WLI2A_ARATH
ID WLI2A_ARATH Reviewed; 200 AA.
AC O04193;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=LIM domain-containing protein WLIM2a {ECO:0000305};
DE AltName: Full=Widely-expressed LIM protein 2 {ECO:0000303|PubMed:11085265};
DE Short=AtWLIM2;
GN Name=WLIN2A {ECO:0000303|PubMed:17573466};
GN Synonyms=WLIM2 {ECO:0000303|PubMed:11085265};
GN OrderedLocusNames=At2g39900 {ECO:0000312|Araport:AT2G39900};
GN ORFNames=T28M21.6 {ECO:0000312|EMBL:AAB95275.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 TISSUE SPECIFICITY.
RX PubMed=11085265; DOI=10.1007/s004380000312;
RA Eliasson A., Gass N., Mundel C., Baltz R., Kraeuter R., Evrard J.L.,
RA Steinmetz A.;
RT "Molecular and expression analysis of a LIM protein gene family from
RT flowering plants.";
RL Mol. Gen. Genet. 264:257-267(2000).
RN [5]
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 [6]
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 -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC siliques. Barely detected in pollen. {ECO:0000269|PubMed:11085265,
CC ECO:0000269|PubMed:20817848}.
CC -!- MISCELLANEOUS: Cross-links actin with a constant of dissociation of 0.4
CC uM. {ECO:0000269|PubMed:20817848}.
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DR EMBL; AF002109; AAB95275.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09747.1; -; Genomic_DNA.
DR EMBL; AY094448; AAM19819.1; -; mRNA.
DR EMBL; AY122901; AAM67434.1; -; mRNA.
DR PIR; G84822; G84822.
DR RefSeq; NP_181519.1; NM_129548.4.
DR AlphaFoldDB; O04193; -.
DR BioGRID; 3915; 5.
DR IntAct; O04193; 5.
DR STRING; 3702.AT2G39900.1; -.
DR iPTMnet; O04193; -.
DR PaxDb; O04193; -.
DR PRIDE; O04193; -.
DR ProteomicsDB; 242767; -.
DR EnsemblPlants; AT2G39900.1; AT2G39900.1; AT2G39900.
DR GeneID; 818577; -.
DR Gramene; AT2G39900.1; AT2G39900.1; AT2G39900.
DR KEGG; ath:AT2G39900; -.
DR Araport; AT2G39900; -.
DR TAIR; locus:2061171; AT2G39900.
DR eggNOG; KOG1700; Eukaryota.
DR HOGENOM; CLU_026811_1_0_1; -.
DR InParanoid; O04193; -.
DR OMA; CRPHFEQ; -.
DR OrthoDB; 1214165at2759; -.
DR PhylomeDB; O04193; -.
DR PRO; PR:O04193; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04193; baseline and differential.
DR Genevisible; O04193; 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: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; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..200
FT /note="LIM domain-containing protein WLIM2a"
FT /id="PRO_0000430593"
FT DOMAIN 8..68
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 107..167
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
SQ SEQUENCE 200 AA; 21901 MW; 81CA8471F94B21DA CRC64;
MSFTGTQQKC RACEKTVYPV ELLSADGISY HKACFKCSHC KSRLQLSNYS SMEGVVYCRP
HFEQLFKESG SFSKNFQSPA KPLTDKPTPE LNRTPSRLAG MFSGTQDKCA TCTKTVYPIE
KVTVESQCYH KSCFKCSHGG CPISPSNYAA LEGILYCKHH FAQLFKEKGS YNHLIKSASI
KRATAAATAA AAAVAAVPES