FH8_ARATH
ID FH8_ARATH Reviewed; 760 AA.
AC O04532;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Formin-like protein 8;
DE Short=AtFH8;
DE Short=AtFORMIN-1;
DE Flags: Precursor;
GN Name=FH8; OrderedLocusNames=At1g70140; ORFNames=F20P5.14;
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, AND SUBCELLULAR LOCATION.
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).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15923338; DOI=10.1104/pp.104.055665;
RA Yi K., Guo C., Chen D., Zhao B., Yang B., Ren H.;
RT "Cloning and functional characterization of a formin-like protein (AtFH8)
RT from Arabidopsis.";
RL Plant Physiol. 138:1071-1082(2005).
CC -!- FUNCTION: Might be involved in the organization and polarity of the
CC actin cytoskeleton. Interacts with the barbed end of actin filaments
CC and nucleates actin-filament polymerization in vitro.
CC {ECO:0000269|PubMed:15923338, ECO:0000269|PubMed:16313636}.
CC -!- SUBUNIT: Interacts with profilin. {ECO:0000269|PubMed:15923338}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16313636};
CC Single-pass membrane protein {ECO:0000269|PubMed:16313636}.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000305}.
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DR EMBL; AC002062; AAB61101.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35024.1; -; Genomic_DNA.
DR PIR; B96724; B96724.
DR RefSeq; NP_177171.1; NM_105682.3.
DR AlphaFoldDB; O04532; -.
DR SMR; O04532; -.
DR BioGRID; 28571; 1.
DR STRING; 3702.AT1G70140.1; -.
DR iPTMnet; O04532; -.
DR PaxDb; O04532; -.
DR PRIDE; O04532; -.
DR ProteomicsDB; 230778; -.
DR EnsemblPlants; AT1G70140.1; AT1G70140.1; AT1G70140.
DR GeneID; 843350; -.
DR Gramene; AT1G70140.1; AT1G70140.1; AT1G70140.
DR KEGG; ath:AT1G70140; -.
DR Araport; AT1G70140; -.
DR TAIR; locus:2020568; AT1G70140.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_007699_3_0_1; -.
DR InParanoid; O04532; -.
DR OMA; PTCHCQT; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; O04532; -.
DR PRO; PR:O04532; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04532; baseline and differential.
DR Genevisible; O04532; AT.
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:0009506; C:plasmodesma; IDA:TAIR.
DR GO; GO:0003779; F:actin binding; ISS:TAIR.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR GO; GO:0005522; F:profilin binding; IDA:TAIR.
DR GO; GO:0045010; P:actin nucleation; IDA:TAIR.
DR GO; GO:0009932; P:cell tip growth; IMP:TAIR.
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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..760
FT /note="Formin-like protein 8"
FT /id="PRO_0000308533"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 296..732
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 83603 MW; F96CEBA5FCD94F38 CRC64;
MAAMFNHPWP NLTLIYFFFI VVLPFQSLSQ FDSPQNIETF FPISSLSPVP PPLLPPSSNP
SPPSNNSSSS DKKTITKAVL ITAASTLLVA GVFFFCLQRC IIARRRRDRV GPVRVENTLP
PYPPPPMTSA AVTTTTLARE GFTRFGGVKG LILDENGLDV LYWRKLQSQR ERSGSFRKQI
VTGEEEDEKE VIYYKNKKKT EPVTEIPLLR GRSSTSHSVI HNEDHQPPPQ VKQSEPTPPP
PPPSIAVKQS APTPSPPPPI KKGSSPSPPP PPPVKKVGAL SSSASKPPPA PVRGASGGET
SKQVKLKPLH WDKVNPDSDH SMVWDKIDRG SFSFDGDLME ALFGYVAVGK KSPEQGDEKN
PKSTQIFILD PRKSQNTAIV LKSLGMTREE LVESLIEGND FVPDTLERLA RIAPTKEEQS
AILEFDGDTA KLADAETFLF HLLKSVPTAF TRLNAFLFRA NYYPEMAHHS KCLQTLDLAC
KELRSRGLFV KLLEAILKAG NRMNAGTARG NAQAFNLTAL LKLSDVKSVD GKTSLLNFVV
EEVVRSEGKR CVMNRRSHSL TRSGSSNYNG GNSSLQVMSK EEQEKEYLKL GLPVVGGLSS
EFSNVKKAAC VDYETVVATC SALAVRAKDA KTVIGECEDG EGGRFVKTMM TFLDSVEEEV
KIAKGEERKV MELVKRTTDY YQAGAVTKGK NPLHLFVIVR DFLAMVDKVC LDIMRNMQRR
KVGSPISPSS QRNAVKFPVL PPNFMSDRAW SDSGGSDSDM
