EHD2_MOUSE
ID EHD2_MOUSE Reviewed; 543 AA.
AC Q8BH64; Q8BL28;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=EH domain-containing protein 2 {ECO:0000305};
GN Name=Ehd2 {ECO:0000312|MGI:MGI:2154274};
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], FUNCTION, INTERACTION WITH EHBP1, SUBCELLULAR
RP LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND
RP DOMAIN.
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Embryonic eye, Embryonic head, Embryonic lung,
RC Forelimb, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP FUNCTION, INTERACTION WITH MYOF, MUTAGENESIS OF GLY-65, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-438 AND SER-468, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [8]
RP FUNCTION, AND INTERACTION WITH FER1L5 AND MYOF.
RX PubMed=21177873; DOI=10.1074/jbc.m110.157222;
RA Posey A.D. Jr., Pytel P., Gardikiotes K., Demonbreun A.R., Rainey M.,
RA George M., Band H., McNally E.M.;
RT "Endocytic recycling proteins EHD1 and EHD2 interact with fer-1-like-5
RT (Fer1L5) and mediate myoblast fusion.";
RL J. Biol. Chem. 286:7379-7388(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND
RP CALCIUM IONS, SUBUNIT, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF THR-72; THR-94; ILE-157; ARG-167; PHE-322; LYS-324; LYS-327;
RP LYS-328 AND LYS-329.
RX PubMed=17914359; DOI=10.1038/nature06173;
RA Daumke O., Lundmark R., Vallis Y., Martens S., Butler P.J.G., McMahon H.T.;
RT "Architectural and mechanistic insights into an EHD ATPase involved in
RT membrane remodelling.";
RL Nature 449:923-927(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 5-543 IN COMPLEX WITH ATP ANALOG
RP AND CALCIUM IONS, FUNCTION, SUBCELLULAR LOCATION, MEMBRANE-BINDING, AND
RP REGION.
RX PubMed=24508342; DOI=10.1016/j.str.2013.12.015;
RA Shah C., Hegde B.G., Moren B., Behrmann E., Mielke T., Moenke G.,
RA Spahn C.M., Lundmark R., Daumke O., Langen R.;
RT "Structural insights into membrane interaction and caveolar targeting of
RT dynamin-like EHD2.";
RL Structure 22:409-420(2014).
CC -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC reorganization/tubulation upon ATP hydrolysis (PubMed:24508342). Plays
CC a role in membrane trafficking between the plasma membrane and
CC endosomes. Important for the internalization of GLUT4
CC (PubMed:14676205). Required for fusion of myoblasts to skeletal muscle
CC myotubes. Required for normal translocation of FER1L5 to the plasma
CC membrane (PubMed:18502764, PubMed:21177873). Regulates the equilibrium
CC between cell surface-associated and cell surface-dissociated caveolae
CC by constraining caveolae at the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZN4, ECO:0000269|PubMed:14676205,
CC ECO:0000269|PubMed:18502764, ECO:0000269|PubMed:21177873,
CC ECO:0000269|PubMed:24508342}.
CC -!- ACTIVITY REGULATION: The very low intrinsic ATPase activity is
CC increased upon interaction with liposomes.
CC {ECO:0000269|PubMed:17914359}.
CC -!- SUBUNIT: Homodimer and homooligomer (By similarity). Interacts with
CC EHD1 (By similarity). May also interact with EHD3 and EHD4 (By
CC similarity). Interacts with MYOF (PubMed:18502764, PubMed:21177873).
CC Interacts with EHBP1 (PubMed:14676205). Interacts with FER1L5 (via
CC second C2 domain) (PubMed:21177873). Interacts with CAV1 in a
CC cholesterol-dependent manner (By similarity). Interacts (via EH domain)
CC with PACSIN2 (via NPF motifs); this interaction probably stabilizes the
CC caveolae (By similarity). {ECO:0000250|UniProtKB:Q9NZN4,
CC ECO:0000269|PubMed:14676205, ECO:0000269|PubMed:17914359,
CC ECO:0000269|PubMed:18502764, ECO:0000269|PubMed:21177873}.
