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Protein

FYVE, RhoGEF and PH domain-containing protein 4

Gene

Fgd4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 MAPK8.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri559 – 61961FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • actin binding Source: MGI
  • actin filament binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • Rho guanyl-nucleotide exchange factor activity Source: InterPro

GO - Biological processi

  • activation of JUN kinase activity Source: MGI
  • regulation of cell shape Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Actin-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:Fgd4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi708357. Fgd4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 766766FYVE, RhoGEF and PH domain-containing protein 4PRO_0000080949Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei702 – 7021PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO88387.

Expressioni

Tissue specificityi

Detected in brain, lung, liver, skeletal muscle, kidney, testis and cultured hippocampal neurons.1 Publication

Gene expression databases

GenevisibleiO88387. RN.

Interactioni

Subunit structurei

Homooligomer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002491.

Structurei

3D structure databases

ProteinModelPortaliO88387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini206 – 393188DHPROSITE-ProRule annotationAdd
BLAST
Domaini422 – 521100PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini643 – 74098PH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 150150Actin filament-bindingAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri559 – 61961FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5422.
HOGENOMiHOG000220866.
HOVERGENiHBG007506.
InParanoidiO88387.
KOiK05723.
PhylomeDBiO88387.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESNPAPTS CASKGKHSKV SDLISHFEGG SVLSSYTDVQ KDSTMNLNIP
60 70 80 90 100
QTPRQHGLTS TTPQKLPSHK SPQKQEKDSD QNQGQHGCLA NGVAAAQSQM
110 120 130 140 150
ECETEKEAAL SPETDTQTAA ASPDAHVLNG VRNETTTDSA SSVTNSHDEN
160 170 180 190 200
ACDSSCRTQG TDLGLPSKEG EPVIEAELQE RENGLSTEGL NPLDQHHEVK
210 220 230 240 250
ETNEQKLHKI ATELLLTERA YVSRLNLLDQ VFYCKLLEEA NRGSFPAEMV
260 270 280 290 300
NKIFSNISSI NAFHSKFLLP ELEKRMQEWE TTPRIGDILQ KLAPFLKMYG
310 320 330 340 350
EYVKGFDNAV ELVKNMTERV PQFKSVTEEI QKQKICGSLT LQHHMLEPIQ
360 370 380 390 400
RIPRYEMLLK DYLKKLSPDA PDWNDAKKSL EIISTAASHS NSAIRKMENL
410 420 430 440 450
KKLLEIYEML GEEEDIVNPS NELIKEGQIL KLAARNTSAQ ERYLFLFNNM
460 470 480 490 500
LLYCVPRFSL VGSKFTVRTR VGIDGMKIVE THNEEYPHTF QVSGKERTLE
510 520 530 540 550
LQASSEQDKE EWIKALQESI DAFHQRHETF RNAIAKENDI PLEVSTAELG
560 570 580 590 600
KRAPRWIRDN EVTMCMKCKE SFNALTRRRH HCRACGHVVC WKCSDYKAQL
610 620 630 640 650
EYDGGRLNKV CKDCYQIMSG FAESEEKKRR GILEIESAEV SGNSEVCSFL
660 670 680 690 700
QYMEKSKPWQ KIWCVIPKQD PLVLYMYGAP QDVRAQATIP LLGYIVDDMP
710 720 730 740 750
KSADLPHSFK LTQSKSVHSF AADSEELKQK WLKIILLAVT GETPDGPSEH
760
LDTLDNLPGP KEKSEC
Length:766
Mass (Da):86,454
Last modified:November 1, 1998 - v1
Checksum:iE34831DC0B0B334C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038388 mRNA. Translation: AAC27698.1.
RefSeqiNP_640356.1. NM_139263.1.
UniGeneiRn.29988.

Genome annotation databases

GeneIDi246174.
KEGGirno:246174.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038388 mRNA. Translation: AAC27698.1.
RefSeqiNP_640356.1. NM_139263.1.
UniGeneiRn.29988.

3D structure databases

ProteinModelPortaliO88387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002491.

Proteomic databases

PRIDEiO88387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi246174.
KEGGirno:246174.

Organism-specific databases

CTDi121512.
RGDi708357. Fgd4.

Phylogenomic databases

eggNOGiCOG5422.
HOGENOMiHOG000220866.
HOVERGENiHBG007506.
InParanoidiO88387.
KOiK05723.
PhylomeDBiO88387.

Miscellaneous databases

NextBioi623462.
PROiO88387.

Gene expression databases

GenevisibleiO88387. RN.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000219. DH-domain.
IPR011993. PH-like_dom.
IPR001849. PH_domain.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiFGD4_RAT
AccessioniPrimary (citable) accession number: O88387
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1998
Last modified: July 22, 2015
This is version 100 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.