FIMB3_ARATH
ID FIMB3_ARATH Reviewed; 714 AA.
AC Q9FJ70;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Fimbrin-3 {ECO:0000305};
DE Short=AtFIM3;
DE AltName: Full=Fimbrin3 {ECO:0000305};
GN Name=FIM3 {ECO:0000305};
GN OrderedLocusNames=At5g55400 {ECO:0000312|Araport:AT5G55400};
GN ORFNames=MTE17.11 {ECO:0000312|EMBL:BAB08557.1};
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=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 [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; AB015479; BAB08557.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96625.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70910.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70911.1; -; Genomic_DNA.
DR RefSeq; NP_001318801.1; NM_001345124.1.
DR RefSeq; NP_001332484.1; NM_001345126.1.
DR RefSeq; NP_001332485.1; NM_001345125.1.
DR AlphaFoldDB; Q9FJ70; -.
DR SMR; Q9FJ70; -.
DR STRING; 3702.AT5G55400.1; -.
DR PaxDb; Q9FJ70; -.
DR PRIDE; Q9FJ70; -.
DR ProteomicsDB; 230098; -.
DR EnsemblPlants; AT5G55400.1; AT5G55400.1; AT5G55400.
DR EnsemblPlants; AT5G55400.2; AT5G55400.2; AT5G55400.
DR EnsemblPlants; AT5G55400.3; AT5G55400.3; AT5G55400.
DR GeneID; 835633; -.
DR Gramene; AT5G55400.1; AT5G55400.1; AT5G55400.
DR Gramene; AT5G55400.2; AT5G55400.2; AT5G55400.
DR Gramene; AT5G55400.3; AT5G55400.3; AT5G55400.
DR KEGG; ath:AT5G55400; -.
DR Araport; AT5G55400; -.
DR TAIR; locus:2173867; AT5G55400.
DR eggNOG; KOG0046; Eukaryota.
DR HOGENOM; CLU_015284_3_1_1; -.
DR InParanoid; Q9FJ70; -.
DR OMA; DSEIISW; -.
DR OrthoDB; 312506at2759; -.
DR PhylomeDB; Q9FJ70; -.
DR PRO; PR:Q9FJ70; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJ70; baseline and differential.
DR Genevisible; Q9FJ70; 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:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR GO; GO:0051639; P:actin filament network formation; IDA:TAIR.
DR CDD; cd00014; CH; 3.
DR Gene3D; 1.10.418.10; -; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR039959; Fimbrin/Plastin.
DR PANTHER; PTHR19961; PTHR19961; 2.
DR Pfam; PF00307; CH; 4.
DR SMART; SM00033; CH; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 4.
PE 3: Inferred from homology;
KW Actin-binding; Calcium; Cytoplasm; Cytoskeleton; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..714
FT /note="Fimbrin-3"
FT /id="PRO_0000073755"
FT DOMAIN 7..55
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 124..241
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 269..372
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 393..499
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 514..622
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 124..372
FT /note="Actin-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00300"
FT REGION 393..622
FT /note="Actin-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00300"
FT REGION 628..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 79788 MW; 8D193BA3644B009C CRC64;
MSGFVGVIVS DPWLQSQLTQ VELRSLNSKF VALKNQSGKV TLEDLPSVLV KVKSLSSSFK
EKEIKEILGG LGSDYESDDD LDFESFLKVY LNLRDKAADK AGGGLKHSSS FLKAGTTTLH
TINQSEKGSF VLHINRYLGD DPFLKQFLPL DPDSNDLYEL VKDGVLLCKL INIAVPGTID
ERAINTKRVL NPWERNENHT LCLNSAKAVG CSVVNIGTQD LAEGRPHLVL GLISQLIKIQ
LLADLSLKKM PQLVELVEDN EDIEEFLRLP PEKVLLKWMN FHLKKGGYKK TVGNFSSDLK
DAQAYAYLLN VLAPEHCDPA TLNAEDDLER ANMVLEHAER MNCKRYLTAE EIVEGSSYLN
LAFVAQIFHE RNGLSTDGRF SFAEMMTEDL QTCRDERCYR LWINSLGIES YVNNVFEDVR
NGWILLEVVD KVYPGSVNWK QASKPPIKMP FRKVENCNQV VKIGKEMRFS LVNVAGNDIV
QGNKKLILGF LWQLMRTHML QLLKSLRSRT RGKDMTDSEI ISWANRKVRI MGRKSQIESF
KDKSLSSGLF FLDLLWAVEP RVVNWNLVTK GESDDEKRLN ATYIVSVARK LGCSVFLLPE
DIVEVNQKMI LILTASIMYW SLQQQSSSSE SSSSSSDSSS THSTTTTCTS TCTSTDASPA
PSVTGEDEVS SLNGEVSSLT IEEDNEVSSL TIEEDNDADI LSDITSISEE AANE
