EHD3_HUMAN
ID EHD3_HUMAN Reviewed; 535 AA.
AC Q9NZN3; B4DFR5; D6W574; Q8N514; Q9NZB3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=EH domain-containing protein 3 {ECO:0000305};
DE AltName: Full=PAST homolog 3 {ECO:0000305};
GN Name=EHD3 {ECO:0000312|HGNC:HGNC:3244};
GN Synonyms=EHD2 {ECO:0000303|PubMed:10673336},
GN PAST3 {ECO:0000312|HGNC:HGNC:3244};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10673336; DOI=10.1006/geno.1999.6087;
RA Pohl U., Smith J.S., Tachibana I., Ueki K., Lee H.K., Ramaswamy S., Wu Q.,
RA Mohrenweiser H.W., Jenkins R.B., Louis D.N.;
RT "EHD2, EHD3, and EHD4 encode novel members of a highly conserved family of
RT EH domain-containing proteins.";
RL Genomics 63:255-262(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 1-10, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP FUNCTION, SUBUNIT, INTERACTION WITH RAB11FIP2, ATP-BINDING SITE,
RP MUTAGENESIS OF GLY-65; VAL-203 AND TRP-485, AND SUBCELLULAR LOCATION.
RX PubMed=16251358; DOI=10.1091/mbc.e05-05-0466;
RA Naslavsky N., Rahajeng J., Sharma M., Jovic M., Caplan S.;
RT "Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early
RT endosomal transport.";
RL Mol. Biol. Cell 17:163-177(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=17233914; DOI=10.1186/1471-2121-8-3;
RA George M., Ying G., Rainey M.A., Solomon A., Parikh P.T., Gao Q., Band V.,
RA Band H.;
RT "Shared as well as distinct roles of EHD proteins revealed by biochemical
RT and functional comparisons in mammalian cells and C. elegans.";
RL BMC Cell Biol. 8:3-3(2007).
RN [9]
RP INTERACTION WITH EHD4.
RX PubMed=18331452; DOI=10.1111/j.1600-0854.2008.00732.x;
RA Sharma M., Naslavsky N., Caplan S.;
RT "A role for EHD4 in the regulation of early endosomal transport.";
RL Traffic 9:995-1018(2008).
RN [10]
RP FUNCTION.
RX PubMed=19139087; DOI=10.1242/jcs.037051;
RA Naslavsky N., McKenzie J., Altan-Bonnet N., Sheff D., Caplan S.;
RT "EHD3 regulates early-endosome-to-Golgi transport and preserves Golgi
RT morphology.";
RL J. Cell Sci. 122:389-400(2009).
RN [11]
RP INTERACTION WITH MICALL1.
RX PubMed=19864458; DOI=10.1091/mbc.e09-06-0535;
RA Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.;
RT "MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor
RT recycling.";
RL Mol. Biol. Cell 20:5181-5194(2009).
RN [12]
RP FUNCTION, INTERACTION WITH ANK2, AND SUBCELLULAR LOCATION.
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 [13]
RP FUNCTION.
RX PubMed=21791287; DOI=10.1016/j.neuron.2011.05.036;
RA Kotowski S.J., Hopf F.W., Seif T., Bonci A., von Zastrow M.;
RT "Endocytosis promotes rapid dopaminergic signaling.";
RL Neuron 71:278-290(2011).
RN [14]
RP FUNCTION.
RX PubMed=24019528; DOI=10.1074/jbc.m113.488627;
RA Cai B., Giridharan S.S., Zhang J., Saxena S., Bahl K., Schmidt J.A.,
RA Sorgen P.L., Guo W., Naslavsky N., Caplan S.;
RT "Differential roles of C-terminal Eps15 homology domain proteins as
RT vesiculators and tubulators of recycling endosomes.";
RL J. Biol. Chem. 288:30172-30180(2013).
RN [15]
RP FUNCTION.