CC -!- INTERACTION:
CC Q8BH64; Q8BH64: Ehd2; NbExp=6; IntAct=EBI-1994334, EBI-1994334;
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:0000269|PubMed:24508342}; Peripheral membrane protein
CC {ECO:0000269|PubMed:24508342}; Cytoplasmic side
CC {ECO:0000269|PubMed:24508342}. 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: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 (PubMed:18502764).
CC {ECO:0000269|PubMed:14676205, ECO:0000269|PubMed:18502764}.
CC -!- TISSUE SPECIFICITY: Detected in lung and adipocytes. Detected at lower
CC levels in heart and skeletal muscle. {ECO:0000269|PubMed:14676205}.
CC -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target
CC proteins. {ECO:0000269|PubMed:14676205}.
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; AY531389; AAS48536.1; -; mRNA.
DR EMBL; AK031203; BAC27298.1; -; mRNA.
DR EMBL; AK046566; BAC32789.1; -; mRNA.
DR EMBL; AK048356; BAC33310.1; -; mRNA.
DR EMBL; AK050243; BAC34142.1; -; mRNA.
DR EMBL; AK084455; BAC39188.1; -; mRNA.
DR EMBL; AK085016; BAC39339.1; -; mRNA.
DR EMBL; BC113161; AAI13162.1; -; mRNA.
DR CCDS; CCDS20842.1; -.
DR RefSeq; NP_694708.2; NM_153068.3.
DR RefSeq; XP_011248884.1; XM_011250582.2.
DR PDB; 2QPT; X-ray; 3.10 A; A=1-543.
DR PDB; 4CID; X-ray; 3.00 A; A=5-543.
DR PDBsum; 2QPT; -.
DR PDBsum; 4CID; -.
DR AlphaFoldDB; Q8BH64; -.
DR SMR; Q8BH64; -.
DR BioGRID; 234420; 3.
DR DIP; DIP-46806N; -.
DR ELM; Q8BH64; -.
DR IntAct; Q8BH64; 7.
DR STRING; 10090.ENSMUSP00000096397; -.
DR iPTMnet; Q8BH64; -.
DR PhosphoSitePlus; Q8BH64; -.
DR SwissPalm; Q8BH64; -.
DR EPD; Q8BH64; -.
DR jPOST; Q8BH64; -.
DR MaxQB; Q8BH64; -.
DR PaxDb; Q8BH64; -.
DR PeptideAtlas; Q8BH64; -.
DR PRIDE; Q8BH64; -.
DR ProteomicsDB; 277566; -.
DR Antibodypedia; 31594; 211 antibodies from 31 providers.
DR DNASU; 259300; -.
DR Ensembl; ENSMUST00000098799; ENSMUSP00000096397; ENSMUSG00000074364.
DR GeneID; 259300; -.
DR KEGG; mmu:259300; -.
DR UCSC; uc009fgt.1; mouse.
DR CTD; 30846; -.
DR MGI; MGI:2154274; Ehd2.
DR VEuPathDB; HostDB:ENSMUSG00000074364; -.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000159256; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q8BH64; -.
DR OMA; CEKMQEL; -.
DR OrthoDB; 377342at2759; -.
DR PhylomeDB; Q8BH64; -.
DR TreeFam; TF314429; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 259300; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Ehd2; mouse.
DR EvolutionaryTrace; Q8BH64; -.
DR PRO; PR:Q8BH64; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BH64; protein.
DR Bgee; ENSMUSG00000074364; Expressed in ascending aorta and 194 other tissues.
DR ExpressionAtlas; Q8BH64; baseline and differential.
DR Genevisible; Q8BH64; MM.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA: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; IDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA: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; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
DR GO; GO:2001137; P:positive regulation of endocytic recycling; IMP:UniProtKB.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR CDD; cd00052; EH; 1.
DR DisProt; DP01940; -.
