FYVE, RhoGEF and PH domain-containing protein 4

Contribute

Send feedback

Read comments (?) or add your own

O88387 (FGD4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
FYVE, RhoGEF and PH domain-containing protein 4

Alternative name(s):
Actin filament-binding protein frabin
FGD1-related F-actin-binding protein

Gene names

Name:

Fgd4

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	766 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Plays a role in regulating the actin cytoskeleton and cell shape. Activates MAPK8. Ref.1 Ref.2
Subunit structure	Homooligomer. Ref.1
Subcellular location	Cytoplasm › cytoskeleton. Cell projection › filopodium. Note: Concentrated in filopodia and poorly detected at lamellipodia. Binds along the sides of actin fibers. Ref.2
Tissue specificity	Detected in brain, lung, liver, skeletal muscle, kidney, testis and cultured hippocampal neurons. Ref.2
Domain	The part of the protein spanning the actin filament-binding domain together with the DH domain and the first PH domain is necessary and sufficient for microspike formation. Activation of MAPK8 requires the presence of all domains with the exception of the actin filament-binding domain. Ref.2
Sequence similarities	Contains 1 DH (DBL-homology) domain. Contains 1 FYVE-type zinc finger. Contains 2 PH domains.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton
Domain	Repeat Zinc-finger
Ligand	Actin-binding Metal-binding Zinc
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	activation of JUN kinase activity Inferred from direct assay Ref.1. Source: MGI regulation of Rho protein signal transduction Inferred from electronic annotation. Source: InterPro regulation of cell shape Inferred from mutant phenotype Ref.1. Source: RGD
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell filopodium Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	Rho guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: InterPro actin filament binding Inferred from mutant phenotype Ref.1. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 766

766

FYVE, RhoGEF and PH domain-containing protein 4

PRO_0000080949

Regions

Domain

206 – 393

188

Domain

422 – 521

100

PH 1

Domain

643 – 740

PH 2

Zinc finger

559 – 619

FYVE-type

Region

1 – 150

150

Actin filament-binding

Amino acid modifications

Modified residue

702

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O88387 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: E34831DC0B0B334C
Show »

FASTA

766

86,454

        10         20         30         40         50         60 
MEESNPAPTS CASKGKHSKV SDLISHFEGG SVLSSYTDVQ KDSTMNLNIP QTPRQHGLTS 

        70         80         90        100        110        120 
TTPQKLPSHK SPQKQEKDSD QNQGQHGCLA NGVAAAQSQM ECETEKEAAL SPETDTQTAA 

       130        140        150        160        170        180 
ASPDAHVLNG VRNETTTDSA SSVTNSHDEN ACDSSCRTQG TDLGLPSKEG EPVIEAELQE 

       190        200        210        220        230        240 
RENGLSTEGL NPLDQHHEVK ETNEQKLHKI ATELLLTERA YVSRLNLLDQ VFYCKLLEEA 

       250        260        270        280        290        300 
NRGSFPAEMV NKIFSNISSI NAFHSKFLLP ELEKRMQEWE TTPRIGDILQ KLAPFLKMYG 

       310        320        330        340        350        360 
EYVKGFDNAV ELVKNMTERV PQFKSVTEEI QKQKICGSLT LQHHMLEPIQ RIPRYEMLLK 

       370        380        390        400        410        420 
DYLKKLSPDA PDWNDAKKSL EIISTAASHS NSAIRKMENL KKLLEIYEML GEEEDIVNPS 

       430        440        450        460        470        480 
NELIKEGQIL KLAARNTSAQ ERYLFLFNNM LLYCVPRFSL VGSKFTVRTR VGIDGMKIVE 

       490        500        510        520        530        540 
THNEEYPHTF QVSGKERTLE LQASSEQDKE EWIKALQESI DAFHQRHETF RNAIAKENDI 

       550        560        570        580        590        600 
PLEVSTAELG KRAPRWIRDN EVTMCMKCKE SFNALTRRRH HCRACGHVVC WKCSDYKAQL 

       610        620        630        640        650        660 
EYDGGRLNKV CKDCYQIMSG FAESEEKKRR GILEIESAEV SGNSEVCSFL QYMEKSKPWQ 

       670        680        690        700        710        720 
KIWCVIPKQD PLVLYMYGAP QDVRAQATIP LLGYIVDDMP KSADLPHSFK LTQSKSVHSF 

       730        740        750        760 
AADSEELKQK WLKIILLAVT GETPDGPSEH LDTLDNLPGP KEKSEC

« Hide

References

[1]

"Frabin, a novel FGD1-related actin filament-binding protein capable of changing cell shape and activating c-Jun N-terminal kinase."
Obaishi H., Nakanishi H., Mandai K., Satoh K., Satoh A., Takahashi K., Miyahara M., Nishioka H., Takaishi K., Takai Y.
J. Biol. Chem. 273:18697-18700(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 41-65; 236-252; 276-291; 365-396; 464-475; 478-493; 496-503; 510-551; 702-710 AND 716-428, HOMOOLIGOMERIZATION, FUNCTION.
Tissue: Brain.

[2]

"Association of frabin with the actin cytoskeleton is essential for microspike formation through activation of Cdc42 small G protein."
Umikawa M., Obaishi H., Nakanishi H., Satoh-Horikawa K., Takahashi K., Hotta I., Matsuura Y., Takai Y.
J. Biol. Chem. 274:25197-25200(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACTIN FIBER-BINDING DOMAIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF038388 mRNA. Translation: AAC27698.1.
IPI	IPI00208765.
RefSeq	NP_640356.1. NM_139263.1.
UniGene	Rn.29988.
3D structure databases
ProteinModelPortal	O88387.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000002491.
Proteomic databases
PRIDE	O88387.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	246174.
KEGG	rno:246174.
Organism-specific databases
CTD	121512.
RGD	708357. Fgd4.
Phylogenomic databases
eggNOG	COG5422.
HOGENOM	HOG000220866.
HOVERGEN	HBG007506.
InParanoid	O88387.
KO	K05723.
OrthoDB	EOG418BMQ.
Gene expression databases
ArrayExpress	O88387.
Genevestigator	O88387.
GermOnline	ENSRNOG00000001818. Rattus norvegicus.
Family and domain databases
Gene3D	1.20.900.10. 1 hit. 2.30.29.30. 2 hits. 3.30.40.10. 1 hit.
InterPro	IPR000219. DH-domain. IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. IPR000306. Znf_FYVE. IPR017455. Znf_FYVE-rel. IPR011011. Znf_FYVE_PHD. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF01363. FYVE. 1 hit. PF00169. PH. 2 hits. PF00621. RhoGEF. 1 hit. [Graphical view]
SMART	SM00064. FYVE. 1 hit. SM00233. PH. 2 hits. SM00325. RhoGEF. 1 hit. [Graphical view]
SUPFAM	SSF48065. DH-domain. 1 hit. SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS50010. DH_2. 1 hit. PS50003. PH_DOMAIN. 2 hits. PS50178. ZF_FYVE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	623462.

Entry information

Entry name

FGD4_RAT

Accession

Primary (citable) accession number: O88387

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents