FH5_ARATH
ID FH5_ARATH Reviewed; 900 AA.
AC Q94B77; Q0WPT9; Q6PSU8; Q9FIU0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Formin-like protein 5;
DE Short=AtFH5;
DE Short=AtFORMIN-5;
DE AltName: Full=Formin homology 2 domain-containing protein 5;
GN Name=FH5; Synonyms=FHP5; OrderedLocusNames=At5g54650; ORFNames=MRB17.15;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=cv. C24;
RX PubMed=15765105; DOI=10.1038/ncb1238;
RA Ingouff M., Fitz Gerald J.N., Guerin C., Robert H., Sorensen M.B.,
RA Van Damme D., Geelen D., Blanchoin L., Berger F.;
RT "Plant formin AtFH5 is an evolutionarily conserved actin nucleator involved
RT in cytokinesis.";
RL Nat. Cell Biol. 7:374-380(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-204.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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. Interacts with the barbed end of actin filaments
CC and nucleates actin-filament polymerization in vitro. Seems to play a
CC role in cytokinesis. {ECO:0000269|PubMed:15765105}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the endosperm. Localizes to the cell
CC plate, a plant-specific membranous component that is assembled at the
CC plane of cell division. {ECO:0000269|PubMed:15765105}.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000305}.
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DR EMBL; AY581683; AAS93430.1; -; mRNA.
DR EMBL; AY611066; AAT37554.1; -; Genomic_DNA.
DR EMBL; AB016879; BAB09344.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96522.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96523.1; -; Genomic_DNA.
DR EMBL; AY042801; AAK68741.1; -; mRNA.
DR EMBL; AY128923; AAM91323.1; -; mRNA.
DR EMBL; AK228971; BAF00860.1; -; mRNA.
DR RefSeq; NP_200276.1; NM_124846.2.
DR RefSeq; NP_851191.1; NM_180860.2.
DR AlphaFoldDB; Q94B77; -.
DR SMR; Q94B77; -.
DR BioGRID; 20798; 1.
DR STRING; 3702.AT5G54650.1; -.
DR iPTMnet; Q94B77; -.
DR PaxDb; Q94B77; -.
DR PRIDE; Q94B77; -.
DR ProteomicsDB; 228904; -.
DR EnsemblPlants; AT5G54650.1; AT5G54650.1; AT5G54650.
DR EnsemblPlants; AT5G54650.2; AT5G54650.2; AT5G54650.
DR GeneID; 835554; -.
DR Gramene; AT5G54650.1; AT5G54650.1; AT5G54650.
DR Gramene; AT5G54650.2; AT5G54650.2; AT5G54650.
DR KEGG; ath:AT5G54650; -.
DR Araport; AT5G54650; -.
DR TAIR; locus:2172129; AT5G54650.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_007699_1_1_1; -.
DR InParanoid; Q94B77; -.
DR OMA; MEETSWA; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; Q94B77; -.
DR PRO; PR:Q94B77; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94B77; baseline and differential.
DR Genevisible; Q94B77; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0003779; F:actin binding; ISS:TAIR.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0030041; P:actin filament polymerization; IDA:TAIR.
DR GO; GO:0045010; P:actin nucleation; IDA:TAIR.
DR GO; GO:0009960; P:endosperm development; IMP:TAIR.
DR GO; GO:0048317; P:seed morphogenesis; IGI: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; 2.
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-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..900
FT /note="Formin-like protein 5"
FT /id="PRO_0000308530"
FT TRANSMEM 15..32
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 433..865
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 136..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..428
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 65
FT /note="Q -> L (in Ref. 1; AAS93430/AAT37554)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="S -> A (in Ref. 1; AAS93430/AAT37554)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="Q -> P (in Ref. 1; AAS93430/AAT37554)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="K -> T (in Ref. 1; AAS93430/AAT37554)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="E -> G (in Ref. 4; AAK68741/AAM91323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 98358 MW; 36A0AA6D01252524 CRC64;
MVGMIRGGMG DQNWSRLVFW LILFSGLLVI TLEENPEKDE IFLSQFMAPS TGQVNEHMEE
TSWAQRCWQD SDCVKEAVAE FNLCFPGSKD SRELFGLNHT NLKQTLLDCI QEKGKLNGHN
PKYLELLSSM LDIPRRNLAT KPGSSPSPSP SRPPKRSRGP PRPPTRPKSP PPRKSSFPPS
RSPPPPPAKK NASKNSTSAP VSPAKKKEDH EKTIIIAVVV TAVSTFLLAA LFFLCCSRVC
GNGSGGRKND ERPLLSLSSS DYSVGSSINY GGSVKGDKQG HQSFNIYSNQ GKMSSFDGSN
SDTSDSLEER LSHEGLRNNS ITNHGLPPLK PPPGRTASVL SGKSFSGKVE PLPPEPPKFL
KVSSKKASAP PPPVPAPQMP SSAGPPRPPP PAPPPGSGGP KPPPPPGPKG PRPPPPMSLG
PKAPRPPSGP ADALDDDAPK TKLKPFFWDK VQANPEHSMV WNDIRSGSFQ FNEEMIESLF
GYAAADKNKN DKKGSSGQAA LPQFVQILEP KKGQNLSILL RALNATTEEV CDALREGNEL
PVEFIQTLLK MAPTPEEELK LRLYCGEIAQ LGSAERFLKA VVDIPFAFKR LEALLFMCTL
HEEMAFVKES FQKLEVACKE LRGSRLFLKL LEAVLKTGNR MNDGTFRGGA QAFKLDTLLK
LADVKGTDGK TTLLHFVVQE IIRTEGVRAA RTIRESQSFS SVKTEDLLVE ETSEESEENY
RNLGLEKVSG LSSELEHVKK SANIDADGLT GTVLKMGHAL SKARDFVNSE MKSSGEESGF
REALEDFIQN AEGSIMSILE EEKRIMALVK STGDYFHGKA GKDEGLRLFV IVRDFLIILD
KSCKEVREAR GRPVRMARKQ GSTASASSET PRQTPSLDPR QKLFPAITER RVDQSSSDSD
