LNG2_ARATH
ID LNG2_ARATH Reviewed; 905 AA.
AC Q9S823; Q8LD57; Q940B7;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Protein LONGIFOLIA 2;
DE AltName: Full=Protein TON1 RECRUITING MOTIF 1;
GN Name=LNG2; Synonyms=TRM1; OrderedLocusNames=At3g02170;
GN ORFNames=F14P3.18, F1C9.4;
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=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 448-905.
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17038516; DOI=10.1242/dev.02604;
RA Lee Y.K., Kim G.T., Kim I.J., Park J., Kwak S.S., Choi G., Chung W.I.;
RT "LONGIFOLIA1 and LONGIFOLIA2, two homologous genes, regulate longitudinal
RT cell elongation in Arabidopsis.";
RL Development 133:4305-4314(2006).
RN [6]
RP FUNCTION, INTERACTION WITH TON1A AND TON1B, AND SUBCELLULAR LOCATION.
RX PubMed=22286137; DOI=10.1105/tpc.111.089748;
RA Drevensek S., Goussot M., Duroc Y., Christodoulidou A., Steyaert S.,
RA Schaefer E., Duvernois E., Grandjean O., Vantard M., Bouchez D.,
RA Pastuglia M.;
RT "The Arabidopsis TRM1-TON1 interaction reveals a recruitment network common
RT to plant cortical microtubule arrays and eukaryotic centrosomes.";
RL Plant Cell 24:178-191(2012).
CC -!- FUNCTION: In association with LNG1, regulates leaf morphology by
CC promoting longitudinal polar cell elongation independently of ROT3.
CC Associates with microtubules and recruits TON1A and TON1B to the
CC cytoskeleton through its C-terminus. {ECO:0000269|PubMed:17038516,
CC ECO:0000269|PubMed:22286137}.
CC -!- SUBUNIT: Interacts (via C-terminus) with TON1A and TON1B.
CC {ECO:0000269|PubMed:22286137}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22286137}. Note=Localizes to cortical microtubules
CC arrays.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the lng1 and lng2 double mutant shows reduced length of
CC cotyledons, rosette leaves, siliques and flowers.
CC {ECO:0000269|PubMed:17038516}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM64269.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009755; AAF02120.1; -; Genomic_DNA.
DR EMBL; AC011664; AAF14821.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73772.1; -; Genomic_DNA.
DR EMBL; AY056131; AAL07210.1; -; mRNA.
DR EMBL; AY150501; AAN13017.1; -; mRNA.
DR EMBL; AY086190; AAM64269.1; ALT_INIT; mRNA.
DR RefSeq; NP_566165.2; NM_111084.4.
DR AlphaFoldDB; Q9S823; -.
DR BioGRID; 6612; 1.
DR STRING; 3702.AT3G02170.1; -.
DR iPTMnet; Q9S823; -.
DR PaxDb; Q9S823; -.
DR PRIDE; Q9S823; -.
DR ProteomicsDB; 238451; -.
DR EnsemblPlants; AT3G02170.1; AT3G02170.1; AT3G02170.
DR GeneID; 821279; -.
DR Gramene; AT3G02170.1; AT3G02170.1; AT3G02170.
DR KEGG; ath:AT3G02170; -.
DR Araport; AT3G02170; -.
DR TAIR; locus:2076557; AT3G02170.
DR eggNOG; ENOG502R7XZ; Eukaryota.
DR HOGENOM; CLU_007647_0_0_1; -.
DR InParanoid; Q9S823; -.
DR OMA; PRFSCDD; -.
DR OrthoDB; 185064at2759; -.
DR PhylomeDB; Q9S823; -.
DR PRO; PR:Q9S823; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S823; baseline and differential.
DR Genevisible; Q9S823; AT.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0051513; P:regulation of monopolar cell growth; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IGI:TAIR.
DR InterPro; IPR025486; DUF4378.
DR InterPro; IPR033334; LNG1/2.
DR PANTHER; PTHR31680; PTHR31680; 1.
DR Pfam; PF14309; DUF4378; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..905
FT /note="Protein LONGIFOLIA 2"
FT /id="PRO_0000420919"
FT REGION 42..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 268
FT /note="S -> Y (in Ref. 3; AAL07210)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="E -> K (in Ref. 4; AAM64269)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="R -> S (in Ref. 4; AAM64269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 905 AA; 101628 MW; 134FEE48F551BE76 CRC64;
MSAKLLYNLS DENPNLNKQF GCMNGIFQVF YRQHCPATPV TVSGGAEKSL PPGERRGSVG
ETNMESDKET ERSSTKKKKS AAKEKHRVSF ESSSRPSFSS SPRSSSFSSA EVSTTASQFD
QPGENLIREQ PNGGLMMPYD LKELVKGSIN REIRTRGEEA SFTQQQQPIS ARSSMLLLKE
SSLRSPCRSS NEWNEGRGAA MKFKESHRLS YDEREMRNNG FRVGSKLKET PRLSLDSRSN
SFRSPRADAA RSSCPEEPAT MTHRRSSSSV VAKLMGLEVI ADNSDTEQRR ENRFCDSPRP
MSRVEPTALQ RSRSVDSIKR IPASAASKFP MEPAPWKQMK AGDSALTVYG EIQKRLTQLE
FKKSGKDLRA LKQILEAMEK TQQLIDESRD DGTLSTTTLM QRTHKPVSAA TSPARNFKSS
SIVVMKSAAP VSTSPLPQNV TLPNVKVGNS RQTRKVTSGK QNAMDLTPRP GLYKGQLDST
KSNSPKTVRS RQALAADAGS MTKSGRSQQH SVSPRTQPKK LGFEKQTRPT TPKSEPGKRQ
LGRQQTEVAS PRRKQMIKPH STLQQPDDRL SDARSDLRSL RSDSNISLGS NVDIEVTSRH
RLERNCDFPE QHTPKQRSPD FGIKQDRPSL KPLKVTVEQP SPVSVLDAVF DEEDSPSPVR
KISLSFKEED ALRSEESEWI NKPTSFCRSV PFPQSNRGPM KPSSDHFECS PEEGADFKSG
NHKYILEILL ASGILRDLEY SMISFQLHQT RLPINPGLFF ILEQNKASNV TLPDNKHRGR
GFRQQQTNPT ETIRRKLVFD TVNEILARKF TAEGCIKPRL IANPLKKLEK ISKEEQLLQT
LCSEIDRLQQ NNSNCILEDD EEDIIWEDLQ SQSMNLKEFE GETPGIVLDI ERMIFRDLVN
EVCFC
