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Protein

Radixin

Gene

Rdx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.

Enzyme regulationi

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei278Phosphatidylinositol1

GO - Molecular functioni

  • actin binding Source: MGI
  • ATPase binding Source: MGI
  • cadherin binding involved in cell-cell adhesion Source: MGI
  • poly(A) RNA binding Source: MGI
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Radixin
Alternative name(s):
ESP10
Gene namesi
Name:Rdx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:97887. Rdx.

Subcellular locationi

GO - Cellular componenti

  • apical part of cell Source: MGI
  • apical plasma membrane Source: MGI
  • cell-cell adherens junction Source: MGI
  • cell periphery Source: MGI
  • cell tip Source: Ensembl
  • cleavage furrow Source: UniProtKB-SubCell
  • cortical actin cytoskeleton Source: UniProtKB
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • extrinsic component of membrane Source: InterPro
  • filopodium Source: UniProtKB
  • focal adhesion Source: MGI
  • lamellipodium Source: UniProtKB
  • microvillus Source: UniProtKB
  • midbody Source: Ensembl
  • myelin sheath Source: UniProtKB
  • plasma membrane Source: MGI
  • ruffle Source: MGI
  • stereocilium Source: MGI
  • T-tubule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194221 – 583RadixinAdd BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei83N6-succinyllysineCombined sources1
Modified residuei564Phosphothreonine; by ROCK21 Publication1

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP26043.
MaxQBiP26043.
PaxDbiP26043.
PeptideAtlasiP26043.
PRIDEiP26043.

2D gel databases

REPRODUCTION-2DPAGEP26043.

PTM databases

iPTMnetiP26043.
PhosphoSitePlusiP26043.
SwissPalmiP26043.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032050.
CleanExiMM_RDX.
ExpressionAtlasiP26043. baseline and differential.
GenevisibleiP26043. MM.

Interactioni

Subunit structurei

Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145). Binds SLC9A3R1 (By similarity). Interacts with LAYN (PubMed:15913605). Interacts with NHERF1 and NHERF2 (PubMed:16615918). Interacts with MME/NEP (PubMed:17459884). Interacts with ICAM2 (PubMed:12554651).By similarity5 Publications

GO - Molecular functioni

  • actin binding Source: MGI
  • ATPase binding Source: MGI
  • cadherin binding involved in cell-cell adhesion Source: MGI
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi202845. 7 interactors.
DIPiDIP-29091N.
IntActiP26043. 5 interactors.
MINTiMINT-1862372.
STRINGi10090.ENSMUSP00000000590.

Structurei

Secondary structure

1583
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Beta strandi15 – 20Combined sources6
Helixi26 – 36Combined sources11
Helixi42 – 44Combined sources3
Beta strandi45 – 51Combined sources7
Beta strandi56 – 58Combined sources3
Beta strandi61 – 64Combined sources4
Helixi65 – 67Combined sources3
Beta strandi74 – 82Combined sources9
Helixi89 – 91Combined sources3
Helixi96 – 111Combined sources16
Helixi119 – 134Combined sources16
Turni139 – 141Combined sources3
Turni144 – 149Combined sources6
Helixi155 – 160Combined sources6
Helixi165 – 178Combined sources14
Turni179 – 181Combined sources3
Helixi184 – 195Combined sources12
Turni199 – 202Combined sources4
Beta strandi204 – 210Combined sources7
Beta strandi215 – 221Combined sources7
Beta strandi224 – 229Combined sources6
Beta strandi232 – 235Combined sources4
Beta strandi237 – 241Combined sources5
Helixi242 – 244Combined sources3
Beta strandi245 – 251Combined sources7
Beta strandi254 – 264Combined sources11
Beta strandi267 – 270Combined sources4
Helixi274 – 293Combined sources20
Helixi300 – 310Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GC6X-ray2.90A1-297[»]
1GC7X-ray2.80A1-297[»]
1J19X-ray2.40A1-310[»]
2D10X-ray2.50A/B/C/D1-310[»]
2D11X-ray2.81A/B/C/D1-310[»]
2D2QX-ray2.80A/B1-310[»]
2EMSX-ray2.90A1-310[»]
2EMTX-ray2.80A/B1-310[»]
2YVCX-ray3.20A/B/C1-310[»]
2ZPYX-ray2.10A1-310[»]
3X23X-ray2.40A1-310[»]
ProteinModelPortaliP26043.
SMRiP26043.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 295FERMPROSITE-ProRule annotationAdd BLAST291

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni60 – 63Phosphatidylinositol binding4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi311 – 522Glu-richAdd BLAST212
Compositional biasi470 – 477Poly-Pro8

Domaini

The N-terminal domain interacts with the C-terminal domain of LAYN. An interdomain interaction between its N-terminal and C-terminal domains inhibits its ability to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN.

