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Protein

Radixin

Gene

RDX

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

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

GO - Biological processi

Keywordsi

Molecular functionActin capping, Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Radixin
Gene namesi
Name:RDX
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

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, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002546521 – 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

PaxDbiQ32LP2.
PeptideAtlasiQ32LP2.
PRIDEiQ32LP2.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006129.

Structurei

3D structure databases

ProteinModelPortaliQ32LP2.
SMRiQ32LP2.
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.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiQ32LP2.
KOiK05762.

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.
IPR035963. FERM_2.
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.

Sequencei

Sequence statusi: Complete.

Q32LP2-1 [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
LRQIEEQTMK AQKELEEQTR KALELDQERK RAKEEAERLE KERQAAEEAK
410 420 430 440 450
SALAKQAADQ MKNQEQLAAE LAEFTAKIAL LEEAKKKKEE EATEWQHKAF
460 470 480 490 500
AAQEDLEKTK EELKTVMSAP PPPPPPPVIP PTENEHDEHD ENNAEASAEL
510 520 530 540 550
SNDGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD ETKKTQNDVL
560 570 580
HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM
Length:583
Mass (Da):68,568
Last modified:December 6, 2005 - v1
Checksum:i9F8C1C502AC098C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC109485 mRNA. Translation: AAI09486.1.
RefSeqiNP_001069217.1. NM_001075749.1.
UniGeneiBt.35977.

Genome annotation databases

GeneIDi517111.
KEGGibta:517111.

Similar proteinsi

Entry informationi

Entry nameiRADI_BOVIN
AccessioniPrimary (citable) accession number: Q32LP2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 6, 2005
Last modified: October 25, 2017
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome