EHD3_MOUSE
ID EHD3_MOUSE Reviewed; 535 AA.
AC Q9QXY6; Q8K590;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=EH domain-containing protein 3 {ECO:0000305};
GN Name=Ehd3 {ECO:0000312|MGI:MGI:1928900}; Synonyms=Ehd2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP EHD1.
RX PubMed=12121420; DOI=10.1034/j.1600-0854.2002.30807.x;
RA Galperin E., Benjamin S., Rapaport D., Rotem-Yehudar R., Tolchinsky S.,
RA Horowitz M.;
RT "EHD3: a protein that resides in recycling tubular and vesicular membrane
RT structures and interacts with EHD1.";
RL Traffic 3:575-589(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Park S.Y., Lee W.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [5]
RP PROTEIN SEQUENCE OF 33-41; 125-162; 252-268; 270-280 AND 359-370, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17507647; DOI=10.1091/mbc.e07-02-0169;
RA Roland J.T., Kenworthy A.K., Peranen J., Caplan S., Goldenring J.R.;
RT "Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and
RT EHD3.";
RL Mol. Biol. Cell 18:2828-2837(2007).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=17251388; DOI=10.1681/asn.2006060675;
RA Patrakka J., Xiao Z., Nukui M., Takemoto M., He L., Oddsson A., Perisic L.,
RA Kaukinen A., Szigyarto C.A.-K., Uhlen M., Jalanko H., Betsholtz C.,
RA Tryggvason K.;
RT "Expression and subcellular distribution of novel glomerulus-associated
RT proteins Dendrin, Ehd3, Sh2d4a, Plekhh2, and 2310066E14Rik.";
RL J. Am. Soc. Nephrol. 18:689-697(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION.
RX PubMed=20489164; DOI=10.1161/circresaha.110.216713;
RA Gudmundsson H., Hund T.J., Wright P.J., Kline C.F., Snyder J.S., Qian L.,
RA Koval O.M., Cunha S.R., George M., Rainey M.A., Kashef F.E., Dun W.,
RA Boyden P.A., Anderson M.E., Band H., Mohler P.J.;
RT "EH domain proteins regulate cardiac membrane protein targeting.";
RL Circ. Res. 107:84-95(2010).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=21408024; DOI=10.1371/journal.pone.0017838;
RA George M., Rainey M.A., Naramura M., Foster K.W., Holzapfel M.S.,
RA Willoughby L.L., Ying G., Goswami R.M., Gurumurthy C.B., Band V.,
RA Satchell S.C., Band H.;
RT "Renal thrombotic microangiopathy in mice with combined deletion of
RT endocytic recycling regulators EHD3 and EHD4.";
RL PLoS ONE 6:E17838-E17838(2011).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=22974368; DOI=10.1186/2044-5040-2-19;
RA Mate S.E., Van Der Meulen J.H., Arya P., Bhattacharyya S., Band H.,
RA Hoffman E.P.;
RT "Eps homology domain endosomal transport proteins differentially localize
RT to the neuromuscular junction.";
RL Skelet. Muscle 2:19-19(2012).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24373286; DOI=10.1016/j.celrep.2013.12.006;
RA Buggia-Prevot V., Fernandez C.G., Udayar V., Vetrivel K.S., Elie A.,
RA Roseman J., Sasse V.A., Lefkow M., Meckler X., Bhattacharyya S., George M.,
RA Kar S., Bindokas V.P., Parent A.T., Rajendran L., Band H., Vassar R.,
RA Thinakaran G.;
RT "A function for EHD family proteins in unidirectional retrograde dendritic
RT transport of BACE1 and Alzheimer's disease Abeta production.";
RL Cell Rep. 5:1552-1563(2013).
RN [14]
RP FUNCTION.
RX PubMed=24759929; DOI=10.1161/circresaha.115.304149;
RA Curran J., Makara M.A., Little S.C., Musa H., Liu B., Wu X., Polina I.,
RA Alecusan J.S., Wright P., Li J., Billman G.E., Boyden P.A., Gyorke S.,
RA Band H., Hund T.J., Mohler P.J.;
RT "EHD3-dependent endosome pathway regulates cardiac membrane excitability
RT and physiology.";
RL Circ. Res. 115:68-78(2014).
RN [15]
RP FUNCTION, INTERACTION WITH CACNA1GG AND CACNA1H, AND SUBCELLULAR LOCATION.
RX PubMed=25825486; DOI=10.1074/jbc.m115.646893;
RA Curran J., Musa H., Kline C.F., Makara M.A., Little S.C., Higgins J.D.,
RA Hund T.J., Band H., Mohler P.J.;
RT "Eps15 homology domain-containing protein 3 regulates cardiac T-type Ca2+
RT channel targeting and function in the atria.";
RL J. Biol. Chem. 290:12210-12221(2015).
