Q9WVK4 (EHD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
EH domain-containing protein 1

Alternative name(s):
PAST homolog 1
Short name=mPAST1

Gene names

Name:	Ehd1
Synonyms:	Past1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	534 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Ref.4
Subunit structure	Homodimer, and heterodimer with EHD2, EHD3 and EHD4. Interacts with ZFYVE20 By similarity. Interacts with PACSIN1 and PACSIN2. Ref.4
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein By similarity Ref.4.
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	Contains 1 EF-hand domain. Contains 1 EH domain.

Ontologies

Keywords
Cellular component	Cell membrane Endosome Membrane
Domain	Coiled coil
Ligand	ATP-binding Calcium Metal-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC 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 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 positive regulation of cholesterol storage Inferred from mutant phenotype PubMed 17451652. Source: BHF-UCL protein homooligomerization Inferred from electronic annotation. Source: Compara
Cellular_component	early endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB endocytic vesicle Inferred from direct assay PubMed 12121420. Source: MGI 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 PubMed 15247266. Source: MGI 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_function	ATP 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 534	534	EH domain-containing protein 1		PRO_0000146110
Regions
	Domain	444 – 532	89	EH
	Domain	476 – 511	36	EF-hand
	Nucleotide binding	65 – 72	8	ATP By similarity
	Calcium binding	489 – 500	12	By similarity
	Coiled coil	198 – 227	30	Potential
Sites
	Binding site	220	1	ATP By similarity
	Binding site	258	1	ATP By similarity
Amino acid modifications
	Modified residue	456	1	Phosphoserine By similarity
Experimental info
	Mutagenesis	65	1	G → R: Abolishes interaction with PACSIN2. Ref.4
	Mutagenesis	485	1	W → A: Abolishes interaction with PACSIN2. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9WVK4 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 35502055BC6164F7	FASTA	534	60,603
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.
IPI	IPI00126083.
RefSeq	NP_034249.1. NM_010119.5.
UniGene	Mm.30169.
3D structure databases
ProteinModelPortal	Q9WVK4.
SMR	Q9WVK4. Positions 19-534.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59491N.
PTM databases
PhosphoSite	Q9WVK4.
Proteomic databases
PaxDb	Q9WVK4.
PRIDE	Q9WVK4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025684; ENSMUSP00000025684; ENSMUSG00000024772.
GeneID	13660.
KEGG	mmu:13660.
Organism-specific databases
CTD	10938.
MGI	MGI:1341878. Ehd1.
Phylogenomic databases
eggNOG	NOG136252.
GeneTree	ENSGT00700000104190.
HOVERGEN	HBG018183.
InParanoid	Q9WVK4.
KO	K12483.
OMA	QAYIISS.
OrthoDB	EOG418BN4.
Gene expression databases
ArrayExpress	Q9WVK4.
Bgee	Q9WVK4.
CleanEx	MM_EHD1.
Genevestigator	Q9WVK4.
GermOnline	ENSMUSG00000024772. Mus musculus.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR001401. Dynamin_GTPase. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR000261. EPS15_homology. [Graphical view]
Pfam	PF00350. Dynamin_N. 1 hit. [Graphical view]
SMART	SM00027. EH. 1 hit. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 1 hit. PS50031. EH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	284400.
SOURCE	Search...

Entry information

Entry name

EHD1_MOUSE

Accession

Primary (citable) accession number: Q9WVK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program