ELLMAHDFTK FHSLKPKLLE ALDEMLTHDI AKLMPLLRQE ELESVEAGVQ GGAFEGTRMG
PFVERGPDEA IEDGEEGSED DAEWVVTKDK SKYDEIFYNL APADGKLSGS KAKTWMVGTK
LPNSVLGRIW KLSDVDRDGM LDDEEFALAS HLIEAKLEGH GLPTNLPRRL VPPSKRRQKG
SAE
