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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei278 – 2781PhosphatidylinositolBy similarity

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 583583RadixinPRO_0000254652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei83 – 831N6-succinyllysineBy similarity
Modified residuei564 – 5641Phosphothreonine; by ROCK2By similarity

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

Phosphoprotein

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006129.

Structurei

3D structure databases

ProteinModelPortaliQ32LP2.
SMRiQ32LP2. Positions 1-374, 494-583.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 295291FERMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 634Phosphatidylinositol bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi311 – 522212Glu-richAdd
BLAST
Compositional biasi470 – 4778Poly-Pro

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

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiQ32LP2.
KOiK05762.

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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ32LP2.
SMRiQ32LP2. Positions 1-374, 494-583.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006129.

Proteomic databases

PaxDbiQ32LP2.
PeptideAtlasiQ32LP2.
PRIDEiQ32LP2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi517111.
KEGGibta:517111.

Organism-specific databases

CTDi5962.

Phylogenomic databases

eggNOGiKOG3529. Eukaryota.
ENOG410XQFP. LUCA.
HOGENOMiHOG000007113.
HOVERGENiHBG002185.
InParanoidiQ32LP2.
KOiK05762.

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_BOVIN
AccessioniPrimary (citable) accession number: Q32LP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: December 6, 2005
Last modified: July 6, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.