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 3D-structure; ATP-binding; Calcium; Cell membrane; Cytoplasm; Endosome;
KW Hydrolase; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..543
FT /note="EH domain-containing protein 2"
FT /id="PRO_0000322643"
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:0000269|PubMed:24508342"
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:0000269|PubMed:17914359,
FT ECO:0000269|PubMed:24508342, ECO:0007744|PDB:2QPT,
FT ECO:0007744|PDB:4CID"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:24508342,
FT ECO:0007744|PDB:4CID"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17914359,
FT ECO:0000269|PubMed:24508342, ECO:0007744|PDB:2QPT,
FT ECO:0007744|PDB:4CID"
FT BINDING 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:24508342,
FT ECO:0007744|PDB:2QPT, ECO:0007744|PDB:4CID"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:24508342,
FT ECO:0007744|PDB:2QPT, ECO:0007744|PDB:4CID"
FT BINDING 498
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:24508342,
FT ECO:0007744|PDB:2QPT, ECO:0007744|PDB:4CID"
FT BINDING 500
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:24508342,
FT ECO:0007744|PDB:2QPT, ECO:0007744|PDB:4CID"
FT BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:17914359, ECO:0000269|PubMed:24508342,
FT ECO:0007744|PDB:2QPT, ECO:0007744|PDB:4CID"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V8H8"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZN4"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZN4"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V8H8"
FT MUTAGEN 65
FT /note="G->R: Inhibits myoblast fusion."
FT /evidence="ECO:0000269|PubMed:18502764"
FT MUTAGEN 72
FT /note="T->A: Abolishes ATP binding."
FT /evidence="ECO:0000269|PubMed:17914359"
FT MUTAGEN 94
FT /note="T->A: Abolishes increase of intrinsic ATPase
FT activity upon interaction with membranes."
FT /evidence="ECO:0000269|PubMed:17914359"
FT MUTAGEN 157
FT /note="I->Q: Increases intrinsic ATPase activity."
FT /evidence="ECO:0000269|PubMed:17914359"
FT MUTAGEN 167
FT /note="R->E: Increases intrinsic ATPase activity."
FT /evidence="ECO:0000269|PubMed:17914359"
FT MUTAGEN 322
FT /note="F->A: Abolishes localization at the plasma membrane;
FT reduces increase of intrinsic ATPase activity upon
FT interaction with membranes."
FT /evidence="ECO:0000269|PubMed:17914359"
FT MUTAGEN 324
FT /note="K->D: Abolishes localization at the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:17914359"
FT MUTAGEN 327
FT /note="K->D: Abolishes localization at the plasma membrane;
FT abolishes increase of intrinsic ATPase activity upon
FT interaction with membranes."
FT /evidence="ECO:0000269|PubMed:17914359"
FT MUTAGEN 328
FT /note="K->D: Abolishes localization at the plasma membrane;
FT reduces increase of intrinsic ATPase activity upon
FT interaction with membranes."
FT /evidence="ECO:0000269|PubMed:17914359"
FT MUTAGEN 329
FT /note="K->D: Abolishes localization at the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:17914359"
FT CONFLICT 181
FT /note="R -> S (in Ref. 2; BAC32789)"
FT /evidence="ECO:0000305"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4CID"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 226..244
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2QPT"
FT HELIX 268..283
FT /evidence="ECO:0007829|PDB:4CID"
FT TURN 284..288
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 289..317
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 324..346
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 376..387
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 389..403
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:2QPT"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 447..459
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 469..476
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 483..493
FT /evidence="ECO:0007829|PDB:4CID"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 503..518
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:4CID"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:4CID"
SQ SEQUENCE 543 AA; 61174 MW; 47637795B0B1096E CRC64;
MFSWLKKGGA RGQRPEAIRT 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 ISYLKKEMPT VFGKENKKKQ LILKLPVIFA KIQLEHHISP GDFPDCQKMQ
ELLMAHDFTK FHSLKPKLLE ALDDMLAQDI AKLMPLLRQE ELESVEAGVQ GGAFEGTRMG
PFVERGPDEA IEDGEEGSED DAEWVVTKDK SKYDEIFYNL APADGKLSGS KAKTWMVGTK
LPNSVLGRIW KLSDVDRDGM LDDEEFALAS HLIEAKLEGH GLPTNLPRRL VPPSKRRQKG
SAE
