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   27-MAR-2024, entry version 165.
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,
RC   Pancreas, 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   PDB; 7SOX; EM; 7.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=22-535.
DR   PDBsum; 5MTV; -.
DR   PDBsum; 5MVF; -.
DR   PDBsum; 7SOX; -.
DR   AlphaFoldDB; Q9EQP2; -.
DR   EMDB; EMD-25362; -.
DR   SMR; Q9EQP2; -.
DR   BioGRID; 221151; 12.
DR   IntAct; Q9EQP2; 6.
DR   STRING; 10090.ENSMUSP00000028755; -.
DR   GlyGen; Q9EQP2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9EQP2; -.
DR   PhosphoSitePlus; Q9EQP2; -.
DR   EPD; Q9EQP2; -.
DR   jPOST; Q9EQP2; -.
DR   MaxQB; Q9EQP2; -.
DR   PaxDb; 10090-ENSMUSP00000028755; -.
DR   ProteomicsDB; 277814; -.
DR   Pumba; Q9EQP2; -.
DR   Antibodypedia; 23470; 178 antibodies from 28 providers.
DR   DNASU; 98878; -.
DR   Ensembl; ENSMUST00000028755.8; ENSMUSP00000028755.8; ENSMUSG00000027293.14.
DR   GeneID; 98878; -.
DR   KEGG; mmu:98878; -.
DR   UCSC; uc008lvd.1; mouse.
DR   AGR; MGI:1919619; -.
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; ISAKKEM; -.
DR   OrthoDB; 12127at2759; -.
DR   PhylomeDB; Q9EQP2; -.
DR   TreeFam; TF314429; -.
DR   BioGRID-ORCS; 98878; 1 hit in 78 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 248 other cell types or tissues.
DR   ExpressionAtlas; Q9EQP2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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: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   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.
DR   Genevisible; Q9EQP2; MM.
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
//