WLI2B_ARATH
ID WLI2B_ARATH Reviewed; 199 AA.
AC Q9M047; B9DH94; F4IY27;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=LIM domain-containing protein WLIM2b {ECO:0000305};
DE AltName: Full=Widely-expressed LIM protein 2B {ECO:0000305};
GN Name=WLIM2B {ECO:0000303|PubMed:17573466};
GN OrderedLocusNames=At3g55770 {ECO:0000312|Araport:AT3G55770};
GN ORFNames=F1I16.180 {ECO:0000312|EMBL:CAB81602.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] (ISOFORM 1).
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17573466; DOI=10.1093/dnares/dsm013;
RA Arnaud D., Dejardin A., Leple J.C., Lesage-Descauses M.C., Pilate G.;
RT "Genome-wide analysis of LIM gene family in Populus trichocarpa,
RT Arabidopsis thaliana, and Oryza sativa.";
RL DNA Res. 14:103-116(2007).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP F-ACTIN.
RX PubMed=20817848; DOI=10.1105/tpc.110.075960;
RA Papuga J., Hoffmann C., Dieterle M., Moes D., Moreau F., Tholl S.,
RA Steinmetz A., Thomas C.;
RT "Arabidopsis LIM proteins: a family of actin bundlers with distinct
RT expression patterns and modes of regulation.";
RL Plant Cell 22:3034-3052(2010).
CC -!- FUNCTION: Binds to actin filaments and promotes cross-linking into
CC thick bundles. Has an actin-stabilizing activity. The actin regulatory
CC activities are not regulated by pH and [Ca(2+)].
CC {ECO:0000269|PubMed:20817848}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:20817848}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20817848}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M047-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M047-2; Sequence=VSP_056810;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. Barely detected in pollen. {ECO:0000269|PubMed:20817848}.
CC -!- MISCELLANEOUS: Cross-links actin with a constant of dissociation of 0.5
CC uM. {ECO:0000269|PubMed:20817848}.
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DR EMBL; AL161667; CAB81602.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79434.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79435.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79436.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79438.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79440.1; -; Genomic_DNA.
DR EMBL; AY063924; AAL36280.1; -; mRNA.
DR EMBL; AY091249; AAM14188.1; -; mRNA.
DR EMBL; AK317129; BAH19816.1; -; mRNA.
DR EMBL; AK317349; BAH20021.1; -; mRNA.
DR EMBL; AK317444; BAH20111.1; -; mRNA.
DR EMBL; AY084361; AAM60942.1; -; mRNA.
DR PIR; T47716; T47716.
DR RefSeq; NP_001030868.1; NM_001035791.1. [Q9M047-1]
DR RefSeq; NP_001030870.1; NM_001035793.2. [Q9M047-1]
DR RefSeq; NP_001190099.1; NM_001203170.1. [Q9M047-2]
DR RefSeq; NP_191136.1; NM_115435.6. [Q9M047-1]
DR RefSeq; NP_680133.2; NM_148878.2. [Q9M047-1]
DR AlphaFoldDB; Q9M047; -.
DR BioGRID; 10059; 5.
DR IntAct; Q9M047; 4.
DR iPTMnet; Q9M047; -.
DR PRIDE; Q9M047; -.
DR ProteomicsDB; 242768; -. [Q9M047-1]
DR EnsemblPlants; AT3G55770.1; AT3G55770.1; AT3G55770. [Q9M047-1]
DR EnsemblPlants; AT3G55770.2; AT3G55770.2; AT3G55770. [Q9M047-1]
DR EnsemblPlants; AT3G55770.3; AT3G55770.3; AT3G55770. [Q9M047-1]
DR EnsemblPlants; AT3G55770.5; AT3G55770.5; AT3G55770. [Q9M047-1]
DR EnsemblPlants; AT3G55770.7; AT3G55770.7; AT3G55770. [Q9M047-2]
DR GeneID; 824743; -.
DR Gramene; AT3G55770.1; AT3G55770.1; AT3G55770. [Q9M047-1]
DR Gramene; AT3G55770.2; AT3G55770.2; AT3G55770. [Q9M047-1]
DR Gramene; AT3G55770.3; AT3G55770.3; AT3G55770. [Q9M047-1]
DR Gramene; AT3G55770.5; AT3G55770.5; AT3G55770. [Q9M047-1]
DR Gramene; AT3G55770.7; AT3G55770.7; AT3G55770. [Q9M047-2]
DR KEGG; ath:AT3G55770; -.
DR Araport; AT3G55770; -.
DR TAIR; locus:2079006; AT3G55770.
DR OMA; VQCEGHS; -.
DR OrthoDB; 1583903at2759; -.
DR PhylomeDB; Q9M047; -.
DR PRO; PR:Q9M047; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M047; baseline and differential.
DR Genevisible; Q9M047; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR InterPro; IPR045268; LIMA-like.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24206; PTHR24206; 1.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00132; LIM; 2.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton; LIM domain;
KW Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..199
FT /note="LIM domain-containing protein WLIM2b"
FT /id="PRO_0000430594"
FT DOMAIN 8..68
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 106..166
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT VAR_SEQ 120
FT /note="K -> KIHNPLSYRELARKPNVLHRCIDPGDIGSCYFNLH (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056810"
FT CONFLICT 14
FT /note="E -> G (in Ref. 4; BAH20111)"
SQ SEQUENCE 199 AA; 21664 MW; 25AD823DBB2C567C CRC64;
MSFTGTQQKC KACEKTVYAV ELLSADGVGY HKSCFKCTHC KSRLQLSSYS SMEGVLYCKP
HFEQLFKESG SFNKNFQSPA KSADKSTPEL TRTPSRVAGR FSGTQEKCAT CSKTVYPIEK
VTVESQTYHK SCFKCSHGGC PISPSNYAAL EGILYCKHHF AQLFKEKGSY NHLIKSASIK
RSAAAAVAAG VPAASVPES
