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Protein

FERM, RhoGEF and pleckstrin domain-containing protein 2

Gene

Farp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as guanine nucleotide exchange factor that activates RAC1. May have relatively low activity (PubMed:23375260 and PubMed:20702777). Plays a role in the response to class 3 semaphorins and remodeling of the actin cytoskeleton. Plays a role in TNFSF11-mediated osteoclast differentiation, especially in podosome rearrangement and reorganization of the actin cytoskeleton. Regulates the activation of ITGB3, integrin signaling and cell adhesion.4 Publications

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • cell adhesion Source: UniProtKB
  • neuron remodeling Source: MGI
  • osteoclast differentiation Source: UniProtKB
  • podosome assembly Source: UniProtKB
  • Rac protein signal transduction Source: MGI
  • regulation of integrin activation Source: UniProtKB
  • regulation of Rho protein signal transduction Source: InterPro
  • semaphorin-plexin signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Enzyme and pathway databases

ReactomeiR-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

Names & Taxonomyi

Protein namesi
Recommended name:
FERM, RhoGEF and pleckstrin domain-containing protein 2
Alternative name(s):
FERM domain including RhoGEF
Short name:
FIR
Gene namesi
Name:Farp2
Synonyms:Kiaa0793
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2385126. Farp2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi730L → R: Increases guanyl-nucleotide exchange factor activity with RAC1; when associated with Q-733. 1 Publication1
Mutagenesisi733L → Q: Increases guanyl-nucleotide exchange factor activity with RAC1; when associated with R-730. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002327561 – 1065FERM, RhoGEF and pleckstrin domain-containing protein 2Add BLAST1065

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei389PhosphoserineBy similarity1
Modified residuei440PhosphoserineBy similarity1
Modified residuei863PhosphoserineCombined sources1
Modified residuei880PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ91VS8.
PaxDbiQ91VS8.
PeptideAtlasiQ91VS8.
PRIDEiQ91VS8.

PTM databases

iPTMnetiQ91VS8.
PhosphoSitePlusiQ91VS8.

Expressioni

Tissue specificityi

Detected in adult brain, lung and testis. Detected in embryonic hippocampus and brain cortex.1 Publication

Inductioni

Up-regulated by TNFSF11.1 Publication

Gene expression databases

BgeeiENSMUSG00000034066.
CleanExiMM_FARP2.
ExpressionAtlasiQ91VS8. baseline and differential.
GenevisibleiQ91VS8. MM.

Interactioni

Subunit structurei

Interacts with PLXNA1. Interaction with PLXNA1 or PIP5K1C lowers its guanine nucleotide exchange activity. Dissociates from PLXNA1 when SEMA3A binds to the receptor. Interacts with PIP5K1C via its FERM domain. The interaction with PIP5K1C is enhanced by SEMA3A binding. Interacts with RAC1.3 Publications

Protein-protein interaction databases

IntActiQ91VS8. 2 interactors.
MINTiMINT-8178498.
STRINGi10090.ENSMUSP00000043545.

Structurei

Secondary structure

11065
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi538 – 561Combined sources24
Helixi563 – 570Combined sources8
Helixi576 – 583Combined sources8
Turni584 – 586Combined sources3
Helixi587 – 608Combined sources22
Helixi613 – 619Combined sources7
Helixi623 – 633Combined sources11
Helixi634 – 636Combined sources3
Helixi637 – 641Combined sources5
Helixi643 – 655Combined sources13
Helixi658 – 668Combined sources11
Helixi677 – 680Combined sources4
Helixi683 – 701Combined sources19
Helixi709 – 725Combined sources17
Helixi727 – 743Combined sources17
Beta strandi746 – 748Combined sources3
Beta strandi759 – 768Combined sources10
Beta strandi773 – 781Combined sources9
Beta strandi784 – 788Combined sources5
Beta strandi799 – 806Combined sources8
Beta strandi810 – 813Combined sources4
Turni817 – 822Combined sources6
Beta strandi823 – 827Combined sources5
Beta strandi832 – 836Combined sources5
Helixi840 – 856Combined sources17
Helixi909 – 914Combined sources6
Turni915 – 917Combined sources3
Beta strandi919 – 921Combined sources3
Helixi922 – 928Combined sources7
Beta strandi933 – 939Combined sources7
Beta strandi948 – 955Combined sources8
Beta strandi958 – 964Combined sources7
Beta strandi971 – 975Combined sources5
Beta strandi980 – 982Combined sources3
Beta strandi994 – 1000Combined sources7
Beta strandi1003 – 1008Combined sources6
Beta strandi1010 – 1012Combined sources3
Helixi1013 – 1023Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GYVX-ray2.90A/B/C/D/E/F/G/H/I536-749[»]
4GZUX-ray3.20A/B536-1032[»]
ProteinModelPortaliQ91VS8.
SMRiQ91VS8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini44 – 324FERMPROSITE-ProRule annotationAdd BLAST281
Domaini538 – 729DHPROSITE-ProRule annotationAdd BLAST192
Domaini758 – 855PH 1PROSITE-ProRule annotationAdd BLAST98
Domaini930 – 1027PH 2PROSITE-ProRule annotationAdd BLAST98