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00860000133686.
HOVERGENiHBG002185.
InParanoidiP26043.
KOiK05762.
OMAiLSREDSM.
OrthoDBiEOG091G06UO.
TreeFamiTF313935.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
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_tail.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV
60 70 80 90 100
DSKGYSTWLK LNKKVTQQDV KKENPLQFKF RAKFFPEDVS EELIQEITQR
110 120 130 140 150
LFFLQVKEAI LNDEIYCPPE TAVLLASYAV QAKYGDYNKE IHKPGYLAND
160 170 180 190 200
RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR GMLREDSMME YLKIAQDLEM
210 220 230 240 250
YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF PWSEIRNISF
260 270 280 290 300
NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI
310 320 330 340 350
EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER
360 370 380 390 400
LRQIEEQTVK AQKELEEQTR KALELEQERQ RAKEEAERLD RERRAAEEAK
410 420 430 440 450
SAIAKQAADQ MKNQEQLAAE LAEFTAKIAL LEEAKKKKEE EATEWQHKAF
460 470 480 490 500
AAQEDLEKTK EELKTVMSAP PPPPPPPVIP PTENEHDEQD ENSAEASAEL
510 520 530 540 550
SSEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD ETKKTQNDVL
560 570 580
HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM
Length:583
Mass (Da):68,543
Last modified:July 27, 2011 - v3
Checksum:i25752653017F0879
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti312 – 313EK → VL in CAA43087 (PubMed:1955455).Curated2
Sequence conflicti514R → W in CAA43087 (PubMed:1955455).Curated1
Sequence conflicti575 – 576QR → HA AA sequence (PubMed:1955455).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60672 mRNA. Translation: CAA43087.1.
AK162204 mRNA. Translation: BAE36790.1.
CCDSiCCDS40634.1.
PIRiA41129.
RefSeqiNP_001098086.1. NM_001104616.1.
NP_033067.2. NM_009041.3.
UniGeneiMm.245746.
Mm.472057.

Genome annotation databases

EnsembliENSMUST00000000590; ENSMUSP00000000590; ENSMUSG00000032050.
ENSMUST00000163153; ENSMUSP00000128249; ENSMUSG00000032050.
GeneIDi19684.
KEGGimmu:19684.
UCSCiuc009plq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60672 mRNA. Translation: CAA43087.1.
AK162204 mRNA. Translation: BAE36790.1.
CCDSiCCDS40634.1.
PIRiA41129.
RefSeqiNP_001098086.1. NM_001104616.1.
NP_033067.2. NM_009041.3.
UniGeneiMm.245746.
Mm.472057.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GC6X-ray2.90A1-297[»]
1GC7X-ray2.80A1-297[»]
1J19X-ray2.40A1-310[»]
2D10X-ray2.50A/B/C/D1-310[»]
2D11X-ray2.81A/B/C/D1-310[»]
2D2QX-ray2.80A/B1-310[»]
2EMSX-ray2.90A1-310[»]
2EMTX-ray2.80A/B1-310[»]
2YVCX-ray3.20A/B/C1-310[»]
2ZPYX-ray2.10A1-310[»]
3X23X-ray2.40A1-310[»]
ProteinModelPortaliP26043.
SMRiP26043.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202845. 7 interactors.
DIPiDIP-29091N.
IntActiP26043. 5 interactors.
MINTiMINT-1862372.
STRINGi10090.ENSMUSP00000000590.

PTM databases

iPTMnetiP26043.
PhosphoSitePlusiP26043.
SwissPalmiP26043.

2D gel databases

REPRODUCTION-2DPAGEP26043.

Proteomic databases

EPDiP26043.
MaxQBiP26043.
PaxDbiP26043.
PeptideAtlasiP26043.
PRIDEiP26043.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000590; ENSMUSP00000000590; ENSMUSG00000032050.
ENSMUST00000163153; ENSMUSP00000128249; ENSMUSG00000032050.
GeneIDi19684.
KEGGimmu:19684.
UCSCiuc009plq.2. mouse.

Organism-specific databases

CTDi5962.
MGIiMGI:97887. Rdx.

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00860000133686.
HOVERGENiHBG002185.
InParanoidiP26043.
KOiK05762.
OMAiLSREDSM.
OrthoDBiEOG091G06UO.
TreeFamiTF313935.

Miscellaneous databases

ChiTaRSiRdx. mouse.
EvolutionaryTraceiP26043.
PROiP26043.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032050.
CleanExiMM_RDX.
ExpressionAtlasiP26043. baseline and differential.
GenevisibleiP26043. MM.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
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_tail.
IPR011993. PH_dom-like.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00769. ERM. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
[Graphical view]
PIRSFiPIRSF002305. ERM. 1 hit.
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01196. FERM_C. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48678. SSF48678. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRADI_MOUSE
AccessioniPrimary (citable) accession number: P26043
Secondary accession number(s): Q3TS85, Q9QW27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.