FIMB5_ARATH
ID FIMB5_ARATH Reviewed; 687 AA.
AC Q9FKI0; Q56Z07;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Fimbrin-5 {ECO:0000305};
DE Short=AtFIM5;
DE AltName: Full=Fimbrin-like protein 2 {ECO:0000312|EMBL:AED94007.1};
DE AltName: Full=Fimbrin5 {ECO:0000303|PubMed:21098731};
GN Name=FIM5 {ECO:0000303|PubMed:21098731};
GN Synonyms=FIM2 {ECO:0000312|EMBL:AED94007.1};
GN OrderedLocusNames=At5g35700 {ECO:0000312|Araport:AT5G35700};
GN ORFNames=MXH1.5 {ECO:0000312|EMBL:BAB09267.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(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).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 551-687.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP F-ACTIN.
RX PubMed=21098731; DOI=10.1105/tpc.110.080283;
RA Wu Y., Yan J., Zhang R., Qu X., Ren S., Chen N., Huang S.;
RT "Arabidopsis FIMBRIN5, an actin bundling factor, is required for pollen
RT germination and pollen tube growth.";
RL Plant Cell 22:3745-3763(2010).
CC -!- FUNCTION: Cross-links actin filaments (F-actin) in a calcium
CC independent manner. Induces the formation of actin bundles. Stabilizes
CC and prevents F-actin depolymerization mediated by latrunculin B (LatB).
CC {ECO:0000269|PubMed:21098731}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:21098731}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q7G188}.
CC -!- TISSUE SPECIFICITY: Expressed in mature pollen.
CC {ECO:0000269|PubMed:21098731}.
CC -!- DISRUPTION PHENOTYPE: Delayed pollen germination and inhibition of
CC pollen tube growth due to the disorganization and redistribution of
CC actin filaments. {ECO:0000269|PubMed:21098731}.
CC -!- MISCELLANEOUS: Cross-links actin with a constant of dissociation of
CC 0.71 uM. {ECO:0000269|PubMed:21098731}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB011485; BAB09267.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94007.1; -; Genomic_DNA.
DR EMBL; AY045780; AAK76454.1; -; mRNA.
DR EMBL; AY142570; AAN13139.1; -; mRNA.
DR EMBL; AK221162; BAD95202.1; -; mRNA.
DR RefSeq; NP_198420.1; NM_122961.4.
DR AlphaFoldDB; Q9FKI0; -.
DR SMR; Q9FKI0; -.
DR STRING; 3702.AT5G35700.1; -.
DR PaxDb; Q9FKI0; -.
DR PRIDE; Q9FKI0; -.
DR ProteomicsDB; 228924; -.
DR EnsemblPlants; AT5G35700.1; AT5G35700.1; AT5G35700.
DR GeneID; 833544; -.
DR Gramene; AT5G35700.1; AT5G35700.1; AT5G35700.
DR KEGG; ath:AT5G35700; -.
DR Araport; AT5G35700; -.
DR TAIR; locus:2177291; AT5G35700.
DR eggNOG; KOG0046; Eukaryota.
DR HOGENOM; CLU_015284_3_1_1; -.
DR InParanoid; Q9FKI0; -.
DR OMA; AFNGTID; -.
DR OrthoDB; 312506at2759; -.
DR PhylomeDB; Q9FKI0; -.
DR PRO; PR:Q9FKI0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKI0; baseline and differential.
DR Genevisible; Q9FKI0; 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; IDA:TAIR.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:TAIR.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP: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; 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; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 4.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome; Repeat.
FT CHAIN 1..687
FT /note="Fimbrin-5"
FT /id="PRO_0000073754"
FT DOMAIN 7..74
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 122..239
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 267..370
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 122..370
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 628..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..687
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 76758 MW; 137CAEBDED0F40E3 CRC64;
MSSYVGVLVS DPWLQSQFTQ VELRTLKSKF VSNKTQLGRF TVGDLPPVFE KLKAFNGTID
EDEIKSVLDK SYPNADDEVD FEFFLRAFLS VQARGVEKSG GSKGASSFLK TSTTTVHHAI
NESEKASYVS HVNNYLRDDP FLKSYLPIDP ATNAFFDLVK DGVLLCKLIN VAVPGTIDER
AINTKKTLNP WERNENLTLG LNSAKAIGCT VVNIGTQDIA EGRPYLVLGL ISQIIKIQML
ADLNFKKTPS LFQLVDDTQD AEELMGLAPE KVLLKWMNFH LKKAGYEKQV TNFSSDLKDG
EAYAYLLNAL APEHSTHVAL ETKDPTERAK KVLEQAEKLD CKRYLSPKDI VDGSANLNLA
FVAQIFQHRN GLTVDDSKTS FAEMMTDDVE TSREERCFRL WINSLGTATY VNNVFEDLRN
GWVLLEVLDK VSPGSVNWKH ANKPPIKMPF KKVENCNEVI KIGKELRFSL VNVAGNDIVQ
GNKKLLLAFL WQLMRYTMLQ LLRNLRSHSQ GKEITDADIL NWANRKVKRG GRTSQADSFR
DKNLSSGMFF LELLSAVEPR VVNWSLVTNG ETEEDKKLNA TYIISVARKL GCSIFLLPED
IIEVNQKMML ILAASIMYWS LQQQSDTEST VSEDATDDGD ANSVAGEISN LSIDGASESS
PTVQDQELLT KADNDEDEVD GENNKDA
