FH7_ARATH
ID FH7_ARATH Reviewed; 929 AA.
AC Q9XIE0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Formin-like protein 7;
DE Short=AtFH7;
DE Short=AtFORMIN-7;
GN Name=FH7; OrderedLocusNames=At1g59910; ORFNames=F23H11.22;
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 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 [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:0000250}.
CC -!- SIMILARITY: Belongs to the formin-like family. Class-I subfamily.
CC {ECO:0000305}.
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DR EMBL; AC007258; AAD39332.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33639.1; -; Genomic_DNA.
DR EMBL; BT010460; AAQ62880.1; -; mRNA.
DR PIR; C96623; C96623.
DR RefSeq; NP_176199.1; NM_104683.3.
DR AlphaFoldDB; Q9XIE0; -.
DR SMR; Q9XIE0; -.
DR STRING; 3702.AT1G59910.1; -.
DR iPTMnet; Q9XIE0; -.
DR PaxDb; Q9XIE0; -.
DR PRIDE; Q9XIE0; -.
DR ProteomicsDB; 228906; -.
DR EnsemblPlants; AT1G59910.1; AT1G59910.1; AT1G59910.
DR GeneID; 842285; -.
DR Gramene; AT1G59910.1; AT1G59910.1; AT1G59910.
DR KEGG; ath:AT1G59910; -.
DR Araport; AT1G59910; -.
DR TAIR; locus:2025981; AT1G59910.
DR eggNOG; KOG1922; Eukaryota.
DR HOGENOM; CLU_007699_3_0_1; -.
DR InParanoid; Q9XIE0; -.
DR OMA; PNFMSES; -.
DR OrthoDB; 1204639at2759; -.
DR PRO; PR:Q9XIE0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XIE0; baseline and differential.
DR Genevisible; Q9XIE0; AT.
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; 2.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 2: Evidence at transcript level;
KW Reference proteome.
FT CHAIN 1..929
FT /note="Formin-like protein 7"
FT /id="PRO_0000308532"
FT DOMAIN 453..884
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 98582 MW; 0865DF1699BF1A6F CRC64;
MSFLFRKNGS SSRRKIKEKL RGRHSDRGGK REEDERYGGS GSDLPPPPSP WGFLFPEDFV
RIDGNLKAVI VDDEGLDVIY WKKLLELENS GKIRKNPKPR RRGDKSGDGF RRTGADQDDN
DDGDDEVGDE SIEEAFSFHV KKSQSASSSG GEIRDQSNNG GGGGGGGGGG GRYYTSSSAS
PSRPSSSSAS AASPSRTSYA TSAGSDYGGG GGGKQSQSKF QAPGGGSFPS SPSQIHSGGG
RSPPLPLPPG QFTAGNASFP SSTQPPPGQY MAGNASFPSS TPPPPGQYMA GNAPFSSSTP
LPPGQYPAVN AQLSTSAPSV PLPPGQYTAV NAPFSTSTQP VSLPPGQYMP GNAALSASTP
LTPGQFTTAN APPAPPGPAN QTSPPPPPPP SAAAPPPPPP PKKGPAAPPP PPPPGKKGAG
PPPPPPMSKK GPPKPPGNPK GPTKSGETSL AVGKTEDPTQ PKLKPLHWDK MNPDASRSMV
WHKIDGGSFN FDGDLMEALF GYVARKPSES NSVPQNQTVS NSVPHNQTYI LDPRKSQNKA
IVLKSLGMTK EEIIDLLTEG HDAESDTLEK LAGIAPTPEE QTEIIDFDGE PMTLAYADSL
LFHILKAVPS AFNRFNVMLF KINYGSEVAQ QKGSLLTLES ACNELRARGL FMKLLEAILK
AGNRMNAGTA RGNAQAFNLT ALRKLSDVKS VDAKTTLLHF VVEEVVRSEG KRAAMNKNMM
SSDNGSGENA DMSREEQEIE FIKMGLPIIG GLSSEFTNVK KAAGIDYDSF VATTLALGTR
VKETKRLLDQ SKGKEDGCLT KLRSFFESAE EELKVITEEQ LRIMELVKKT TNYYQAGALK
ERNLFQLFVI IRDFLGMVDN ACSEIARNQR KQQQQRPATT VAGASSSPAE TPSVAAAPQR
NAVRFPILPP NFMSESSRYS SSSDSDSES