RX PubMed=23781025; DOI=10.1242/jcs.122465;
RA Waxmonsky N.C., Conner S.D.;
RT "Alphavbeta3-integrin-mediated adhesion is regulated through an AAK1L- and
RT EHD3-dependent rapid-recycling pathway.";
RL J. Cell Sci. 126:3593-3601(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [18]
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 [19]
RP SUMOYLATION, AND MUTAGENESIS OF LYS-315 AND LYS-511.
RX PubMed=26226295; DOI=10.1371/journal.pone.0134053;
RA Cabasso O., Pekar O., Horowitz M.;
RT "SUMOylation of EHD3 Modulates Tubulation of the Endocytic Recycling
RT Compartment.";
RL PLoS ONE 10:E0134053-E0134053(2015).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP STRUCTURE BY NMR OF 433-535.
RX PubMed=23754701; DOI=10.1007/s12104-013-9497-z;
RA Spagnol G., Reiling C., Kieken F., Caplan S., Sorgen P.L.;
RT "Chemical shift assignments of the C-terminal Eps15 homology domain-3 EH
RT domain.";
RL Biomol. NMR. Assign. 8:263-267(2014).
CC -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC reorganization/tubulation upon ATP hydrolysis (PubMed:25686250). In
CC vitro causes tubulation of endocytic membranes (PubMed:24019528).
CC Binding to phosphatidic acid induces its membrane tubulation activity
CC (By similarity). Plays a role in endocytic transport. Involved in early
CC endosome to recycling endosome compartment (ERC), retrograde early
CC endosome to Golgi, and endosome to plasma membrane (rapid recycling)
CC protein transport. Involved in the regulation of Golgi maintenance and
CC morphology (PubMed:16251358, PubMed:17233914, PubMed:19139087,
CC PubMed:23781025). Involved in the recycling of internalized D1 dopamine
CC receptor (PubMed:21791287). Plays a role in cardiac protein trafficking
CC probably implicating ANK2 (PubMed:20489164). 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 (By
CC similarity). In conjunction with EHD4 may be involved in endocytic
CC trafficking of KDR/VEGFR2 implicated in control of glomerular function
CC (By similarity). Involved in the rapid recycling of integrin beta-3
CC implicated in cell adhesion maintenance (PubMed:23781025). Involved in
CC the unidirectional retrograde dendritic transport of endocytosed BACE1
CC and in efficient sorting of BACE1 to axons implicating a function in
CC neuronal APP processing (By similarity). Plays a role in the formation
CC of the ciliary vesicle, an early step in cilium biogenesis; possibly
CC sharing redundant functions with EHD1 (PubMed:25686250).
CC {ECO:0000250|UniProtKB:Q9QXY6, ECO:0000269|PubMed:16251358,
CC ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:19139087,
CC ECO:0000269|PubMed:21791287, ECO:0000269|PubMed:23781025,
CC ECO:0000269|PubMed:24019528, ECO:0000269|PubMed:25686250,
CC ECO:0000305|PubMed:20489164}.
CC -!- SUBUNIT: Homooligomer, and heterooligomer with EHD1, EHD2 and EHD4,
CC ATP-binding is required for heterooligomerization (PubMed:16251358,
CC PubMed:17233914). Interacts with PACSIN1 (By similarity). Interacts
CC with PACSIN2 (By similarity). Interacts (via EH domain) with MICALL1
CC (PubMed:19864458). Interacts (via EH domain) with RAB11FIP2
CC (PubMed:16251358). Interacts with ANK2 (PubMed:20489164).
CC {ECO:0000250|UniProtKB:Q9QXY6, ECO:0000269|PubMed:16251358,
CC ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:18331452,
CC ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:20489164}.
CC -!- INTERACTION:
CC Q9NZN3; Q01484: ANK2; NbExp=2; IntAct=EBI-2870749, EBI-941975;
CC Q9NZN3; Q9P2R3: ANKFY1; NbExp=3; IntAct=EBI-2870749, EBI-2513908;
CC Q9NZN3; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-2870749, EBI-714543;
CC Q9NZN3; Q9H4M9: EHD1; NbExp=8; IntAct=EBI-2870749, EBI-490691;
CC Q9NZN3; Q8N3F8: MICALL1; NbExp=5; IntAct=EBI-2870749, EBI-1056885;
CC Q9NZN3; Q9QXY6: Ehd3; Xeno; NbExp=5; IntAct=EBI-2870749, EBI-775304;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:17233914}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:17233914}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, cilium
CC membrane {ECO:0000269|PubMed:25686250}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Localizes to the
CC ciliary pocket from where the cilium protrudes (PubMed:25686250).
