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Protein

Radixin

Gene

RDX

Organism
Homo sapiens (Human)
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 sitei278PhosphatidylinositolBy similarity1

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL
  • protein domain specific binding Source: Ensembl
  • protein homodimerization activity Source: UniProtKB
  • protein kinase A binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

  • apical protein localization Source: Ensembl
  • barbed-end actin filament capping Source: Ensembl
  • cellular response to platelet-derived growth factor stimulus Source: Ensembl
  • cellular response to thyroid hormone stimulus Source: UniProtKB
  • establishment of endothelial barrier Source: UniProtKB
  • establishment of protein localization Source: UniProtKB
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • microvillus assembly Source: Ensembl
  • negative regulation of adherens junction organization Source: UniProtKB
  • negative regulation of cell size Source: UniProtKB
  • negative regulation of GTPase activity Source: UniProtKB
  • negative regulation of homotypic cell-cell adhesion Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cellular protein catabolic process Source: UniProtKB
  • positive regulation of early endosome to late endosome transport Source: UniProtKB
  • positive regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of protein localization to early endosome Source: UniProtKB
  • protein kinase A signaling Source: UniProtKB
  • regulation of actin filament bundle assembly Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of cell size Source: UniProtKB
  • regulation of GTPase activity Source: UniProtKB
  • regulation of organelle assembly Source: UniProtKB
  • regulation of Rap protein signal transduction Source: UniProtKB
  • regulation of ruffle assembly Source: UniProtKB

Keywordsi

Molecular functionActin capping, Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-437239. Recycling pathway of L1.
SIGNORiP35241.

Names & Taxonomyi

Protein namesi
Recommended name:
Radixin
Gene namesi
Name:RDX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9944. RDX.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • cell-cell adherens junction Source: Ensembl
  • cell periphery Source: UniProtKB
  • cell tip Source: Ensembl
  • cleavage furrow Source: UniProtKB-SubCell
  • cortical actin cytoskeleton Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • filopodium Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • microvillus Source: UniProtKB
  • midbody Source: Ensembl
  • myelin sheath Source: Ensembl
  • plasma membrane Source: HPA
  • ruffle Source: Ensembl
  • stereocilium Source: Ensembl
  • T-tubule Source: Ensembl

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Deafness, autosomal recessive, 24 (DFNB24)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
See also OMIM:611022
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036859578D → N in DFNB24. 1 PublicationCorresponds to variant dbSNP:rs121918379Ensembl.1

Keywords - Diseasei

Deafness, Disease mutation, Non-syndromic deafness

Organism-specific databases

DisGeNETi5962.
GeneReviewsiRDX.
MalaCardsiRDX.
MIMi611022. phenotype.
OpenTargetsiENSG00000137710.
Orphaneti90636. Autosomal recessive non-syndromic sensorineural deafness type DFNB.
PharmGKBiPA34311.

Polymorphism and mutation databases

BioMutaiRDX.
DMDMi464541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194211 – 583RadixinAdd BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei60N6-acetyllysineBy similarity1
Modified residuei79N6-acetyllysineBy similarity1
Modified residuei83N6-succinyllysineBy similarity1
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 ROCK2By similarity1

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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP35241.
MaxQBiP35241.
PaxDbiP35241.
PeptideAtlasiP35241.
PRIDEiP35241.

PTM databases

iPTMnetiP35241.
PhosphoSitePlusiP35241.
SwissPalmiP35241.

Expressioni

Gene expression databases

BgeeiENSG00000137710.
CleanExiHS_RDX.
ExpressionAtlasiP35241. baseline and differential.
GenevisibleiP35241. HS.

Organism-specific databases

HPAiCAB037312.
HPA000263.
HPA000763.

Interactioni

Subunit structurei

Binds SLC9A3R1 (PubMed:9430655). Interacts with NHERF1, NHERF2, LAYN, MME/NEP and ICAM2 (By similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB2P051072EBI-2514878,EBI-300173

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • cadherin binding Source: BHF-UCL
  • protein domain specific binding Source: Ensembl
  • protein homodimerization activity Source: UniProtKB
  • protein kinase A binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111894. 75 interactors.
IntActiP35241. 11 interactors.
MINTiMINT-1536950.
STRINGi9606.ENSP00000342830.

Structurei

3D structure databases

ProteinModelPortaliP35241.
SMRiP35241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni60 – 63Phosphatidylinositol bindingBy similarity4

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 (By similarity).By similarity

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
GeneTreeiENSGT00890000139341.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiP35241.
KOiK05762.
OMAiTMKAQKE.
OrthoDBiEOG091G06UO.
PhylomeDBiP35241.
TreeFamiTF313935.

