EHD2_HUMAN
ID EHD2_HUMAN Reviewed; 543 AA.
AC Q9NZN4; B2RDH9; B4DNU6; Q96CB6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=EH domain-containing protein 2 {ECO:0000305};
DE AltName: Full=PAST homolog 2 {ECO:0000305};
GN Name=EHD2 {ECO:0000312|HGNC:HGNC:3243};
GN Synonyms=PAST2 {ECO:0000312|HGNC:HGNC:3243};
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=Fetal 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).
RA Benjamin S., Horowitz M.;
RT "hEHD2, an EH domain containing protein-2.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Placenta;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [7]
RP PROTEIN SEQUENCE OF 33-41; 168-176; 270-280 AND 342-358.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
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 [10]
RP INTERACTION WITH MYOF.
RX PubMed=18502764; DOI=10.1074/jbc.m802306200;
RA Doherty K.R., Demonbreun A.R., Wallace G.Q., Cave A., Posey A.D.,
RA Heretis K., Pytel P., McNally E.M.;
RT "The endocytic recycling protein EHD2 interacts with myoferlin to regulate
RT myoblast fusion.";
RL J. Biol. Chem. 283:20252-20260(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND SER-468, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP INTERACTION WITH PACSIN2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-72;
RP THR-94; LYS-120; PHE-122; PHE-128; HIS-192 AND LYS-193.
RX PubMed=22323287; DOI=10.1091/mbc.e11-09-0787;
RA Moren B., Shah C., Howes M.T., Schieber N.L., McMahon H.T., Parton R.G.,
RA Daumke O., Lundmark R.;
RT "EHD2 regulates caveolar dynamics via ATP-driven targeting and
RT oligomerization.";
RL Mol. Biol. Cell 23:1316-1329(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-468; SER-470 AND
RP SER-484, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND IDENTIFICATION BY
RP 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 [18]
RP FUNCTION, AND INTERACTION WITH CAV1.
RX PubMed=25588833; DOI=10.1242/jcs.161463;
RA Mohan J., Moren B., Larsson E., Holst M.R., Lundmark R.;
RT "Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of
RT caveolae.";
RL J. Cell Sci. 128:979-991(2015).
CC -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC reorganization/tubulation upon ATP hydrolysis (By similarity). Plays a
CC role in membrane trafficking between the plasma membrane and endosomes
CC (PubMed:17233914). Important for the internalization of GLUT4. Required
CC for fusion of myoblasts to skeletal muscle myotubes. Required for
CC normal translocation of FER1L5 to the plasma membrane (By similarity).
CC Regulates the equilibrium between cell surface-associated and cell
CC surface-dissociated caveolae by constraining caveolae at the cell
CC membrane (PubMed:25588833). {ECO:0000250|UniProtKB:Q8BH64,
CC ECO:0000269|PubMed:17233914, ECO:0000269|PubMed:25588833}.
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 (PubMed:17233914). Interacts with MYOF
CC (PubMed:18502764). Interacts with EHBP1. Interacts with FER1L5 (via
CC second C2 domain) (By similarity). Interacts with CAV1 in a
CC cholesterol-dependent manner (PubMed:25588833). Interacts (via EH
CC domain) with PACSIN2 (via NPF motifs); this interaction probably
CC stabilizes the caveolae (PubMed:22323287).
CC {ECO:0000250|UniProtKB:Q8BH64, ECO:0000269|PubMed:17233914,
CC ECO:0000269|PubMed:18502764, ECO:0000269|PubMed:22323287,
CC ECO:0000269|PubMed:25588833}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17233914};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q8BH64}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q8BH64}. Membrane, caveola
CC {ECO:0000269|PubMed:22323287}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8BH64}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8BH64}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q4V8H8}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q4V8H8}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q4V8H8}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8BH64}. Note=Colocalizes with GLUT4 in
CC intracellular tubulovesicular structures that are associated with
CC cortical F-actin. Colocalizes with FER1L5 at plasma membrane in
CC myoblasts and myotubes. {ECO:0000250|UniProtKB:Q8BH64}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NZN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NZN4-2; Sequence=VSP_056212;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and moderately expressed
CC in placenta, lung, and skeletal muscle. {ECO:0000269|PubMed:10673336}.
CC -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target
CC proteins. {ECO:0000269|PubMed:22323287}.
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; AF181263; AAF40470.1; -; mRNA.
DR EMBL; AF454952; AAL51078.1; -; mRNA.
DR EMBL; AK298067; BAG60358.1; -; mRNA.
DR EMBL; AK315548; BAG37926.1; -; mRNA.
DR EMBL; AC008745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57505.1; -; Genomic_DNA.
DR EMBL; BC014445; AAH14445.1; -; mRNA.
DR CCDS; CCDS12704.1; -. [Q9NZN4-1]
DR RefSeq; NP_055416.2; NM_014601.3. [Q9NZN4-1]
DR AlphaFoldDB; Q9NZN4; -.
DR SMR; Q9NZN4; -.
DR BioGRID; 119056; 71.
DR IntAct; Q9NZN4; 20.
DR MINT; Q9NZN4; -.
DR STRING; 9606.ENSP00000263277; -.
DR iPTMnet; Q9NZN4; -.
DR MetOSite; Q9NZN4; -.
DR PhosphoSitePlus; Q9NZN4; -.
DR SwissPalm; Q9NZN4; -.
DR BioMuta; EHD2; -.
DR DMDM; 57015322; -.
DR CPTAC; CPTAC-1605; -.
DR EPD; Q9NZN4; -.
DR jPOST; Q9NZN4; -.
DR MassIVE; Q9NZN4; -.
DR MaxQB; Q9NZN4; -.
DR PaxDb; Q9NZN4; -.
DR PeptideAtlas; Q9NZN4; -.
DR PRIDE; Q9NZN4; -.
DR ProteomicsDB; 4726; -.
DR ProteomicsDB; 83459; -. [Q9NZN4-1]
DR TopDownProteomics; Q9NZN4-1; -. [Q9NZN4-1]
DR Antibodypedia; 31594; 211 antibodies from 31 providers.
DR DNASU; 30846; -.
DR Ensembl; ENST00000263277.8; ENSP00000263277.2; ENSG00000024422.12. [Q9NZN4-1]
DR Ensembl; ENST00000538399.1; ENSP00000439036.1; ENSG00000024422.12. [Q9NZN4-2]
DR GeneID; 30846; -.
DR KEGG; hsa:30846; -.
DR MANE-Select; ENST00000263277.8; ENSP00000263277.2; NM_014601.4; NP_055416.2.
DR UCSC; uc002phj.5; human. [Q9NZN4-1]
DR CTD; 30846; -.
DR DisGeNET; 30846; -.
DR GeneCards; EHD2; -.
DR HGNC; HGNC:3243; EHD2.
DR HPA; ENSG00000024422; Low tissue specificity.
DR MIM; 605890; gene.
DR neXtProt; NX_Q9NZN4; -.
DR OpenTargets; ENSG00000024422; -.
DR PharmGKB; PA27678; -.
DR VEuPathDB; HostDB:ENSG00000024422; -.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000159256; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q9NZN4; -.
DR OMA; CEKMQEL; -.
DR PhylomeDB; Q9NZN4; -.
DR TreeFam; TF314429; -.
DR PathwayCommons; Q9NZN4; -.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9NZN4; -.
DR BioGRID-ORCS; 30846; 14 hits in 1087 CRISPR screens.
DR ChiTaRS; EHD2; human.
DR GeneWiki; EHD2; -.
DR GenomeRNAi; 30846; -.
DR Pharos; Q9NZN4; Tbio.
DR PRO; PR:Q9NZN4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NZN4; protein.
DR Bgee; ENSG00000024422; Expressed in stromal cell of endometrium and 178 other tissues.
DR ExpressionAtlas; Q9NZN4; baseline and differential.
DR Genevisible; Q9NZN4; HS.
DR GO; GO:0005901; C:caveola; IDA:MGI.
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:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0003676; F:nucleic acid binding; TAS:ProtInc.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0032456; P:endocytic recycling; IGI:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
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 Alternative splicing; ATP-binding; Calcium; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Endosome; Hydrolase; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..543
FT /note="EH domain-containing protein 2"
FT /id="PRO_0000146111"
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 523..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 120..122
FT /note="KPF loop; caveolar targeting"
FT /evidence="ECO:0000269|PubMed:22323287"
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:0000250|UniProtKB:Q4V8H8"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V8H8"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056212"
FT VARIANT 57
FT /note="G -> S (in dbSNP:rs34140460)"
FT /id="VAR_033917"
FT MUTAGEN 72
FT /note="T->A: Incapable of binding membranes and localizing
FT to caveolae."
FT /evidence="ECO:0000269|PubMed:22323287"
FT MUTAGEN 94
FT /note="T->A: Lowers the level of CAV1; distorded caveolae."
FT /evidence="ECO:0000269|PubMed:22323287"
FT MUTAGEN 120
FT /note="K->N: Complete loss of localization to CAV1 positive
FT caveolae."
FT /evidence="ECO:0000269|PubMed:22323287"
FT MUTAGEN 122
FT /note="F->A: Complete loss of localization to CAV1 positive
FT caveolae."
FT /evidence="ECO:0000269|PubMed:22323287"
FT MUTAGEN 128
FT /note="F->A: No effect on caveolae targeting."
FT /evidence="ECO:0000269|PubMed:22323287"
FT MUTAGEN 192
FT /note="H->D: Distorded caveolae."
FT /evidence="ECO:0000269|PubMed:22323287"
FT MUTAGEN 193
FT /note="K->D: Distorded caveolae."
FT /evidence="ECO:0000269|PubMed:22323287"
FT CONFLICT 96
FT /note="C -> F (in Ref. 1; AAF40470)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="R -> G (in Ref. 1; AAF40470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 61161 MW; 0EBF691B0A707359 CRC64;
MFSWLKRGGA RGQQPEAIRT VTSALKELYR TKLLPLEEHY RFGAFHSPAL EDADFDGKPM
VLVAGQYSTG KTSFIQYLLE QEVPGSRVGP EPTTDCFVAV MHGDTEGTVP GNALVVDPDK
PFRKLNPFGN TFLNRFMCAQ LPNQVLESIS IIDTPGILSG AKQRVSRGYD FPAVLRWFAE
RVDLIILLFD AHKLEISDEF SEAIGALRGH EDKIRVVLNK ADMVETQQLM RVYGALMWAL
GKVVGTPEVL RVYIGSFWSQ PLLVPDNRRL FELEEQDLFR DIQGLPRHAA LRKLNDLVKR
ARLVRVHAYI ISYLKKEMPS VFGKENKKKQ LILKLPVIFA KIQLEHHISP GDFPDCQKMQ
ELLMAHDFTK FHSLKPKLLE ALDEMLTHDI AKLMPLLRQE ELESTEVGVQ GGAFEGTHMG
PFVERGPDEA MEDGEEGSDD EAEWVVTKDK SKYDEIFYNL APADGKLSGS KAKTWMVGTK
LPNSVLGRIW KLSDVDRDGM LDDEEFALAS HLIEAKLEGH GLPANLPRRL VPPSKRRHKG
SAE
