FIMB4_ARATH
ID FIMB4_ARATH Reviewed; 652 AA.
AC Q9SJ84;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Fimbrin-4 {ECO:0000305};
DE Short=AtFIM4;
DE AltName: Full=Fimbrin4 {ECO:0000305};
GN Name=FIM4 {ECO:0000305};
GN OrderedLocusNames=At2g04750 {ECO:0000312|Araport:AT2G04750};
GN ORFNames=F28I8.21 {ECO:0000312|EMBL:AAD22331.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
CC -!- FUNCTION: Cross-links actin filaments (F-actin). Stabilizes and
CC prevents F-actin depolymerization mediated by profilin. May regulate
CC actin cytoarchitecture, cell cycle, cell division, cell elongation and
CC cytoplasmic tractus. {ECO:0000250|UniProtKB:Q7G188}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000250|UniProtKB:Q7G188}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q7G188}.
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DR EMBL; AC006955; AAD22331.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05860.1; -; Genomic_DNA.
DR PIR; A84461; A84461.
DR RefSeq; NP_178552.1; NM_126505.1.
DR AlphaFoldDB; Q9SJ84; -.
DR SMR; Q9SJ84; -.
DR STRING; 3702.AT2G04750.1; -.
DR PaxDb; Q9SJ84; -.
DR PRIDE; Q9SJ84; -.
DR EnsemblPlants; AT2G04750.1; AT2G04750.1; AT2G04750.
DR GeneID; 815018; -.
DR Gramene; AT2G04750.1; AT2G04750.1; AT2G04750.
DR KEGG; ath:AT2G04750; -.
DR Araport; AT2G04750; -.
DR TAIR; locus:2049158; AT2G04750.
DR eggNOG; KOG0046; Eukaryota.
DR HOGENOM; CLU_015284_3_1_1; -.
DR InParanoid; Q9SJ84; -.
DR OMA; TVNHLYV; -.
DR OrthoDB; 312506at2759; -.
DR PhylomeDB; Q9SJ84; -.
DR PRO; PR:Q9SJ84; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJ84; baseline and differential.
DR Genevisible; Q9SJ84; AT.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR CDD; cd00014; CH; 3.
DR Gene3D; 1.10.418.10; -; 4.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR039959; Fimbrin/Plastin.
DR PANTHER; PTHR19961; PTHR19961; 1.
DR Pfam; PF00307; CH; 4.
DR SMART; SM00033; CH; 4.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 4.
PE 3: Inferred from homology;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT CHAIN 1..652
FT /note="Fimbrin-4"
FT /id="PRO_0000430599"
FT DOMAIN 116..233
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 261..364
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 388..494
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 509..617
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 116..364
FT /note="Actin-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00300"
FT REGION 388..617
FT /note="Actin-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00300"
FT REGION 623..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 652 AA; 73443 MW; BCA95FDCA22C7DF0 CRC64;
MSSYVGVLVS DPWLQSQFTQ VELRTLKSKF YSTKTRFGRV TVKHLPPVFA KLKYFNGKFD
ENEIKTILDE SYPNRAKEVE FETFLRAFLS VQSRGSKGAS SFLKTSTTTF HHSINESEKA
SYVSHINSYL KDEPNLKSYL PINPTTNALF DLVKDGVLLC KLINIAVPGT IDERAINTKK
ELNPWERTEN LSLCLNSAKA IGCTVVNIGT QDIAEGTPHL VLGLIFQIIK IQLLADLNLK
KTPQLVELVE ENQDVEELMG LAPEKLLLKW MNFHLKKAGY EKQVTNFSSD VKDGEAYAYL
LNALAPEHST NVTLEIKDPS ERATKVLEQA EKLDCKRFLS PKDIVEGSAN LNLAFVAQLF
HHRNGLSDES PKVPISVAEM VTEDEETSRE ERCFRHWMNS LGAVTYVDNV FEDVRNGWVL
LEVLDKVSPG SVNWKHANKP PIKMPFKKVE NCNQVIKIGK ELNFSLVNVA GHDIMQGNKK
LLLAFLWQLM RYTMLQILNN LRSHCQGKDI TEADILNWAN RKVKKSGRTS QAVSFKDKNL
ANGIFFLELL SAVEPRVVNW SLVSKGETQE EKNLNATYII SVARKLGCSI FLLPEDILEV
NQRMMLILAA SIMNWSLQQQ SDTESTVSDD TDVSSVTEEI SNLSTDDGSS DV