CC Colocalizes with RAB8A and MYO5B to a cytoplasmic tubular network
CC devoid of RAB11A (By similarity). Colocalizes with ANK2 in myocyte
CC perinuclear region (PubMed:20489164). Colocalizes with BACE1 in
CC tubulovesicular cytoplasmic membranes. Colocalizes with BACE1 and APP
CC amyloid beta proteins in hippocampal mossy fiber terminals (By
CC similarity). {ECO:0000250|UniProtKB:Q9QXY6,
CC ECO:0000269|PubMed:20489164, ECO:0000269|PubMed:25686250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZN3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZN3-2; Sequence=VSP_056606, VSP_056607;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and brain and moderately
CC expressed in kidney, liver, and placenta.
CC {ECO:0000269|PubMed:10673336}.
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=AAF40471.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF181264; AAF40471.1; ALT_FRAME; mRNA.
DR EMBL; AF214736; AAF32285.1; -; mRNA.
DR EMBL; AK294222; BAG57526.1; -; mRNA.
DR EMBL; AK316006; BAH14377.1; -; mRNA.
DR EMBL; AL121657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00480.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00481.1; -; Genomic_DNA.
DR CCDS; CCDS1774.1; -. [Q9NZN3-1]
DR RefSeq; NP_055415.1; NM_014600.2. [Q9NZN3-1]
DR AlphaFoldDB; Q9NZN3; -.
DR BMRB; Q9NZN3; -.
DR SMR; Q9NZN3; -.
DR BioGRID; 119055; 26.
DR IntAct; Q9NZN3; 12.
DR MINT; Q9NZN3; -.
DR STRING; 9606.ENSP00000327116; -.
DR iPTMnet; Q9NZN3; -.
DR MetOSite; Q9NZN3; -.
DR PhosphoSitePlus; Q9NZN3; -.
DR BioMuta; EHD3; -.
DR DMDM; 300669636; -.
DR OGP; Q9NZN3; -.
DR EPD; Q9NZN3; -.
DR jPOST; Q9NZN3; -.
DR MassIVE; Q9NZN3; -.
DR MaxQB; Q9NZN3; -.
DR PaxDb; Q9NZN3; -.
DR PeptideAtlas; Q9NZN3; -.
DR PRIDE; Q9NZN3; -.
DR ProteomicsDB; 4072; -.
DR ProteomicsDB; 83458; -. [Q9NZN3-1]
DR Antibodypedia; 29084; 153 antibodies from 29 providers.
DR DNASU; 30845; -.
DR Ensembl; ENST00000322054.10; ENSP00000327116.5; ENSG00000013016.16. [Q9NZN3-1]
DR GeneID; 30845; -.
DR KEGG; hsa:30845; -.
DR MANE-Select; ENST00000322054.10; ENSP00000327116.5; NM_014600.3; NP_055415.1.
DR UCSC; uc002rnu.4; human. [Q9NZN3-1]
DR CTD; 30845; -.
DR DisGeNET; 30845; -.
DR GeneCards; EHD3; -.
DR HGNC; HGNC:3244; EHD3.
DR HPA; ENSG00000013016; Tissue enhanced (brain, esophagus).
DR MIM; 605891; gene.
DR neXtProt; NX_Q9NZN3; -.
DR OpenTargets; ENSG00000013016; -.
DR PharmGKB; PA27679; -.
DR VEuPathDB; HostDB:ENSG00000013016; -.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000159274; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q9NZN3; -.
DR OMA; KDMPSMF; -.
DR OrthoDB; 377342at2759; -.
