FH4_ARATH
ID FH4_ARATH Reviewed; 763 AA.
AC O48682; F4I956;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Formin-like protein 4;
DE Short=AtFH4;
DE Short=AtFORMIN-4;
DE Flags: Precursor;
GN Name=FH4; OrderedLocusNames=At1g24150; ORFNames=F3I6.8;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
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 [5]
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
RX PubMed=16313636; DOI=10.1111/j.1469-8137.2005.01582.x;
RA Deeks M.J., Cvrckova F., Machesky L.M., Mikitova V., Ketelaar T.,
RA Zarsky V., Davies B., Hussey P.J.;
RT "Arabidopsis group Ie formins localize to specific cell membrane domains,
RT interact with actin-binding proteins and cause defects in cell expansion
RT upon aberrant expression.";
RL New Phytol. 168:529-540(2005).
CC -!- FUNCTION: Might be involved in the organization and polarity of the
CC actin cytoskeleton. {ECO:0000269|PubMed:16313636}.
CC -!- SUBUNIT: Interacts with profilin. {ECO:0000269|PubMed:16313636}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16313636};
CC Single-pass membrane protein {ECO:0000269|PubMed:16313636}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant (at protein level).
CC {ECO:0000269|PubMed:16313636}.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00575.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC00575.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC002396; AAC00575.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30487.2; -; Genomic_DNA.
DR PIR; T00645; T00645.
DR RefSeq; NP_001319073.1; NM_001332639.1.
DR AlphaFoldDB; O48682; -.
DR SMR; O48682; -.
DR BioGRID; 24266; 2.
DR STRING; 3702.AT1G24150.1; -.
DR iPTMnet; O48682; -.
DR PeptideAtlas; O48682; -.
DR PRIDE; O48682; -.
DR ProteomicsDB; 230512; -.
DR EnsemblPlants; AT1G24150.2; AT1G24150.2; AT1G24150.
DR GeneID; 839028; -.
DR Gramene; AT1G24150.2; AT1G24150.2; AT1G24150.
DR KEGG; ath:AT1G24150; -.
DR Araport; AT1G24150; -.
DR eggNOG; KOG1922; Eukaryota.
DR InParanoid; O48682; -.
DR OrthoDB; 596704at2759; -.
DR PhylomeDB; O48682; -.
DR PRO; PR:O48682; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O48682; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..763
FT /note="Formin-like protein 4"
FT /id="PRO_0000308529"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 303..738
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 52..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 84066 MW; 9C5F96A12A994F65 CRC64;
MAAMLMQPWP PFLPHLTLVF LTLILFFPNQ SFSQSDSPRN IETFFPNDTI TPPVQSPVLS
PPQNPSSSSS DSDRGNILRA VLITAASTLL VAAVFFFLVH KCRRRRNRVG GVDNTLQPPV
PPLAEAALAR EGFTRFGGNV KGLILDENGL DVLYWRKLQQ SQRDNKGGSF RKEIIHGDDE
EKNVIYSKSK KKSGPVTETP LLRGRSSTSH SVIHNDNYRN ATTTHPPHVK TDSFEFVKPD
PTPPPPPPPP IPVKQSATPP PPPPPKLKNN GPSPPPPPPL KKTAALSSSA SKKPPPAPRG
SSSGESSNGQ VKLKPLHWDK VNPDSDHSMV WDKIDRGSFS FDGDLMEALF GYVAVGKKSP
DDGGDKKPSS ASPAQIFILD PRKSQNTAIV LKSLGMTRDE LVESLMEGHD FHPDTLERLS
RIAPTKEEQS AILQFDGDTK MLADAESFLF HLLKAVPCAF TRLNALLFRA NYYPEISNHN
KNLQTLDLAC TELRSRGLFV KLLEAILKSG NRMNAGTARG DAQAFNLTAL LKLSDVKSVD
GKTTLLNFVV EEVVRSEGKR CVLNRRTNRS FSRSSSSSIS EVISKEEQEK EYLRLGLPVV
GGLSSEFTNV KKAAAVDYDT VAATCLALTS RAKDARRVLA QSEGDNKEGV RFVKKMNEFL
DSVEEEVKLA KEEEKKVLEL VKRTTEYYQA GAVKGKNPLH LFVIVRDFLA MVDKVCVEIA
RNLQRRSSMG STQQRNAVKF PVLPPNFMSD RSRSDSGGSD SDM
