FH6_ARATH
ID FH6_ARATH Reviewed; 899 AA.
AC Q9FJX6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Formin-like protein 6;
DE Short=AtFH6;
DE Short=AtFORMIN-6;
DE Flags: Precursor;
GN Name=FH6; OrderedLocusNames=At5g67470; ORFNames=K9I9.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=15319477; DOI=10.1105/tpc.104.024372;
RA Favery B., Chelysheva L.A., Lebris M., Jammes F., Marmagne A.,
RA De Almeida-Engler J., Lecomte P., Vaury C., Arkowitz R.A., Abad P.;
RT "Arabidopsis formin AtFH6 is a plasma membrane-associated protein
RT upregulated in giant cells induced by parasitic nematodes.";
RL Plant Cell 16:2529-2540(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP GENE FAMILY ORGANIZATION.
RX PubMed=11104517; DOI=10.1186/gb-2000-1-1-research001;
RA Cvrckova F.;
RT "Are plant formins integral membrane proteins?";
RL Genome Biol. 1:RESEARCH001.1-RESEARCH001.7(2000).
RN [5]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=12417149; DOI=10.1016/s1360-1385(02)02341-5;
RA Deeks M.J., Hussey P.J., Davies B.;
RT "Formins: intermediates in signal-transduction cascades that affect
RT cytoskeletal reorganization.";
RL Trends Plant Sci. 7:492-498(2002).
RN [6]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=15256004; DOI=10.1186/1471-2164-5-44;
RA Cvrckova F., Novotny M., Pickova D., Zarsky V.;
RT "Formin homology 2 domains occur in multiple contexts in angiosperms.";
RL BMC Genomics 5:44-44(2004).
CC -!- FUNCTION: Might be involved in the organization and polarity of the
CC actin cytoskeleton. {ECO:0000269|PubMed:15319477}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15319477}; Single-
CC pass membrane protein {ECO:0000269|PubMed:15319477}.
CC -!- INDUCTION: Up-regulated during gall formation induced by root-knot
CC nematodes. {ECO:0000269|PubMed:15319477}.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000305}.
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DR EMBL; AY337456; AAQ99143.1; -; mRNA.
DR EMBL; AB013390; BAB08455.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98348.1; -; Genomic_DNA.
DR RefSeq; NP_201548.1; NM_126147.4.
DR AlphaFoldDB; Q9FJX6; -.
DR SMR; Q9FJX6; -.
DR STRING; 3702.AT5G67470.1; -.
DR iPTMnet; Q9FJX6; -.
DR PaxDb; Q9FJX6; -.
DR PRIDE; Q9FJX6; -.
DR ProteomicsDB; 230777; -.
DR EnsemblPlants; AT5G67470.1; AT5G67470.1; AT5G67470.
DR GeneID; 836883; -.
DR Gramene; AT5G67470.1; AT5G67470.1; AT5G67470.
DR KEGG; ath:AT5G67470; -.
DR Araport; AT5G67470; -.
DR TAIR; locus:2158576; AT5G67470.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_007699_0_0_1; -.
DR InParanoid; Q9FJX6; -.
DR OMA; CRDTAFY; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; Q9FJX6; -.
DR PRO; PR:Q9FJX6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJX6; baseline and differential.
DR Genevisible; Q9FJX6; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0005819; C:spindle; HDA:TAIR.
DR GO; GO:0003779; F:actin binding; ISS:TAIR.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR027643; Formin-like_plant.
DR PANTHER; PTHR23213; PTHR23213; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..899
FT /note="Formin-like protein 6"
FT /id="PRO_0000308531"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 452..867
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 35..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 98650 MW; F7D035CA83C5BFD1 CRC64;
MKALQSRFFF FFFFYIFFSV SVSSEAHRRI LHQPLFPESS TPPPPDFQST PSPPLPDTPD
QPFFPENPST PQQTLFPPPP PPVSADVNGG LPIPTATTQS AKPGKKVAIV ISVGIVTLGM
LSALAFFLYR HKAKHASDTQ KLVTGGGDGG GSRRFQEDSG PPTTTSSTFL YMGTVEPTRV
SASESNGGTN GPVNSSPYRK LNSAKRSERY RPSPELQPLP PLAKPPQPSD NSPSALSPSS
SSSGEECRDT AFYTPHGSAI SSDDGYYTAF PRSANGSLPH SKRTSPRSKF GSAPTTAASR
SPEMKHVIIP SIKQKLPPPV QPPPLRGLES DEQELPYSQN KPKFSQPPPP PNRAAFQAIT
QEKSPVPPPR RSPPPLQTPP PPPPPPPLAP PPPPQKRPRD FQMLRKVTNS EATTNSTTSP
SRKQAFKTPS PKTKAVEEVN SVSAGSLEKS GDGDTDPSKP KLKPLHWDKV RASSDRATVW
DQLKSSSFQL NEDRMEHLFG CNSGSSAPKE PVRRSVIPLA ENENRVLDPK KSQNIAILLR
ALNVTREEVS EALTDGNPES LGAELLETLV KMAPTKEEEI KLREYSGDVS KLGTAERFLK
TILDIPFAFK RVEAMLYRAN FDAEVKYLRN SFQTLEEASL ELKASRLFLK LLEAVLMTGN
RMNVGTNRGD AIAFKLDTLL KLVDIKGVDG KTTLLHFVVQ EITRSEGTTT TKDETILHGN
NDGFRKQGLQ VVAGLSRDLV NVKKSAGMDF DVLSSYVTKL EMGLDKLRSF LKTETTQGRF
FDSMKTFLKE AEEEIRKIKG GERKALSMVK EVTEYFHGNA AREEAHPLRI FMVVRDFLGV
LDNVCKEVKT MQEMSTSMGS ASARSFRISA TASLPVLHRY KARQDDTSSD SEHSSNSST