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi397 – 491Pro/Ser-richAdd BLAST95

Domaini

Intramolecular interaction between the DH domain and the PH domains can stabilize the protein in an autoinhibited conformation.1 Publication

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 FERM domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3531. Eukaryota.
ENOG410XP7Q. LUCA.
GeneTreeiENSGT00860000133686.
HOGENOMiHOG000007957.
HOVERGENiHBG081521.
InParanoidiQ91VS8.
KOiK06082.
OMAiMHVCWYR.
OrthoDBiEOG091G015W.
TreeFamiTF351276.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 3 hits.
InterProiIPR019749. Band_41_domain.
IPR000219. DH-domain.
IPR000798. Ez/rad/moesin-like.
IPR014847. FERM-adjacent.
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.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF08736. FA. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view]
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01195. FA. 1 hit.
SM01196. FERM_C. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 3 hits.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS00660. FERM_1. 1 hit.
PS50057. FERM_3. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91VS8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEIEGTYRA LPTSGTRLGG QTAIGVSTLE PEQSLSPRMQ EKHMRIRVKL
60 70 80 90 100
LDSTVELFDI EPKCDGQVLL TQVWKHLNLI ECDYFGLEFK NVQSYWIWLE
110 120 130 140 150
PMKPIIRQVR KPKNAVLRLA VKFFPPDPGQ LQEEYTRYLF ALQLKRDLLE
160 170 180 190 200
ERLTCTANTA ALLISHLLQS EIGDYDETLD REHLKANEYL PNQEKSLEKI
210 220 230 240 250
LDFHQRHTGQ TPAESDFQVL EIARKLEMYG IRFHMASDRE GTKINLAVSH
260 270 280 290 300
MGVLVFQGTT KINTFNWSKV RKLSFKRKRF LIKLHPEVHG PYQDTLEFLL
310 320 330 340 350
GSRDECKNFW KICVEYHTFF RLSDQPKPKA KAVFFSRGSS FRYSGRTQKQ
360 370 380 390 400
LVDYVKDGGM KRIPYERRHS KTRTSLHALT VDLPKQSVSF TDGLRTSASL
410 420 430 440 450
SSANVSFYPP PSSSLSPPGL PNLKDSSSSL VDPQAPVIKS TAAERSSGPS
460 470 480 490 500
SSDGPSTQSA HLPGPPVLRP GPGFSMDSPQ PSPSSLKSHL SLCPELQAAL
510 520 530 540 550
STAEQGASPV LSPVLSGAGT ARMDNQEEQK HKHMPEDEAY FIAKEILATE
560 570 580 590 600
RTYLKDLEVI TVWFRSVLIK EEAMPAALMA LLFSNIDPVY EFHRGFLHEV
610 620 630 640 650
EQRLALWEGP SSAHLKGDHQ RIGDILLRNM RQLKEFTSYF QRHDEVLTEL
660 670 680 690 700
EKATKHCKKL EAVYKEFELQ KVCYLPLNTF LLKPVQRLVH YRLLLSRLCA
710 720 730 740 750
HYSPGHRDYA DCHEALKAIT EVTTELQQSL TRLENLQKLT ELQRDLVGVE
760 770 780 790 800
NLIAPGREFI REGCLHKLTK KGLQQRMFFL FSDMLLYTSK SVTGASHFRI
810 820 830 840 850
RGFLPLRGML VEESENEWSV PHCFTIYAAQ KTIVVAASTR LEKEKWMQDL
860 870 880 890 900
NAAIQAAKTI GDSPPVLLGG PVYTRTPRSS DEVSLEESED GRGNRGSLEG
910 920 930 940 950
NSQHRANTTM HVCWYRNTSV SRADHSAAVE NQLSGYLLRK FKNSNGWQKL
960 970 980 990 1000
WVVFTNFCLF FYKTHQDDYP LASLPLLGYS VSLPREADSI HKDYVFKLQF
1010 1020 1030 1040 1050
KSHVYFFRAE SKYTFERWMD VIKRASSSPG RPPSFTQDCS HHSPGLEAEI
1060
REKEACPSPC LDKNL
Length:1,065
Mass (Da):121,281
Last modified:July 27, 2011 - v2
Checksum:i452F3BB652BE99D9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti234H → R in BAE42626 (PubMed:16141072).Curated1
Sequence conflicti821P → L in BAE42626 (PubMed:16141072).Curated1
Sequence conflicti821P → L in AAH09153 (PubMed:15489334).Curated1
Sequence conflicti1019M → I in BAD32306 (PubMed:15368895).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK171713 mRNA. Translation: BAE42626.1.
AC108412 Genomic DNA. No translation available.
AC131316 Genomic DNA. No translation available.
BC009153 mRNA. Translation: AAH09153.1.
AK173028 mRNA. Translation: BAD32306.1.
CCDSiCCDS15191.1.
RefSeqiNP_663494.2. NM_145519.2.
UniGeneiMm.243091.

