ID EHD1_MOUSE Reviewed; 534 AA.
AC Q9WVK4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=EH domain-containing protein 1 {ECO:0000305};
DE AltName: Full=PAST homolog 1 {ECO:0000305};
DE Short=mPAST1 {ECO:0000312|EMBL:AAF24223.1};
GN Name=Ehd1 {ECO:0000312|MGI:MGI:1341878};
GN Synonyms=Past1 {ECO:0000312|EMBL:AAF24223.1};
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=ICR;
RX PubMed=10395801; DOI=10.1006/geno.1999.5800;
RA Mintz L., Galperin E., Pasmanik-Chor M., Tulzinsky S., Bromberg Y.,
RA Kozak C.A., Joyner A., Fein A., Horowitz M.;
RT "EHD1 -- an EH-domain-containing protein with a specific expression
RT pattern.";
RL Genomics 59:66-76(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Plomann M., Behrendt D., Ritter B., Modregger J., Halback A., Paulsson M.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 FUNCTION, DOMAIN, MUTAGENESIS OF GLY-65 AND TRP-485, AND INTERACTION WITH
RP 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-456, 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 [7]
RP FUNCTION.
RX PubMed=20159556; DOI=10.1016/j.molcel.2009.12.037;
RA Allaire P.D., Marat A.L., Dall'Armi C., Di Paolo G., McPherson P.S.,
RA Ritter B.;
RT "The Connecdenn DENN domain: a GEF for Rab35 mediating cargo-specific exit
RT from early endosomes.";
RL Mol. Cell 37:370-382(2010).
RN [8]
RP FUNCTION, INTERACTION WITH FER1L5 AND MYOF, AND SUBCELLULAR LOCATION.
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 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 [10]
RP INTERACTION WITH MICALL1 AND RAB35.
RX PubMed=23572513; DOI=10.1242/jcs.117846;
RA Kobayashi H., Fukuda M.;
RT "Rab35 establishes the EHD1-association site by coordinating two distinct
RT effectors during neurite outgrowth.";
RL J. Cell Sci. 126:2424-2435(2013).
CC -!- FUNCTION: ATP- and membrane-binding protein that controls membrane
CC reorganization/tubulation upon ATP hydrolysis. In vitro causes
CC vesiculation of endocytic membranes (By similarity). Acts in early
CC endocytic membrane fusion and membrane trafficking of recycling
CC endosomes (PubMed:15930129, PubMed:20159556). Recruited to endosomal
CC membranes upon nerve growth factor stimulation, indirectly regulates
CC neurite outgrowth (By similarity). Plays a role in myoblast fusion
CC (PubMed:21177873). Involved in the unidirectional retrograde dendritic
CC transport of endocytosed BACE1 and in efficient sorting of BACE1 to
CC axons implicating a function in neuronal APP processing
CC (PubMed:24373286). Plays a role in the formation of the ciliary vesicle
CC (CV), an early step in cilium biogenesis. Proposed to be required for
CC the fusion of distal appendage vesicles (DAVs) to form the CV by
CC recruiting SNARE complex component SNAP29. Is required for recruitment
CC of transition zone proteins CEP290, RPGRIP1L, TMEM67 and B9D2, and of
CC IFT20 following DAV reorganization before Rab8-dependent ciliary
CC membrane extension. Required for the loss of CCP110 form the mother
CC centriole essential for the maturation of the basal body during
CC ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q641Z6,
CC ECO:0000250|UniProtKB:Q9H4M9, ECO:0000269|PubMed:15930129,
CC ECO:0000269|PubMed:20159556, ECO:0000269|PubMed:21177873,
CC ECO:0000269|PubMed:24373286}.
CC -!- SUBUNIT: Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4,
CC ATP-binding is required for heterooligomerization (By similarity).
CC Interacts (via EH domain) with MICALL1 (via NPF1 motif); the
CC interaction is direct and recruits EHD1 to membranes (PubMed:23572513).
CC Interacts with RAB35; the interaction is indirect through MICALL1 and
CC recruits EHD1 to membranes (PubMed:23572513). Interacts (via EH domain)
CC with PACSIN2 (via NPF motifs); regulates localization to tubular
CC recycling endosome membranes (PubMed:15930129). Interacts with PACSIN1
CC (PubMed:15930129). Interacts with RAB8A (By similarity). Interacts with
CC FER1L5 (via second C2 domain) (PubMed:21177873). Interacts with MYOF
CC (PubMed:21177873). Interacts with ZFYVE20 (By similarity). Interacts
CC (via EH domain) with RAB11FIP2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000269|PubMed:15930129,
CC ECO:0000269|PubMed:21177873, ECO:0000269|PubMed:23572513}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:21177873}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:24373286}. Cell projection, cilium membrane
CC {ECO:0000250|UniProtKB:Q9H4M9}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Preferentially
CC associates with tubular recycling endosomes (By similarity).
