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Q9WVK4 (EHD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EH domain-containing protein 1
Alternative name(s):
PAST homolog 1
Short name=mPAST1
Gene names
Name:Ehd1
Synonyms:Past1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Plays a role in myoblast fusion. Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth. Ref.4 Ref.6

Subunit structure

Homooligomer, and heterooligomer with EHD2, EHD3 and EHD4. Interacts (via EH domain) with MICALL1 (via NPF1 motif); the interaction is direct and recruits EHD1 to membranes. Interacts with RAB35; the interaction is indirect through MICALL1 and recruits EHD1 to membranes. Interacts (via EH domain) with PACSIN2 (via NPF motifs); regulates localization to tubular recycling endosome membranes. Interacts with PACSIN1. Interacts with RAB8A. Interacts with FER1L5 (via second C2 domain). Interacts with MYOF. Interacts with ZFYVE20. Ref.4 Ref.6 Ref.7

Subcellular location

Recycling endosome membrane; Peripheral membrane protein By similarity. Early endosome membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Preferentially associates with tubular recycling endosomes. Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes. Ref.4 Ref.6

Tissue specificity

Highly expressed in testis. Also expressed in kidney, heart, intestine, and brain.

Developmental stage

Expression is already noted at day 9.5 in the limb buds and pharyngeal arches and at day 10.5 in sclerotomes, at various elements of the branchial apparatus (mandible and hyoid), and in the occipital region. At day 15.5 expression peaks in cartilage, preceding hypertrophy and ossification, and at day 17.5 there is no expression in the bones.

Domain

The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins. Ref.4

Sequence similarities

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. EHD subfamily.

Contains 1 dynamin-type G (guanine nucleotide-binding) domain.

Contains 1 EF-hand domain.

Contains 1 EH domain.

Ontologies

Keywords
   Cellular componentCell membrane
Endosome
Membrane
   DomainCoiled coil
   LigandATP-binding
Calcium
Metal-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to nerve growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cholesterol homeostasis

Inferred from mutant phenotype PubMed 17451652. Source: BHF-UCL

endocytic recycling

Inferred from sequence or structural similarity. Source: UniProtKB

endocytosis

Inferred from direct assay PubMed 15247266. Source: MGI

endosomal transport

Inferred from direct assay PubMed 11389441. Source: MGI

intracellular protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

low-density lipoprotein particle clearance

Inferred from mutant phenotype PubMed 17451652. Source: BHF-UCL

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cholesterol storage

Inferred from mutant phenotype PubMed 17451652. Source: BHF-UCL

positive regulation of endocytic recycling

Inferred from mutant phenotype Ref.6. Source: UniProtKB

positive regulation of myoblast fusion

Inferred from mutant phenotype Ref.6. Source: UniProtKB

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentearly endosome

Inferred from direct assay PubMed 11389441. Source: MGI

early endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

endocytic vesicle

Inferred from direct assay PubMed 12121420. Source: MGI

endosome

Inferred from direct assay PubMed 15247266. Source: MGI

endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

lipid particle

Inferred from direct assay PubMed 17451652. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from direct assay PubMed 20489164. Source: MGI

plasma membrane

Inferred from direct assay Ref.6. Source: UniProtKB

platelet dense tubular network membrane

Inferred from direct assay PubMed 17451652. Source: BHF-UCL

recycling endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTP binding

Inferred from electronic annotation. Source: InterPro

GTPase activity

Inferred from electronic annotation. Source: InterPro

calcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 12121420PubMed 15247266PubMed 20489164. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 534534EH domain-containing protein 1
PRO_0000146110

Regions

Domain55 – 286232Dynamin-type G
Domain444 – 53289EH
Domain476 – 51136EF-hand
Nucleotide binding65 – 728ATP By similarity
Calcium binding489 – 50012 By similarity
Coiled coil198 – 22730 Potential

Sites

Binding site2201ATP By similarity
Binding site2581ATP By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue4561Phosphoserine By similarity

Experimental info

Mutagenesis651G → R: Abolishes interaction with PACSIN2. Ref.4
Mutagenesis4851W → A: Abolishes interaction with PACSIN2. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9WVK4 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 35502055BC6164F7

FASTA53460,603
        10         20         30         40         50         60 
MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL EDADFDNKPM 

        70         80         90        100        110        120 
VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV MHGPTEGVVP GNALVVDPRR 

       130        140        150        160        170        180 
PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS IIDTPGILSG EKQRISRGYD FAAVLEWFAE 

       190        200        210        220        230        240 
RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL 

       250        260        270        280        290        300 
GKIINTPEVV RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR 

       310        320        330        340        350        360 
ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISS GDFPSLRKMQ 

       370        380        390        400        410        420 
ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQAVK GGAFDGTMNG 

       430        440        450        460        470        480 
PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV 

       490        500        510        520        530 
LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLIPPSK RRHE 

« Hide

References

« Hide 'large scale' references
[1]"EHD1 -- an EH-domain-containing protein with a specific expression pattern."
Mintz L., Galperin E., Pasmanik-Chor M., Tulzinsky S., Bromberg Y., Kozak C.A., Joyner A., Fein A., Horowitz M.
Genomics 59:66-76(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
[2]Plomann M., Behrendt D., Ritter B., Modregger J., Halback A., Paulsson M.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[4]"EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling."
Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D., Kessels M.M., Qualmann B.
Mol. Biol. Cell 16:3642-3658(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF GLY-65 AND TRP-485, INTERACTION WITH PACSIN1 AND PACSIN2.
[5]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Endocytic recycling proteins EHD1 and EHD2 interact with fer-1-like-5 (Fer1L5) and mediate myoblast fusion."
Posey A.D. Jr., Pytel P., Gardikiotes K., Demonbreun A.R., Rainey M., George M., Band H., McNally E.M.
J. Biol. Chem. 286:7379-7388(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FER1L5 AND MYOF, SUBCELLULAR LOCATION.
[7]"Rab35 establishes the EHD1-association site by coordinating two distinct effectors during neurite outgrowth."
Kobayashi H., Fukuda M.
J. Cell Sci. 126:2424-2435(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MICALL1 AND RAB35.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF099186 mRNA. Translation: AAD45423.1.
AF173156 mRNA. Translation: AAF24223.1.
AK012896 mRNA. Translation: BAB28540.1.
CCDSCCDS29501.1.
RefSeqNP_034249.1. NM_010119.5.
UniGeneMm.30169.

3D structure databases

ProteinModelPortalQ9WVK4.
SMRQ9WVK4. Positions 1-534.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199408. 1 interaction.
DIPDIP-59491N.
IntActQ9WVK4. 3 interactions.
MINTMINT-4998512.

PTM databases

PhosphoSiteQ9WVK4.

Proteomic databases

MaxQBQ9WVK4.
PaxDbQ9WVK4.
PRIDEQ9WVK4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025684; ENSMUSP00000025684; ENSMUSG00000024772.
GeneID13660.
KEGGmmu:13660.
UCSCuc008ghz.1. mouse.

Organism-specific databases

CTD10938.
MGIMGI:1341878. Ehd1.

Phylogenomic databases

eggNOGNOG136252.
GeneTreeENSGT00700000104190.
HOVERGENHBG018183.
InParanoidQ9WVK4.
KOK12483.
OMAQAYIISS.
OrthoDBEOG757CX9.
PhylomeDBQ9WVK4.
TreeFamTF314429.

Gene expression databases

ArrayExpressQ9WVK4.
BgeeQ9WVK4.
CleanExMM_EHD1.
GenevestigatorQ9WVK4.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR001401. Dynamin_GTPase.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00350. Dynamin_N. 1 hit.
[Graphical view]
SMARTSM00027. EH. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50031. EH. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio284400.
PROQ9WVK4.
SOURCESearch...

Entry information

Entry nameEHD1_MOUSE
AccessionPrimary (citable) accession number: Q9WVK4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot