FIMB1_ARATH
ID FIMB1_ARATH Reviewed; 687 AA.
AC Q7G188; O49182; O49963; Q9SZ12;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Fimbrin-1 {ECO:0000303|PubMed:11123801};
DE Short=AtFIM1;
DE AltName: Full=Fimbrin1 {ECO:0000305};
GN Name=FIM1 {ECO:0000303|PubMed:11123801};
GN OrderedLocusNames=At4g26700 {ECO:0000312|Araport:AT4G26700};
GN ORFNames=F10M23.40 {ECO:0000312|EMBL:CAB36516.1};
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9484459; DOI=10.1023/a:1005884112192;
RA McCurdy D.W., Kim M.;
RT "Molecular cloning of a novel fimbrin-like cDNA from Arabidopsis
RT thaliana.";
RL Plant Mol. Biol. 36:23-31(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 [GENOMIC DNA] OF 1-647, AND NUCLEOTIDE SEQUENCE [MRNA]
RP OF 179-687.
RC STRAIN=cv. Columbia;
RA Christensen H.E.M., Mathur J., Chua N.H.;
RT "Arabidopsis fimbrin.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INTERACTION WITH F-ACTIN.
RX PubMed=11123801; DOI=10.1046/j.1365-313x.2000.00907.x;
RA Kovar D.R., Staiger C.J., Weaver E.A., McCurdy D.W.;
RT "AtFim1 is an actin filament crosslinking protein from Arabidopsis
RT thaliana.";
RL Plant J. 24:625-636(2000).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11506361; DOI=10.1007/s004250000494;
RA Kovar D.R., Gibbon B.C., McCurdy D.W., Staiger C.J.;
RT "Fluorescently-labeled fimbrin decorates a dynamic actin filament network
RT in live plant cells.";
RL Planta 213:390-395(2001).
RN [7]
RP DOMAIN.
RX PubMed=15362112; DOI=10.1002/cm.20024;
RA Wang Y.-S., Motes C.M., Mohamalawari D.R., Blancaflor E.B.;
RT "Green fluorescent protein fusions to Arabidopsis fimbrin 1 for spatio-
RT temporal imaging of F-actin dynamics in roots.";
RL Cell Motil. Cytoskeleton 59:79-93(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 123-623, AND DOMAIN.
RX PubMed=15274920; DOI=10.1016/j.str.2004.04.010;
RA Klein M.G., Shi W., Ramagopal U., Tseng Y., Wirtz D., Kovar D.R.,
RA Staiger C.J., Almo S.C.;
RT "Structure of the actin crosslinking core of fimbrin.";
RL Structure 12:999-1013(2004).
CC -!- FUNCTION: Cross-links actin filaments (F-actin) in a calcium
CC independent manner. Induces the formation of actin aggregates.
CC Stabilizes and prevents F-actin depolymerization mediated by profilin.
CC Key regulator of actin cytoarchitecture, probably involved in cell
CC cycle, cell division, cell elongation and cytoplasmic tractus.
CC {ECO:0000269|PubMed:11123801, ECO:0000269|PubMed:11506361}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:11123801}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11506361}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q7G188-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Constitutively expressed in roots, leaves, flowers
CC and siliques, and to lower extent in stems.
CC {ECO:0000269|PubMed:9484459}.
CC -!- DOMAIN: The actin-binding domain 1 (also called ABD1) seems to not bind
CC F-actin alone while the second actin-binding domain (ABD2) can bind F-
CC actin alone. EF-hand domain and the last 65 C-terminal amino acids are
CC not required to cross-link F-actin, but enhance the stability of the
CC binding. {ECO:0000269|PubMed:15274920, ECO:0000269|PubMed:15362112}.
CC -!- MISCELLANEOUS: Cross-links actin with a constant of dissociation of
CC 0.55 uM and stoichiometry of 4 molecules of F-actin for one molecule of
CC FIM1. {ECO:0000269|PubMed:11123801}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB97846.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U66424; AAC39359.1; -; mRNA.
DR EMBL; AL035440; CAB36516.1; -; Genomic_DNA.
DR EMBL; AL161565; CAB79525.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85239.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85240.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66885.1; -; Genomic_DNA.
DR EMBL; AF042668; AAB97843.1; -; mRNA.
DR EMBL; AF042670; AAB97846.1; ALT_SEQ; Genomic_DNA.
DR PIR; T04793; T04793.
DR RefSeq; NP_001031726.1; NM_001036649.1. [Q7G188-1]
DR RefSeq; NP_001328753.1; NM_001341826.1. [Q7G188-1]
DR RefSeq; NP_194400.1; NM_118804.5. [Q7G188-1]
DR PDB; 1PXY; X-ray; 2.40 A; A/B=123-623.
