P26040 (EZRI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ezrin

Alternative name(s):
Cytovillin
Villin-2
p81

Gene names

Name:	Ezr
Synonyms:	Vil2

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	586 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis By similarity.
Enzyme regulation	A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding. Ref.5
Subunit structure	Interacts with MCC, MPP5, PLEKHG6, SCYL3/PACE1, SLC9A3R1, SLC9A3R2 and TMEM8B. Found in a complex with EZR, PODXL and SLC9A3R2. Interacts with PODXL and SLC9A3R2. Interacts (when phosphorylated) with FES/FPS By similarity.
Subcellular location	Apical cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection By similarity. Cell projection › microvillus membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cell cortex By similarity. Cytoplasm › cytoskeleton By similarity. Note: Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Microvillar peripheral membrane protein (cytoplasmic side). Localizes to cell extensions and peripheral processes of astrocytes By similarity.
Tissue specificity	Expressed in cerebrum and cerebellum (at protein level). Component of the microvilli of intestinal epithelial cells. Ref.6
Developmental stage	Detected in whole embryo from E5 with highest expression at E8, E11, E12, and E18. Expressed at E18 in brain, a clear reduction occurs after birth followed by a transient increase around 2 weeks to 1 month. Hardly detected in adult brain. Ref.6
Post-translational modification	Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding. Ref.5
Sequence similarities	Contains 1 FERM domain.