CC Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes
CC (PubMed:21177873). Localizes to the ciliary pocket from where the
CC cilium protrudes (By similarity). Colocalizes with BACE1 in
CC tubulovesicular cytoplasmic membranes. Colocalizes with BACE1 and APP
CC amyloid beta proteins in hippocampal mossy fiber terminals.
CC {ECO:0000250|UniProtKB:Q9H4M9, ECO:0000269|PubMed:21177873,
CC ECO:0000269|PubMed:24373286}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in
CC kidney, heart, intestine, and brain. {ECO:0000269|PubMed:10395801}.
CC -!- DEVELOPMENTAL STAGE: Expression is already noted at day 9.5 in the limb
CC buds and pharyngeal arches and at day 10.5 in sclerotomes, at various
CC elements of the branchial apparatus (mandible and hyoid), and in the
CC occipital region. At day 15.5 expression peaks in cartilage, preceding
CC hypertrophy and ossification, and at day 17.5 there is no expression in
CC the bones. {ECO:0000269|PubMed:10395801}.
CC -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target
CC proteins. {ECO:0000269|PubMed:15930129}.
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; AF099186; AAD45423.1; -; mRNA.
DR EMBL; AF173156; AAF24223.1; -; mRNA.
DR EMBL; AK012896; BAB28540.1; -; mRNA.
DR CCDS; CCDS29501.1; -.
DR RefSeq; NP_034249.1; NM_010119.5.
DR AlphaFoldDB; Q9WVK4; -.
DR BMRB; Q9WVK4; -.
DR SMR; Q9WVK4; -.
DR BioGRID; 199408; 16.
DR DIP; DIP-59491N; -.
DR IntAct; Q9WVK4; 5.
DR STRING; 10090.ENSMUSP00000025684; -.
DR GlyGen; Q9WVK4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9WVK4; -.
DR PhosphoSitePlus; Q9WVK4; -.
DR SwissPalm; Q9WVK4; -.
DR EPD; Q9WVK4; -.
DR jPOST; Q9WVK4; -.
DR MaxQB; Q9WVK4; -.
DR PaxDb; 10090-ENSMUSP00000025684; -.
DR ProteomicsDB; 275908; -.
DR Pumba; Q9WVK4; -.
DR Antibodypedia; 44098; 211 antibodies from 29 providers.
DR DNASU; 13660; -.
DR Ensembl; ENSMUST00000025684.4; ENSMUSP00000025684.4; ENSMUSG00000024772.10.
DR GeneID; 13660; -.
DR KEGG; mmu:13660; -.
DR UCSC; uc008ghz.1; mouse.
DR AGR; MGI:1341878; -.
DR CTD; 10938; -.
DR MGI; MGI:1341878; Ehd1.
DR VEuPathDB; HostDB:ENSMUSG00000024772; -.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000158249; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q9WVK4; -.
DR OMA; PADWESK; -.
DR OrthoDB; 12127at2759; -.
DR PhylomeDB; Q9WVK4; -.
DR TreeFam; TF314429; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 13660; 1 hit in 80 CRISPR screens.
DR ChiTaRS; Ehd1; mouse.
DR PRO; PR:Q9WVK4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9WVK4; Protein.
DR Bgee; ENSMUSG00000024772; Expressed in granulocyte and 77 other cell types or tissues.
DR ExpressionAtlas; Q9WVK4; baseline and differential.
DR Genevisible; Q9WVK4; MM.
DR GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:BHF-UCL.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031095; C:platelet dense tubular network membrane; IDA:BHF-UCL.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0016197; P:endosomal transport; IDA:MGI.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; IMP:BHF-UCL.
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:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR CDD; cd00052; EH; 1.
DR CDD; cd09913; EHD; 1.
DR Gene3D; 1.10.268.20; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR031692; EHD_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
DR PANTHER; PTHR11216:SF161; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE CLONE 15, ISOFORM A; 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; EF-hand; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Endosome;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..534
FT /note="EH domain-containing protein 1"
FT /id="PRO_0000146110"
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:Q9H4M9"
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 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:Q9H4M9"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 65
FT /note="G->R: Abolishes interaction with PACSIN2."
FT /evidence="ECO:0000269|PubMed:15930129"
FT MUTAGEN 485
FT /note="W->A: Abolishes interaction with PACSIN2."
FT /evidence="ECO:0000269|PubMed:15930129"
SQ SEQUENCE 534 AA; 60603 MW; 35502055BC6164F7 CRC64;
MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL EDADFDNKPM
VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV MHGPTEGVVP GNALVVDPRR
PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS IIDTPGILSG EKQRISRGYD FAAVLEWFAE
RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL
GKIINTPEVV RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR
ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISS GDFPSLRKMQ
ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQAVK GGAFDGTMNG
PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV
LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLIPPSK RRHE
//
