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Protein

Radixin

Gene

Rdx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 Source: MGI
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionActin capping, Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-437239 Recycling pathway of L1

Names & Taxonomyi

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

Organism-specific databases

MGIiMGI:97887 Rdx

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, 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 residuei60N6-acetyllysineBy similarity1
Modified residuei79N6-acetyllysineBy similarity1
Modified residuei83N6-succinyllysineCombined sources1
Modified residuei116PhosphotyrosineBy similarity1
Modified residuei117S-nitrosocysteineBy similarity1
Modified residuei139N6-acetyllysineBy similarity1
Modified residuei146PhosphotyrosineBy similarity1
Modified residuei165N6-acetyllysineBy similarity1
Modified residuei532PhosphoserineBy similarity1
Modified residuei533PhosphoserineBy similarity1
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

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP26043
MaxQBiP26043
PaxDbiP26043
PeptideAtlasiP26043
PRIDEiP26043

2D gel databases

REPRODUCTION-2DPAGEiP26043

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, PubMed:9472040). Interacts with SPN and CD44 (PubMed:9472040).By similarity6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: MGI
  • ATPase binding Source: MGI
  • cadherin binding Source: MGI
  • protein domain specific binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi202845, 9 interactors
DIPiDIP-29091N
IntActiP26043, 12 interactors
MINTiP26043
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.

Phylogenomic databases

eggNOGiKOG3529 Eukaryota
ENOG410XQFP LUCA
GeneTreeiENSGT00890000139341
HOVERGENiHBG002185
InParanoidiP26043
KOiK05762
OMAiTMKAQKE
OrthoDBiEOG091G06UO
TreeFamiTF313935

Family and domain databases

CDDicd14473 FERM_B-lobe, 1 hit
Gene3Di1.20.80.10, 1 hit
1.25.40.1020, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR019749 Band_41_domain
IPR011174 ERM
IPR011259 ERM_C_dom
IPR000798 Ez/rad/moesin-like
IPR014352 FERM/acyl-CoA-bd_prot_sf
IPR035963 FERM_2
IPR019748 FERM_central
IPR019747 FERM_CS
IPR000299 FERM_domain
IPR018979 FERM_N
IPR018980 FERM_PH-like_C
IPR008954 Moesin_tail_sf
IPR011993 PH-like_dom_sf
IPR029071 Ubiquitin-like_domsf
PfamiView protein in Pfam
PF00769 ERM, 1 hit
PF09380 FERM_C, 1 hit
PF00373 FERM_M, 1 hit
PF09379 FERM_N, 1 hit
PIRSFiPIRSF002305 ERM, 1 hit
PRINTSiPR00935 BAND41
PR00661 ERMFAMILY
SMARTiView protein in SMART
SM00295 B41, 1 hit
SM01196 FERM_C, 1 hit
SUPFAMiSSF47031 SSF47031, 1 hit
SSF48678 SSF48678, 1 hit
SSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS00660 FERM_1, 1 hit
PS00661 FERM_2, 1 hit
PS50057 FERM_3, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiRADI_MOUSE
AccessioniPrimary (citable) accession number: P26043
Secondary accession number(s): Q3TS85, Q9QW27
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: March 28, 2018
This is version 163 of the entry and version 3 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health