Reviewed, UniProtKB/Swiss-Prot P35241 (RADI_HUMAN)

Names and origin

Protein names

Recommended name:
    Radixin

Gene names

Name:

RDX

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	583 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.
Subunit structure	Binds SLC9A3R1. Interacts with NHERF1, NHERF2, LAYN, MME/NEP and ICAM2 By similarity.
Subcellular location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Note: Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively.
Domain	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 ablilty to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN By similarity.
Post-translational modification	Phosphorylated by tyrosine-protein kinases By similarity.
Involvement in disease	Defects in RDX are the cause of non-syndromic sensorineural deafness autosomal recessive type 24 (DFNB24) [MIM:611022]. DFNB24 is a form of 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. Ref.6
Sequence similarities	Contains 1 FERM domain.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Disease	Deafness Disease mutation
Ligand	Actin-binding
Molecular function	Actin capping
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	actin filament capping Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from direct assay. Source: HPA
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 583	583	Radixin		PRO_0000219421
Regions
	Domain	5 – 295	291	FERM
	Region	60 – 63	4	Phosphatidylinositol binding By similarity
	Compositional bias	311 – 522	212	Glu-rich
	Compositional bias	470 – 477	8	Poly-Pro
Sites
	Binding site	278	1	Phosphatidylinositol By similarity
Amino acid modifications
	Modified residue	79	1	N6-acetyllysine Ref.5
	Modified residue	258	1	N6-acetyllysine Ref.5
	Modified residue	263	1	N6-acetyllysine Ref.5
	Modified residue	270	1	Phosphotyrosine By similarity
	Modified residue	344	1	N6-acetyllysine Ref.5
Natural variations
	Natural variant	328	1	K → E: dbSNP rs17854427. Ref.2		VAR_036857
	Natural variant	490	1	D → N: dbSNP rs34471100.		VAR_036858
	Natural variant	578	1	D → N in DFNB24. Ref.6		VAR_036859

Sequences

	Sequence		Length	Mass (Da)
	P35241-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 889687E1D675FFE7	FASTA	583	68,564
	10 20 30 40 50 60 MPKPINVRVT TMDAELEFAI QPNTTGKQLF DQVVKTVGLR EVWFFGLQYV DSKGYSTWLK 70 80 90 100 110 120 LNKKVTQQDV KKENPLQFKF RAKFFPEDVS EELIQEITQR LFFLQVKEAI LNDEIYCPPE 130 140 150 160 170 180 TAVLLASYAV QAKYGDYNKE IHKPGYLAND RLLPQRVLEQ HKLTKEQWEE RIQNWHEEHR 190 200 210 220 230 240 GMLREDSMME YLKIAQDLEM YGVNYFEIKN KKGTELWLGV DALGLNIYEH DDKLTPKIGF 250 260 270 280 290 300 PWSEIRNISF NDKKFVIKPI DKKAPDFVFY APRLRINKRI LALCMGNHEL YMRRRKPDTI 310 320 330 340 350 360 EVQQMKAQAR EEKHQKQLER AQLENEKKKR EIAEKEKERI EREKEELMER LKQIEEQTIK 370 380 390 400 410 420 AQKELEEQTR KALELDQERK RAKEEAERLE KERRAAEEAK SAIAKQAADQ MKNQEQLAAE 430 440 450 460 470 480 LAEFTAKIAL LEEAKKKKEE EATEWQHKAF AAQEDLEKTK EELKTVMSAP PPPPPPPVIP 490 500 510 520 530 540 PTENEHDEHD ENNAEASAEL SNEGVMNHRS EEERVTETQK NERVKKQLQA LSSELAQARD 550 560 570 580 ETKKTQNDVL HAENVKAGRD KYKTLRQIRQ GNTKQRIDEF EAM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes." Wilgenbus K.K., Milatovich A., Francke U., Furthmayr H. Genomics 16:199-206(1993) [PubMed: 8486357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLU-328. Tissue: Brain.
[3]	"NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins." Murthy A., Gonzalez-Agosti C., Cordero E., Pinney D., Candia C., Solomon F., Gusella J., Ramesh V. J. Biol. Chem. 273:1273-1276(1998) [PubMed: 9430655] [Abstract] Cited for: INTERACTION WITH SLC9A3R1.
[4]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-258; LYS-263 AND LYS-344, MASS SPECTROMETRY.
[6]	"Mutations of the RDX gene cause nonsyndromic hearing loss at the DFNB24 locus." Khan S.Y., Ahmed Z.M., Shabbir M.I., Kitajiri S., Kalsoom S., Tasneem S., Shayiq S., Ramesh A., Srisailpathy S., Khan S.N., Smith R.J.H., Riazuddin S., Friedman T.B., Riazuddin S. Hum. Mutat. 28:417-423(2007) [PubMed: 17226784] [Abstract] Cited for: VARIANT DFNB24 ASN-578.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L02320 mRNA. Translation: AAA36541.1. BC047109 mRNA. Translation: AAH47109.1.
IPI	IPI00903145.
PIR	A46127.
RefSeq	NP_002897.1.
UniGene	Hs.263671 Hs.592679
3D structure databases
SMR	P35241. Positions 2-310.
ModBase	Search...
Protein-protein interaction databases
STRING	P35241.
PTM databases
PhosphoSite	P35241.
2-D gel databases
Aarhus/Ghent-2DPAGE	2501. IEF.
Proteomic databases
PeptideAtlas	P35241.
PRIDE	P35241.
Genome annotation databases
Ensembl	ENST00000343115; ENSP00000342830; ENSG00000137710; Homo sapiens. [Genome view] ENST00000405097; ENSP00000384136; ENSG00000137710; Homo sapiens. [Genome view]
GeneID	5962.
KEGG	hsa:5962.
UCSC	uc001pku.1. human.
Organism-specific databases
CTD	5962.
GeneCards	GC11M109605.
HGNC	HGNC:9944. RDX.
HPA	HPA000263. HPA000763.
MIM	179410. gene. 611022. phenotype.
Orphanet	90636. Deafness, autosomal recessive, nonsyndromic, sensorineural, type DFNB.
PharmGKB	PA34311.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P35241.
HOVERGEN	P35241.
Gene expression databases
ArrayExpress	P35241.
Bgee	P35241.
CleanEx	HS_RDX.
Genevestigator	P35241.
GermOnline	ENSG00000137710. Homo sapiens.
Family and domain databases
InterPro	IPR019749. Band_41_domain. IPR019750. Band_41_sg. IPR011174. ERM. IPR011259. ERM_C. IPR000798. Ez/rad/moesin. 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. IPR011993. PH_type. [Graphical view]
Gene3D	G3DSA:1.20.80.10. ACBP. 1 hit. G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF00769. ERM. 1 hit. PF09380. FERM_C. 1 hit. PF00373. FERM_M. 1 hit. PF09379. FERM_N. 1 hit. [Graphical view]
PIRSF	PIRSF002305. ERM. 1 hit.
PRINTS	PR00935. BAND41. PR00661. ERMFAMILY.
SMART	SM00295. B41. 1 hit. [Graphical view]
PROSITE	PS00660. FERM_1. 1 hit. PS00661. FERM_2. 1 hit. PS50057. FERM_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	23212.
SOURCE	Search...

Entry information

Entry name

RADI_HUMAN

Accession

Primary (citable) accession number: P35241
Secondary accession number(s): Q86Y61

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 24, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.