Ontologies

Keywords
Biological process	Cell shape
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin filament bundle assembly Inferred from sequence or structural similarity. Source: UniProtKB epithelial cell differentiation Inferred from electronic annotation. Source: Compara establishment or maintenance of apical/basal cell polarity Inferred from mutant phenotype PubMed 15177033. Source: MGI leukocyte cell-cell adhesion Inferred from electronic annotation. Source: Compara membrane to membrane docking Inferred from electronic annotation. Source: Compara regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	actin filament Inferred from sequence or structural similarity. Source: UniProtKB apical plasma membrane Inferred from direct assay PubMed 14625387. Source: MGI basolateral plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: Compara extrinsic to membrane Inferred from sequence or structural similarity. Source: UniProtKB filopodium Inferred from electronic annotation. Source: Compara focal adhesion Inferred from electronic annotation. Source: Compara microtubule basal body Inferred from direct assay PubMed 14996907. Source: MGI microvillus Inferred from direct assay PubMed 17138661PubMed 20551175. Source: MGI microvillus membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: Compara ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell uropod Inferred from direct assay PubMed 11728336. Source: MGI
Molecular_function	actin filament binding Inferred from sequence or structural similarity. Source: UniProtKB cell adhesion molecule binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 586	585	Ezrin		PRO_0000219409
Regions
	Domain	2 – 295	294	FERM
	Region	244 – 586	343	Interaction with SCYL3 By similarity
Amino acid modifications
	Modified residue	60	1	N6-acetyllysine By similarity
	Modified residue	146	1	Phosphotyrosine; by PDGFR By similarity
	Modified residue	354	1	Phosphotyrosine; by PDGFR By similarity
	Modified residue	535	1	Phosphoserine By similarity
	Modified residue	567	1	Phosphothreonine; by ROCK2 and PKC/PRKCI Probable
Experimental info
	Sequence conflict	48	1	Q → P in CAA43086. Ref.1
	Sequence conflict	325	1	T → A in CAA43086. Ref.1
	Sequence conflict	570	1	Q → R in BAB22341. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P26040 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 5B7728F575F6DE3E	FASTA	586	69,407
	10 20 30 40 50 60 MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EVWYFGLQYV DNKGFPTWLK 70 80 90 100 110 120 LDKKVSAQEV RKENPVQFKF RAKFYPEDVA EELIQDITQK LFFLQVKDGI LSDEIYCPPE 130 140 150 160 170 180 TAVLLGSYAV QAKFGDYNKE MHKSGYLSSE RLIPQRVMDQ HKLSRDQWED RIQVWHAEHR 190 200 210 220 230 240 GMLKDSAMLE YLKIAQDLEM YGINYFEIKN KKGTDLWLGV DALGLNIYEK DDKLTPKIGF 250 260 270 280 290 300 PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LQLCMGNHEL YMRRRKPDTI 310 320 330 340 350 360 EVQQMKAQAR EEKHQKQLER QQLETEKKRR ETVEREKEQM LREKEELMLR LQDYEQKTKR 370 380 390 400 410 420 AEKELSEQIE KALQLEEERR RAQEEAERLE ADRMAALRAK EELERQAQDQ IKSQEQLAAE 430 440 450 460 470 480 LAEYTAKIAL LEEARRRKED EVEEWQHRAK EAQDDLVKTK EELHLVMTAP PPPPPPVYEP 490 500 510 520 530 540 VNYHVQEGLQ DEGAEPMGYS AELSSEGILD DRNEEKRITE AEKNERVQRQ LLTLSNELSQ 550 560 570 580 ARDENKRTHN DIIHNENMRQ GRDKYKTLRQ IRQGNTKQRI DEFEAM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Radixin is a novel member of the band 4.1 family." Funayama N., Nagafuchi A., Sato N., Tsukita S., Tsukita S. J. Cell Biol. 115:1039-1048(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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: Kidney.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	Lubec G., Klug S. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 264-273, MASS SPECTROMETRY. Tissue: Hippocampus.
[5]	"Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association." Matsui T., Maeda M., Doi Y., Yonemura S., Amano M., Kaibuchi K., Tsukita S., Tsukita S. J. Cell Biol. 140:647-657(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-567, ENZYME REGULATION.
[6]	"Characterization of the NF2 protein merlin and the ERM protein ezrin in human, rat, and mouse central nervous system." Groenholm M., Teesalu T., Tyynelaa J., Piltti K., Boehling T., Wartiovaara K., Vaheri A., Carpen O. Mol. Cell. Neurosci. 28:683-693(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X60671 mRNA. Translation: CAA43086.1. AK002766 mRNA. Translation: BAB22341.1. BC048181 mRNA. Translation: AAH48181.2.
IPI	IPI00330862.
PIR	B41129.
RefSeq	NP_033536.2. NM_009510.2.
UniGene	Mm.277812. Mm.471952.
3D structure databases
ProteinModelPortal	P26040.
SMR	P26040. Positions 1-586.
ModBase	Search...
Protein-protein interaction databases
IntAct	P26040. 3 interactions.
MINT	MINT-1708640.
Protein family/group databases
TCDB	8.A.25.1.1. ezrin/radixin/moesin (Ezrin) family.
PTM databases
PhosphoSite	P26040.
2D gel databases
REPRODUCTION-2DPAGE	P26040.
Proteomic databases
PaxDb	P26040.
PRIDE	P26040.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000064234; ENSMUSP00000063734; ENSMUSG00000052397.
GeneID	22350.
KEGG	mmu:22350.
Organism-specific databases
CTD	7430.
MGI	MGI:98931. Ezr.
Phylogenomic databases
eggNOG	NOG236035.
HOGENOM	HOG000007113.
HOVERGEN	HBG002185.
InParanoid	P26040.
KO	K08007.
OMA	EGAEPMG.
OrthoDB	EOG4C5CJJ.
Gene expression databases
ArrayExpress	P26040.
Bgee	P26040.
CleanEx	MM_EZR.
Genevestigator	P26040.
GermOnline	ENSMUSG00000052397. Mus musculus.
Family and domain databases
Gene3D	1.20.80.10. 1 hit. 2.30.29.30. 1 hit.
InterPro	IPR019749. Band_41_domain. IPR019750. Band_41_fam. IPR011174. ERM. IPR011259. ERM_C_dom. IPR000798. Ez/rad/moesin_like. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR019747. FERM_CS. IPR000299. FERM_domain. IPR018979. FERM_N. IPR018980. FERM_PH-like_C. IPR008954. Moesin. IPR011993. PH_like_dom. [Graphical view]
Pfam	PF00769. ERM. 1 hit. PF09380. FERM_C. 1 hit. PF00373. FERM_M. 1 hit. PF09379. FERM_N. 1 hit. [Graphical view]
PIRSF	PIRSF002305. ERM. 1 hit.
PRINTS	PR00935. BAND41. PR00661. ERMFAMILY.
SMART	SM00295. B41. 1 hit. [Graphical view]
SUPFAM	SSF47031. FERM_3-hlx. 1 hit. SSF48678. Moesin. 1 hit.
PROSITE	PS00660. FERM_1. 1 hit. PS00661. FERM_2. 1 hit. PS50057. FERM_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EZR. mouse.
NextBio	302635.
SOURCE	Search...

Entry information

Entry name

EZRI_MOUSE

Accession

Primary (citable) accession number: P26040
Secondary accession number(s): Q80ZT8, Q9DCI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program