RN [16]
RP FUNCTION.
RX PubMed=25686250; DOI=10.1038/ncb3109;
RA Lu Q., Insinna C., Ott C., Stauffer J., Pintado P.A., Rahajeng J., Baxa U.,
RA Walia V., Cuenca A., Hwang Y.S., Daar I.O., Lopes S.,
RA Lippincott-Schwartz J., Jackson P.K., Caplan S., Westlake C.J.;
RT "Early steps in primary cilium assembly require EHD1/EHD3-dependent ciliary
RT vesicle formation.";
RL Nat. Cell Biol. 17:228-240(2015).
RN [17]
RP ERRATUM OF PUBMED:25686250.
RA Lu Q., Insinna C., Ott C., Stauffer J., Pintado P.A., Rahajeng J., Baxa U.,
RA Walia V., Cuenca A., Hwang Y.S., Daar I.O., Lopes S.,
RA Lippincott-Schwartz J., Jackson P.K., Caplan S., Westlake C.J.;
RL Nat. Cell Biol. 17:531-531(2015).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF LYS-327.
RX PubMed=26896729; DOI=10.1016/j.yexcr.2016.02.011;
RA Henmi Y., Oe N., Kono N., Taguchi T., Takei K., Tanabe K.;
RT "Phosphatidic acid induces EHD3-containing membrane tubulation and is
RT required for receptor recycling.";
RL Exp. Cell Res. 342:1-10(2016).
CC -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC reorganization/tubulation upon ATP hydrolysis. In vitro causes
CC tubulation of endocytic membranes (By similarity). Binding to
CC phosphatidic acid induces its membrane tubulation activity
CC (PubMed:26896729). Plays a role in endocytic transport. Involved in
CC early endosome to recycling endosome compartment (ERC), retrograde
CC early endosome to Golgi, and endosome to plasma membrane (rapid
CC recycling) protein transport. Involved in the regulation of Golgi
CC maintenance and morphology (By similarity). Involved in the recycling
CC of 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
CC (PubMed:20489164, PubMed:24759929, PubMed:25825486). In conjunction
CC with EHD4 may be involved in endocytic trafficking of KDR/VEGFR2
CC implicated in control of glomerular function (PubMed:21408024).
CC Involved in the rapid recycling of integrin beta-3 implicated in cell
CC adhesion maintenance (By similarity). Involved in the unidirectional
CC retrograde dendritic transport of endocytosed BACE1 and in efficient
CC sorting of BACE1 to axons implicating a function in neuronal APP
CC processing. Plays a role in the formation of the ciliary vesicle, an
CC early step in cilium biogenesis; possibly sharing redundant functions
CC with Ehd1 (PubMed:25686250). {ECO:0000250|UniProtKB:Q9NZN3,
CC ECO:0000269|PubMed:20489164, ECO:0000269|PubMed:21408024,
CC ECO:0000269|PubMed:24373286, ECO:0000269|PubMed:24759929,
CC ECO:0000269|PubMed:25686250, ECO:0000269|PubMed:25825486,
CC ECO:0000269|PubMed:26896729}.
CC -!- SUBUNIT: Homooligomer. Heterooligomer with EHD1 (PubMed:12121420).
CC Heterooligomer with EHD2 and EHD4; ATP-binding is required for
CC heterooligomerization (By similarity). Interacts with PACSIN1
CC (PubMed:15930129). Interacts with PACSIN2 (PubMed:15930129). Interacts
CC (via EH domain) with MICALL1 (By similarity). Interacts (via EH domain)
CC with RAB11FIP2 (By similarity). Interacts with ANK2 (By similarity).
CC Interacts with CACNA1GG and CACNA1H (PubMed:25825486).
CC {ECO:0000250|UniProtKB:Q9NZN3, ECO:0000269|PubMed:12121420,
CC ECO:0000269|PubMed:15930129, ECO:0000269|PubMed:25825486}.
CC -!- INTERACTION:
CC Q9QXY6; Q9H4M9: EHD1; Xeno; NbExp=7; IntAct=EBI-775304, EBI-490691;
CC Q9QXY6; Q9NZN3: EHD3; Xeno; NbExp=5; IntAct=EBI-775304, EBI-2870749;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9NZN3, ECO:0000305|PubMed:12121420}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell
CC membrane {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}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:12121420, ECO:0000269|PubMed:24373286}.
CC Note=Localizes to the ciliary pocket from where the cilium protrudes
CC (By similarity). Colocalizes with RAB8A and MYO5B to a cytoplasmic
CC tubular network devoid of RAB11A (PubMed:17507647). Colocalizes with
CC ANK2 in myocyte perinuclear region (PubMed:25825486). Colocalizes with
CC BACE1 in tubulovesicular cytoplasmic membranes. Colocalizes with BACE1
CC and APP amyloid beta proteins in hippocampal mossy fiber terminals
CC (PubMed:24373286). {ECO:0000250|UniProtKB:Q9NZN3,
CC ECO:0000269|PubMed:17507647, ECO:0000269|PubMed:24373286,
CC ECO:0000269|PubMed:25825486}.
CC -!- TISSUE SPECIFICITY: Strong expression seen in the kidney, brain and
CC liver. In the kidney, expressed exclusively by glomerular endothelial
CC cells; at protein level. Expressed in skeletal muscle neuromuscular
CC junction perisynaptic region; at protein level.
CC {ECO:0000269|PubMed:17251388, ECO:0000269|PubMed:21408024,
CC ECO:0000269|PubMed:22974368}.
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; AF155883; AAF19020.1; -; mRNA.
DR EMBL; AF506002; AAM28633.1; -; mRNA.
DR EMBL; AK141265; BAE24623.1; -; mRNA.
DR EMBL; BC046596; AAH46596.1; -; mRNA.
DR CCDS; CCDS28966.1; -.
DR RefSeq; NP_065603.2; NM_020578.3.
DR AlphaFoldDB; Q9QXY6; -.
DR SMR; Q9QXY6; -.
DR BioGRID; 208297; 7.
DR IntAct; Q9QXY6; 12.
DR MINT; Q9QXY6; -.
DR STRING; 10090.ENSMUSP00000024860; -.
DR iPTMnet; Q9QXY6; -.
DR PhosphoSitePlus; Q9QXY6; -.
DR EPD; Q9QXY6; -.
DR jPOST; Q9QXY6; -.
DR MaxQB; Q9QXY6; -.
DR PaxDb; Q9QXY6; -.
DR PeptideAtlas; Q9QXY6; -.
DR PRIDE; Q9QXY6; -.
DR ProteomicsDB; 277695; -.
DR Antibodypedia; 29084; 153 antibodies from 29 providers.
DR DNASU; 57440; -.
DR Ensembl; ENSMUST00000024860; ENSMUSP00000024860; ENSMUSG00000024065.
DR GeneID; 57440; -.
DR KEGG; mmu:57440; -.
DR UCSC; uc008dnn.2; mouse.
DR CTD; 30845; -.
DR MGI; MGI:1928900; Ehd3.
DR VEuPathDB; HostDB:ENSMUSG00000024065; -.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000159274; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q9QXY6; -.
DR OMA; KDMPSMF; -.
DR OrthoDB; 377342at2759; -.
DR PhylomeDB; Q9QXY6; -.
DR TreeFam; TF314429; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 57440; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ehd3; mouse.
DR PRO; PR:Q9QXY6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9QXY6; protein.
DR Bgee; ENSMUSG00000024065; Expressed in gastrula and 208 other tissues.
DR Genevisible; Q9QXY6; MM.
DR GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA: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; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
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:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0034498; P:early endosome to Golgi transport; ISO:MGI.
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:MGI.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0001881; P:receptor recycling; ISO:MGI.
DR GO; GO:1903779; P:regulation of cardiac conduction; IMP:UniProtKB.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; IMP:MGI.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; ISO:MGI.
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; Cytoplasmic vesicle;
KW Direct protein sequencing; Endosome; Isopeptide bond; Lipid-binding;
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_0000146113"
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:0000250|UniProtKB:Q8R491"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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"
FT MUTAGEN 327
FT /note="K->D: Loss of localization to membranes, reduced
FT binding to phosphatidic acid."
FT /evidence="ECO:0000269|PubMed:26896729"
FT CONFLICT 358
FT /note="R -> K (in Ref. 1; AAF19020)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="S -> Y (in Ref. 1; AAF19020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 60821 MW; 80BF1F3B45CB87DF CRC64;
MFSWLGNDDR RKKDPEVFQT VSDGLKKLYK TKLLPLEEYY RFHEFHSPAL EDADFDNKPM
VLLVGQYSTG KTTFIRYLLE QDFPGMRIGP EPTTDSFIAV MQGDVEGIIP GNALVVDPKK
PFRKLNAFGN AFLNRFVCAQ LPNAVLESIS VIDTPGILSG EKQRISRGYD FAAVLEWFAE
RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKMRVVLNK ADQIETQQLM RVYGALMWSL
GKIVNTPEVI RVYIGSFWSH PLLIPDNRKL FEAEEQDLFR 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 RKVSE