Family and domain databases

CDDicd14473. FERM_B-lobe. 1 hit.
Gene3Di1.20.80.10. 2 hits.
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_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.
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.
SSF50729. SSF50729. 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.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35241-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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
LKQIEEQTIK AQKELEEQTR KALELDQERK RAKEEAERLE KERRAAEEAK
410 420 430 440 450
SAIAKQAADQ MKNQEQLAAE LAEFTAKIAL LEEAKKKKEE EATEWQHKAF
460 470 480 490 500
AAQEDLEKTK EELKTVMSAP PPPPPPPVIP PTENEHDEHD ENNAEASAEL
510 520 530 540 550
SNEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD ETKKTQNDVL
560 570 580
HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM
Length:583
Mass (Da):68,564
Last modified:February 1, 1994 - v1
Checksum:i889687E1D675FFE7
GO
Isoform 2 (identifier: P35241-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-347: Missing.
     583-583: M → MWGPKLYALFQMRSCQSSIKQM

Show »
Length:257
Mass (Da):29,668
Checksum:iF763D99B9343B54A
GO
Isoform 3 (identifier: P35241-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     33-64: Missing.
     168-539: Missing.
     583-583: M → MWGPKLYALFQMRSCQSSIKQM

Show »
Length:200
Mass (Da):23,413
Checksum:i59D476B3466D4CD6
GO
Isoform 4 (identifier: P35241-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-156: MPKPINVRVT...LANDRLLPQR → MLSWNLPFSPIQLANNFLTS

Show »
Length:447
Mass (Da):52,679
Checksum:i6DD0EEED1757180C
GO
Isoform 5 (identifier: P35241-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     583-583: M → MWGPKLYALFQMRSCQSSIKQM

Show »
Length:604
Mass (Da):71,049
Checksum:i62FD7960876C937F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti435K → R in BAH14432 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_036857328K → E1 PublicationCorresponds to variant dbSNP:rs17854427Ensembl.1
Natural variantiVAR_036858490D → N. Corresponds to variant dbSNP:rs34471100Ensembl.1
Natural variantiVAR_036859578D → N in DFNB24. 1 PublicationCorresponds to variant dbSNP:rs121918379Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0453151 – 347Missing in isoform 2. 1 PublicationAdd BLAST347
Alternative sequenceiVSP_0472761 – 156MPKPI…LLPQR → MLSWNLPFSPIQLANNFLTS in isoform 4. 1 PublicationAdd BLAST156
Alternative sequenceiVSP_04531633 – 64Missing in isoform 3. 1 PublicationAdd BLAST32
Alternative sequenceiVSP_045317168 – 539Missing in isoform 3. 1 PublicationAdd BLAST372
Alternative sequenceiVSP_045318583M → MWGPKLYALFQMRSCQSSIK QM in isoform 2, isoform 3 and isoform 5. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02320 mRNA. Translation: AAA36541.1.
AK316061 mRNA. Translation: BAH14432.1.
DQ916738 mRNA. Translation: ABI34710.1.
DQ916739 mRNA. Translation: ABI34711.1.
DQ916741 mRNA. Translation: ABI34713.1.
DQ916742 mRNA. Translation: ABI34714.1.
DQ916740 mRNA. Translation: ABI34712.1.
AP000901 Genomic DNA. No translation available.
AP002788 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67129.1.
BC047109 mRNA. Translation: AAH47109.1.
CCDSiCCDS58171.1. [P35241-2]
CCDS58172.1. [P35241-4]
CCDS58173.1. [P35241-3]
CCDS58174.1. [P35241-5]
CCDS8343.1. [P35241-1]
PIRiA46127.
RefSeqiNP_001247421.1. NM_001260492.1. [P35241-5]
NP_001247422.1. NM_001260493.1. [P35241-5]
NP_001247423.1. NM_001260494.1. [P35241-4]
NP_001247424.1. NM_001260495.1. [P35241-2]
NP_001247425.1. NM_001260496.1. [P35241-3]
NP_002897.1. NM_002906.3. [P35241-1]
UniGeneiHs.263671.
Hs.584560.
Hs.741211.

Genome annotation databases

EnsembliENST00000343115; ENSP00000342830; ENSG00000137710. [P35241-1]
ENST00000405097; ENSP00000384136; ENSG00000137710. [P35241-5]
ENST00000528498; ENSP00000432112; ENSG00000137710. [P35241-5]
ENST00000528900; ENSP00000433580; ENSG00000137710. [P35241-2]
ENST00000530301; ENSP00000436277; ENSG00000137710. [P35241-3]
ENST00000530749; ENSP00000437301; ENSG00000137710. [P35241-5]
ENST00000544551; ENSP00000445826; ENSG00000137710. [P35241-4]
GeneIDi5962.
KEGGihsa:5962.
UCSCiuc001pku.4. human. [P35241-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiRADI_HUMAN
AccessioniPrimary (citable) accession number: P35241
Secondary accession number(s): A7YIJ8
, A7YIK0, A7YIK3, B7Z9U6, F5H1A7, Q86Y61
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: August 30, 2017
This is version 168 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot