WLIM1_ARATH
ID WLIM1_ARATH Reviewed; 190 AA.
AC Q94JX5; Q9SY62;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=LIM domain-containing protein WLIM1 {ECO:0000305};
DE AltName: Full=Widely-expressed LIM protein 1 {ECO:0000303|PubMed:11085265};
DE Short=AtWLIM1;
GN Name=WLIM1 {ECO:0000303|PubMed:11085265, ECO:0000303|PubMed:17573466};
GN OrderedLocusNames=At1g10200 {ECO:0000312|Araport:AT1G10200};
GN ORFNames=F14N23.8 {ECO:0000312|EMBL:AAD32870.1};
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 {ECO:0000312|EMBL:AAK49575.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 [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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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. Not 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD32870.1; Type=Erroneous gene model prediction;
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DR EMBL; AC005489; AAD32870.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28552.1; -; Genomic_DNA.
DR EMBL; AF370569; AAK49575.1; -; mRNA.
DR EMBL; AY085377; AAM62606.1; -; mRNA.
DR RefSeq; NP_172491.1; NM_100894.4.
DR AlphaFoldDB; Q94JX5; -.
DR BioGRID; 22798; 8.
DR IntAct; Q94JX5; 6.
DR STRING; 3702.AT1G10200.1; -.
DR iPTMnet; Q94JX5; -.
DR MetOSite; Q94JX5; -.
DR PaxDb; Q94JX5; -.
DR PRIDE; Q94JX5; -.
DR ProteomicsDB; 242720; -.
DR EnsemblPlants; AT1G10200.1; AT1G10200.1; AT1G10200.
DR GeneID; 837558; -.
DR Gramene; AT1G10200.1; AT1G10200.1; AT1G10200.
DR KEGG; ath:AT1G10200; -.
DR Araport; AT1G10200; -.
DR TAIR; locus:2012798; AT1G10200.
DR eggNOG; KOG1700; Eukaryota.
DR HOGENOM; CLU_026811_1_0_1; -.
DR InParanoid; Q94JX5; -.
DR OMA; HHSMASK; -.
DR OrthoDB; 1214165at2759; -.
DR PhylomeDB; Q94JX5; -.
DR PRO; PR:Q94JX5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94JX5; baseline and differential.
DR Genevisible; Q94JX5; 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 Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; LIM domain;
KW Metal-binding; Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..190
FT /note="LIM domain-containing protein WLIM1"
FT /id="PRO_0000430592"
FT DOMAIN 8..68
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 108..168
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 74..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 190 AA; 21040 MW; 6D8DE2172BAC17E7 CRC64;
MAFAGTTQKC MACDKTVYLV DKLTADNRVY HKACFRCHHC KGTLKLSNYN SFEGVLYCRP
HFDQNFKRTG SLEKSFEGTP KIGKPDRPLE GERPAGTKVS NMFGGTREKC VGCDKTVYPI
EKVSVNGTLY HKSCFKCTHG GCTISPSNYI AHEGKLYCKH HHIQLIKEKG NLSQLEGGGE
NAAKDKVVAA