Genome annotation databases

EnsembliENSMUST00000120301; ENSMUSP00000112725; ENSMUSG00000034066.
GeneIDi227377.
KEGGimmu:227377.
UCSCiuc007cec.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK171713 mRNA. Translation: BAE42626.1.
AC108412 Genomic DNA. No translation available.
AC131316 Genomic DNA. No translation available.
BC009153 mRNA. Translation: AAH09153.1.
AK173028 mRNA. Translation: BAD32306.1.
CCDSiCCDS15191.1.
RefSeqiNP_663494.2. NM_145519.2.
UniGeneiMm.243091.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4GYVX-ray2.90A/B/C/D/E/F/G/H/I536-749[»]
4GZUX-ray3.20A/B536-1032[»]
ProteinModelPortaliQ91VS8.
SMRiQ91VS8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91VS8. 2 interactors.
MINTiMINT-8178498.
STRINGi10090.ENSMUSP00000043545.

PTM databases

iPTMnetiQ91VS8.
PhosphoSitePlusiQ91VS8.

Proteomic databases

MaxQBiQ91VS8.
PaxDbiQ91VS8.
PeptideAtlasiQ91VS8.
PRIDEiQ91VS8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000120301; ENSMUSP00000112725; ENSMUSG00000034066.
GeneIDi227377.
KEGGimmu:227377.
UCSCiuc007cec.2. mouse.

Organism-specific databases

CTDi9855.
MGIiMGI:2385126. Farp2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG3531. Eukaryota.
ENOG410XP7Q. LUCA.
GeneTreeiENSGT00860000133686.
HOGENOMiHOG000007957.
HOVERGENiHBG081521.
InParanoidiQ91VS8.
KOiK06082.
OMAiMHVCWYR.
OrthoDBiEOG091G015W.
TreeFamiTF351276.

Enzyme and pathway databases

ReactomeiR-MMU-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.

Miscellaneous databases

PROiQ91VS8.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000034066.
CleanExiMM_FARP2.
ExpressionAtlasiQ91VS8. baseline and differential.
GenevisibleiQ91VS8. MM.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 3 hits.
InterProiIPR019749. Band_41_domain.
IPR000219. DH-domain.
IPR000798. Ez/rad/moesin-like.
IPR014847. FERM-adjacent.
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.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF08736. FA. 1 hit.
PF09380. FERM_C. 1 hit.
PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF00169. PH. 2 hits.
PF00621. RhoGEF. 1 hit.
[Graphical view]
PRINTSiPR00935. BAND41.
PR00661. ERMFAMILY.
SMARTiSM00295. B41. 1 hit.
SM01195. FA. 1 hit.
SM01196. FERM_C. 1 hit.
SM00233. PH. 2 hits.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 3 hits.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50010. DH_2. 1 hit.
PS00660. FERM_1. 1 hit.
PS50057. FERM_3. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFARP2_MOUSE
AccessioniPrimary (citable) accession number: Q91VS8
Secondary accession number(s): E9QJS4, Q3TAP2, Q69ZZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.