EHD4_MOUSE
ID EHD4_MOUSE Reviewed; 541 AA.
AC Q9EQP2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=EH domain-containing protein 4 {ECO:0000305};
DE AltName: Full=PAST homolog 2 {ECO:0000305};
DE Short=mPAST2 {ECO:0000303|Ref.1};
GN Name=Ehd4 {ECO:0000312|MGI:MGI:1919619};
GN Synonyms=Past2 {ECO:0000303|Ref.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].
RC STRAIN=ICR;
RA Plomann M., Behrendt D., Ritter B., Modregger J., Halbach A., Paulsson M.;
RT "MPAST2, a novel murine isoform of the PAST protein family.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [3]
RP FUNCTION.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-459, 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 [5]
RP 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).
CC -!- FUNCTION: ATP- and membrane-binding protein that probably controls
CC membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in
CC early endosomal transport. {ECO:0000269|PubMed:15930129}.
CC -!- SUBUNIT: Homooligomer, and heterooligomer with EHD1, EHD2 and EHD3.
CC {ECO:0000250|UniProtKB:Q9H223}.
CC -!- INTERACTION:
CC Q9EQP2; Q9QY17: Pacsin2; Xeno; NbExp=4; IntAct=EBI-491022, EBI-491201;
CC Q9EQP2; Q9Z2P6: Snap29; Xeno; NbExp=2; IntAct=EBI-491022, EBI-492883;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9H223}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Recycling endosome
CC membrane {ECO:0000250|UniProtKB:Q9H223}; 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}.
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; AF173639; AAG45672.1; -; mRNA.
DR EMBL; BC007480; AAH07480.1; -; mRNA.
DR CCDS; CCDS16615.1; -.
DR RefSeq; NP_598599.2; NM_133838.4.
DR PDB; 5MTV; X-ray; 2.79 A; A=22-541.
DR PDB; 5MVF; X-ray; 3.27 A; A=22-541.
DR PDBsum; 5MTV; -.
DR PDBsum; 5MVF; -.
DR AlphaFoldDB; Q9EQP2; -.
DR SMR; Q9EQP2; -.
DR BioGRID; 221151; 10.
DR IntAct; Q9EQP2; 6.
DR STRING; 10090.ENSMUSP00000028755; -.
DR iPTMnet; Q9EQP2; -.
DR PhosphoSitePlus; Q9EQP2; -.
DR EPD; Q9EQP2; -.
DR jPOST; Q9EQP2; -.
DR MaxQB; Q9EQP2; -.
DR PaxDb; Q9EQP2; -.
DR PRIDE; Q9EQP2; -.
DR ProteomicsDB; 277814; -.
DR Antibodypedia; 23470; 151 antibodies from 28 providers.
DR DNASU; 98878; -.
DR Ensembl; ENSMUST00000028755; ENSMUSP00000028755; ENSMUSG00000027293.
DR GeneID; 98878; -.
DR KEGG; mmu:98878; -.
DR UCSC; uc008lvd.1; mouse.
DR CTD; 30844; -.
DR MGI; MGI:1919619; Ehd4.
DR VEuPathDB; HostDB:ENSMUSG00000027293; -.
DR eggNOG; KOG1954; Eukaryota.
DR GeneTree; ENSGT00940000158601; -.
DR HOGENOM; CLU_017595_1_1_1; -.
DR InParanoid; Q9EQP2; -.
DR OMA; CDNDGML; -.
DR OrthoDB; 377342at2759; -.
DR PhylomeDB; Q9EQP2; -.
DR TreeFam; TF314429; -.
DR BioGRID-ORCS; 98878; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ehd4; mouse.
DR PRO; PR:Q9EQP2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9EQP2; protein.
DR Bgee; ENSMUSG00000027293; Expressed in interventricular septum and 245 other tissues.
DR ExpressionAtlas; Q9EQP2; baseline and differential.
DR Genevisible; Q9EQP2; MM.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO: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:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
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:0006907; P:pinocytosis; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0030100; P:regulation of endocytosis; 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; IPR029952; EHD4.
DR InterPro; IPR031692; EHD_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11216:SF57; PTHR11216:SF57; 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; Acetylation; ATP-binding; Calcium; Cell membrane; Endosome;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..541
FT /note="EH domain-containing protein 4"
FT /id="PRO_0000146115"
FT DOMAIN 58..289
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 447..535
FT /note="EH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 479..514
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..75
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 94..95
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 156..159
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 222..225
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 246
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 68..75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT BINDING 261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8BH64"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 503
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 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H223"
FT MOD_RES 451
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H223"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:5MTV"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5MTV"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:5MTV"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 229..247
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 271..319
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 338..347
FT /evidence="ECO:0007829|PDB:5MTV"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:5MTV"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:5MVF"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 379..390
FT /evidence="ECO:0007829|PDB:5MTV"
FT HELIX 392..401
FT /evidence="ECO:0007829|PDB:5MTV"
SQ SEQUENCE 541 AA; 61481 MW; D34C28F046D740E1 CRC64;
MFSWMGRQAG GRERSGGMDA VQTVTGGLRS LYQRKVLPLE EAYRFHEFHS PALEDADFEN
KPMILLVGQY STGKTTFIRY LLEQDFPGMR IGPEPTTDSF IAVMYGETEG STPGNALVVD
PKKPFRKLSR FGNAFLNRFM CSQLPNQVLK SISIIDSPGI LSGEKQRISR GYDFCQVLQW
FAERVDRIIL LFDAHKLDIS DEFSEAIKAF RGQDDKIRVV LNKADQVDTQ QLMRVYGALM
WSLGKVINTP EVLRVYIGSF WAQPLQNTDN RRLFEAEAQD LFRDIQSLPQ KAAVRKLNDL
IKRARLAKVH AYIISYLKKE MPNMFGKENK KRELIYRLPE IYVQLQREYQ ISAGDFPEVK
AMQEQLENYD FTKFHSLKPK LIEAVDNMLT NKISSLMGLI SQEEMNMPTQ MVQGGAFDGT
TEGPFNQGYG EGAKEGADEE EWVVAKDKPV YDELFYTLSP INGKISGVNA KKEMVTSKLP
NSVLGKIWKL ADCDCDGMLD EEEFALAKHL IKIKLDGYEL PNSLPPHLVP PSHRKSLPKA
D