DR PDBsum; 1PXY; -.
DR AlphaFoldDB; Q7G188; -.
DR SMR; Q7G188; -.
DR BioGRID; 14064; 1.
DR STRING; 3702.AT4G26700.2; -.
DR iPTMnet; Q7G188; -.
DR PaxDb; Q7G188; -.
DR PRIDE; Q7G188; -.
DR ProteomicsDB; 230097; -. [Q7G188-1]
DR EnsemblPlants; AT4G26700.1; AT4G26700.1; AT4G26700. [Q7G188-1]
DR EnsemblPlants; AT4G26700.2; AT4G26700.2; AT4G26700. [Q7G188-1]
DR EnsemblPlants; AT4G26700.4; AT4G26700.4; AT4G26700. [Q7G188-1]
DR GeneID; 828777; -.
DR Gramene; AT4G26700.1; AT4G26700.1; AT4G26700. [Q7G188-1]
DR Gramene; AT4G26700.2; AT4G26700.2; AT4G26700. [Q7G188-1]
DR Gramene; AT4G26700.4; AT4G26700.4; AT4G26700. [Q7G188-1]
DR KEGG; ath:AT4G26700; -.
DR Araport; AT4G26700; -.
DR TAIR; locus:2116382; AT4G26700.
DR eggNOG; KOG0046; Eukaryota.
DR InParanoid; Q7G188; -.
DR OrthoDB; 312506at2759; -.
DR PhylomeDB; Q7G188; -.
DR EvolutionaryTrace; Q7G188; -.
DR PRO; PR:Q7G188; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q7G188; baseline and differential.
DR Genevisible; Q7G188; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0051639; P:actin filament network formation; IDA:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IEP: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; 1.
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; 2.
DR PROSITE; PS50021; CH; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Calcium; Cytoplasm;
KW Cytoskeleton; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..687
FT /note="Fimbrin-1"
FT /id="PRO_0000073753"
FT DOMAIN 7..55
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 59..94
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 123..240
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 268..371
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 392..498
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 513..621
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 123..371
FT /note="Actin-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00300"
FT REGION 392..621
FT /note="Actin-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00300"
FT REGION 627..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT CONFLICT 120
FT /note="T -> A (in Ref. 1; AAC39359)"
FT /evidence="ECO:0000305"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1PXY"
FT TURN 141..146
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 225..241
FT /evidence="ECO:0007829|PDB:1PXY"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:1PXY"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:1PXY"
FT TURN 296..300
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 302..311
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 326..339
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 356..369
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 390..402
FT /evidence="ECO:0007829|PDB:1PXY"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:1PXY"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 422..431
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 449..465
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 475..479
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 483..503
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 516..528
FT /evidence="ECO:0007829|PDB:1PXY"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 542..546
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 548..557
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 573..590
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 598..602
FT /evidence="ECO:0007829|PDB:1PXY"
FT HELIX 606..620
FT /evidence="ECO:0007829|PDB:1PXY"
SQ SEQUENCE 687 AA; 76928 MW; 4190E4BBDCF55875 CRC64;
MSGYVGVVVS DPWLQSQFTQ VELRTLNSKY VSVKNQNGKV TIEDLPPLFA KLKALSATFK
EDEIKGMLGE LGSDTSTDVS FEEFLKIYLN LLSKAAEKSG GHHKNSSSFL KACTTTLLHT
IYQSEKGPFV QHINRYLGDD PFLKQFLPLD PHSNQLYELV KDGVLLCKLI NVAVPGTIDE
RAINTKRVLN PWERNENHTL CLNSAKAVGC SVVNIGTQDL AEGRPHLVLG LISQLIKIQV
LADLNLKKTP QLVELLEDSD DVEELLRLPP EKVLLKWMNF HLKKGGYKKT VSNFSADLKD
AQAYAFLLNV LAPEHCDPAT LDAKDPLERA ELVLSHAERM NCKRYLTAEE IVEGSSTLNL
AFVAQIFHER NGLNKDGKYA FAEMMTEDVE TCRDERCYRL WINSLGIDSY VNNVFEDVRN
GWILLEVLDK VSPSSVNWKH ASKPPIKMPF RKVENCNQVI KIGKQLKFSL VNVAGNDIVQ
GNKKLILGLL WQLMRFHMLQ LLKSLRSRTL GKEMTDADIL SWANRKVRTM GRKLQIESFK
DKSLSSGLFF LNLLWAVEPR VVNWNLVTKG ETDDEKRLNA TYIVSVARKL GCSVFLLPED
IVEVNQKMIL ILTASIMYWS LQRHSRESSD SSSTQSTTTT CTSTASSPAP SVTEEEEVSS
LSGEVTSLAV GDAVSEITTV SEEASIE
