(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 135.
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};
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   SMR; Q7G188; -.
DR   BioGrid; 14064; 1.
DR   STRING; 3702.AT4G26700.2; -.
DR   iPTMnet; Q7G188; -.
DR   PaxDb; Q7G188; -.
DR   PRIDE; Q7G188; -.
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   eggNOG; COG5069; LUCA.
DR   HOGENOM; HOG000213447; -.
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;
DR   PRODOM; Q7G188.
DR   SWISS-2DPAGE; Q7G188.
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   CA_BIND         33..44
FT                   /evidence="ECO:0000255"
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   COMPBIAS        620..662
FT                   /note="Ser-rich"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        637..644
FT                   /note="Thr-rich"
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:0000244|PDB:1PXY"
FT   TURN            141..146
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           155..159
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           164..173
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           180..182
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           191..207
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           217..222
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           225..241
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   STRAND          242..246
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   TURN            262..264
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           270..284
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   TURN            296..300
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           302..311
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           313..315
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           318..322
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           326..339
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           348..352
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           356..369
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           390..402
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   TURN            403..406
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           414..417
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   TURN            418..420
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           422..431
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           438..440
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           449..465
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           475..479
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           483..503
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           516..528
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   TURN            529..531
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           542..546
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           548..557
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           559..561
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           573..590
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           598..602
FT                   /evidence="ECO:0000244|PDB:1PXY"
FT   HELIX           606..620
FT                   /evidence="ECO:0000244|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
//

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