DR PhylomeDB; Q9NZN3; -.
DR TreeFam; TF314429; -.
DR PathwayCommons; Q9NZN3; -.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9NZN3; -.
DR BioGRID-ORCS; 30845; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; EHD3; human.
DR GenomeRNAi; 30845; -.
DR Pharos; Q9NZN3; Tbio.
DR PRO; PR:Q9NZN3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NZN3; protein.
DR Bgee; ENSG00000013016; Expressed in lateral nuclear group of thalamus and 172 other tissues.
DR Genevisible; Q9NZN3; HS.
DR GO; GO:0020018; C:ciliary pocket membrane; IDA: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; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IDA: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:0003676; F:nucleic acid binding; TAS:ProtInc.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IDA: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; IMP:UniProtKB.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IPI:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IGI:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0001881; P:receptor recycling; IMP:UniProtKB.
DR GO; GO:1903779; P:regulation of cardiac conduction; IEA:Ensembl.
DR GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; IGI:MGI.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:1903358; P:regulation of Golgi organization; IMP: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; 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; Alternative splicing; ATP-binding; Calcium; Cell membrane;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Direct protein sequencing; Endosome; Isopeptide bond; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..535
FT /note="EH domain-containing protein 3"
FT /id="PRO_0000146112"
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:0000269|PubMed:16251358"
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:0000269|PubMed:12665801"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R491"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXY6"
FT CROSSLNK 315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:26226295"
FT CROSSLNK 511
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:26226295"
FT VAR_SEQ 169..175
FT /note="YDFAAVL -> PAAGPGL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056606"
FT VAR_SEQ 176..535
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056607"
FT MUTAGEN 65
FT /note="G->R: Abolishes ATP-binding and localizes to
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:16251358"
FT MUTAGEN 203
FT /note="V->P: Greatly reduces oligomerization and
FT interaction with RAB11FIP2."
FT /evidence="ECO:0000269|PubMed:16251358"
FT MUTAGEN 315
FT /note="K->R: Abolishes sumoylation and localization to
FT tubular structures of the ERC, impairs fast recycling
FT activity from the ERC, no effect on homooligomerization;
FT when associated with R-511."
FT /evidence="ECO:0000269|PubMed:26226295"
FT MUTAGEN 485
FT /note="W->A: Abolishes interaction with RAB11FIP2."
FT /evidence="ECO:0000269|PubMed:16251358"
FT MUTAGEN 511
FT /note="K->R: Abolishes sumoylation localization to tubular
FT structures of the ERC, impairs fast recycling activity from
FT the ERC, no effect on homooligomerization;; when associated
FT with R-315."
FT /evidence="ECO:0000269|PubMed:26226295"
SQ SEQUENCE 535 AA; 60887 MW; 0F8AE99F84B966AD CRC64;
MFSWLGTDDR RRKDPEVFQT VSEGLKKLYK SKLLPLEEHY RFHEFHSPAL EDADFDNKPM
VLLVGQYSTG KTTFIRYLLE QDFPGMRIGP EPTTDSFIAV MQGDMEGIIP GNALVVDPKK
PFRKLNAFGN AFLNRFVCAQ LPNPVLESIS VIDTPGILSG EKQRISRGYD FAAVLEWFAE
RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKMRVVLNK ADQIETQQLM RVYGALMWSL
GKIVNTPEVI RVYIGSFWSH PLLIPDNRKL FEAEEQDLFR DIQSLPRNAA LRKLNDLIKR
ARLAKVHAYI ISSLKKEMPS VFGKDNKKKE LVNNLAEIYG RIEREHQISP GDFPNLKRMQ
DQLQAQDFSK FQPLKSKLLE VVDDMLAHDI AQLMVLVRQE ESQRPIQMVK GGAFEGTLHG
PFGHGYGEGA GEGIDDAEWV VARDKPMYDE IFYTLSPVDG KITGANAKKE MVRSKLPNSV
LGKIWKLADI DKDGMLDDDE FALANHLIKV KLEGHELPNE LPAHLLPPSK RKVAE
