LSH2_ARATH
ID LSH2_ARATH Reviewed; 201 AA.
AC Q9M836;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 2;
DE AltName: Full=Protein ORGAN BOUNDARY 3;
GN Name=LSH2; Synonyms=OBO3; OrderedLocusNames=At3g04510; ORFNames=T27C4.16;
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].
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=14871309; DOI=10.1111/j.1365-313x.2003.01993.x;
RA Zhao L., Nakazawa M., Takase T., Manabe K., Kobayashi M., Seki M.,
RA Shinozaki K., Matsui M.;
RT "Overexpression of LSH1, a member of an uncharacterised gene family, causes
RT enhanced light regulation of seedling development.";
RL Plant J. 37:694-706(2004).
RN [6]
RP GENE FAMILY.
RX PubMed=21245300; DOI=10.1073/pnas.1018542108;
RA Cho E., Zambryski P.C.;
RT "Organ boundary1 defines a gene expressed at the junction between the shoot
RT apical meristem and lateral organs.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2154-2159(2011).
RN [7]
RP DNA-BINDING, AND GENE FAMILY.
RX PubMed=23146749; DOI=10.1186/1745-6150-7-39;
RA Iyer L.M., Aravind L.;
RT "ALOG domains: provenance of plant homeotic and developmental regulators
RT from the DNA-binding domain of a novel class of DIRS1-type retroposons.";
RL Biol. Direct 7:39-39(2012).
CC -!- FUNCTION: Probable transcription regulator that acts as a developmental
CC regulator by promoting cell growth in response to light. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plant homeotic and developmental regulators
CC ALOG protein family. {ECO:0000305}.
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DR EMBL; AC022287; AAF63782.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74090.1; -; Genomic_DNA.
DR EMBL; AY630774; AAT67573.1; -; mRNA.
DR EMBL; AY924763; AAX23838.1; -; Genomic_DNA.
DR RefSeq; NP_187101.1; NM_111322.3.
DR AlphaFoldDB; Q9M836; -.
DR STRING; 3702.AT3G04510.1; -.
DR PaxDb; Q9M836; -.
DR PRIDE; Q9M836; -.
DR ProteomicsDB; 238500; -.
DR EnsemblPlants; AT3G04510.1; AT3G04510.1; AT3G04510.
DR GeneID; 819607; -.
DR Gramene; AT3G04510.1; AT3G04510.1; AT3G04510.
DR KEGG; ath:AT3G04510; -.
DR Araport; AT3G04510; -.
DR TAIR; locus:2100850; AT3G04510.
DR eggNOG; ENOG502QSQJ; Eukaryota.
DR HOGENOM; CLU_071168_1_1_1; -.
DR InParanoid; Q9M836; -.
DR OMA; VASPMIT; -.
DR OrthoDB; 1441744at2759; -.
DR PhylomeDB; Q9M836; -.
DR PRO; PR:Q9M836; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M836; baseline and differential.
DR Genevisible; Q9M836; AT.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009299; P:mRNA transcription; ISS:UniProtKB.
DR GO; GO:0090698; P:post-embryonic plant morphogenesis; ISS:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR InterPro; IPR040222; ALOG.
DR InterPro; IPR006936; ALOG_dom.
DR PANTHER; PTHR31165; PTHR31165; 1.
DR Pfam; PF04852; DUF640; 1.
DR PROSITE; PS51697; ALOG; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..201
FT /note="Protein LIGHT-DEPENDENT SHORT HYPOCOTYLS 2"
FT /id="PRO_0000425289"
FT DOMAIN 33..160
FT /note="ALOG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01033"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 158..162
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 22774 MW; 4CE7B08E12CCAC17 CRC64;
MDLISQNHNN RNPNTSLSTQ TPSSFSSPPS SSRYENQKRR DWNTFCQYLR NHHPPLSLAS
CSGAHVLDFL RYLDQFGKTK VHHQNCAFFG LPNPPAPCPC PLRQAWGSLD ALIGRLRAAY
EENGGAPETS PFGSRSVRIF LREVRDFQAK SRGVSYEKKR KRVNNKQITQ SQPQSQPPLP
QQPQQEQGQS MMANYHHGAT Q
