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O88387

- FGD4_RAT

UniProt

O88387 - FGD4_RAT

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Protein

FYVE, RhoGEF and PH domain-containing protein 4

Gene

Fgd4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

  1. actin binding Source: MGI
  2. actin filament binding Source: RGD
  3. metal ion binding Source: UniProtKB-KW
  4. Rho guanyl-nucleotide exchange factor activity Source: InterPro

GO - Biological processi

  1. activation of JUN kinase activity Source: MGI
  2. 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: Unplaced

Organism-specific databases

RGDi708357. Fgd4.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cell projectionfilopodium 1 Publication
Note: Concentrated in filopodia and poorly detected at lamellipodia. Binds along the sides of actin fibers.

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
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

Proteomic databases

PRIDEiO88387.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriO88387.

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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF038388 mRNA. Translation: AAC27698.1 .
RefSeqi NP_640356.1. NM_139263.1.
UniGenei Rn.29988.

3D structure databases

ProteinModelPortali O88387.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000002491.

Proteomic databases

PRIDEi O88387.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 246174.
KEGGi rno:246174.

Organism-specific databases

CTDi 121512.
RGDi 708357. Fgd4.

Phylogenomic databases

eggNOGi COG5422.
HOGENOMi HOG000220866.
HOVERGENi HBG007506.
InParanoidi O88387.
KOi K05723.
PhylomeDBi O88387.

Miscellaneous databases

NextBioi 623462.
PROi O88387.

Gene expression databases

Genevestigatori O88387.

Family and domain databases

Gene3Di 1.20.900.10. 1 hit.
2.30.29.30. 2 hits.
3.30.40.10. 1 hit.
InterProi IPR000219. DH-domain.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF01363. FYVE. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view ]
SMARTi SM00064. FYVE. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view ]
SUPFAMi SSF48065. SSF48065. 1 hit.
PROSITEi PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50178. ZF_FYVE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 96 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