NAI2_ARATH
ID NAI2_ARATH Reviewed; 772 AA.
AC Q9LSB4; F4J1D7; Q712H0;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=TSA1-like protein;
DE AltName: Full=Protein NAI2;
DE Flags: Precursor;
GN Name=NAI2; OrderedLocusNames=At3g15950; ORFNames=MVC8.9;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 [MRNA] OF 286-772.
RA Mahon P.;
RL Thesis (2000), Cambridge University, United Kingdom.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15964904; DOI=10.1093/pcp/pci155;
RA Suzuki T., Nakajima S., Morikami A., Nakamura K.;
RT "An Arabidopsis protein with a novel calcium-binding repeat sequence
RT interacts with TONSOKU/MGOUN3/BRUSHY1 involved in meristem maintenance.";
RL Plant Cell Physiol. 46:1452-1461(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION, LACK OF
RP INTERACTION WITH PYK10, AND DOMAIN.
RC STRAIN=cv. Columbia;
RX PubMed=18780803; DOI=10.1105/tpc.108.059345;
RA Yamada K., Nagano A.J., Nishina M., Hara-Nishimura I., Nishimura M.;
RT "NAI2 is an endoplasmic reticulum body component that enables ER body
RT formation in Arabidopsis thaliana.";
RL Plant Cell 20:2529-2540(2008).
RN [8]
RP FUNCTION.
RX PubMed=19847124; DOI=10.4161/psb.4.9.9377;
RA Yamada K., Nagano A.J., Ogasawara K., Hara-Nishimura I., Nishimura M.;
RT "The ER body, a new organelle in Arabidopsis thaliana, requires NAI2 for
RT its formation and accumulates specific beta-glucosidases.";
RL Plant Signal. Behav. 4:849-852(2009).
RN [9]
RP FUNCTION, AND INTERACTION WITH MEB1 AND MEB2.
RX PubMed=23166355; DOI=10.1104/pp.112.207654;
RA Yamada K., Nagano A.J., Nishina M., Hara-Nishimura I., Nishimura M.;
RT "Identification of two novel endoplasmic reticulum body-specific integral
RT membrane proteins.";
RL Plant Physiol. 161:108-120(2013).
CC -!- FUNCTION: Responsible for the ER body formation. Regulates the number
CC and shape of the ER bodies and the accumulation of PYK10 in ER bodies,
CC but is not involved in the expression of PYK10.
CC {ECO:0000269|PubMed:18780803, ECO:0000269|PubMed:19847124,
CC ECO:0000269|PubMed:23166355}.
CC -!- SUBUNIT: Has no interaction with PYK10 and is not part of the PYK10
CC complex. Interacts directly or indirectly with MEB1 and MEB2.
CC {ECO:0000269|PubMed:23166355}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:18780803}. Note=Located in ER bodies.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LSB4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LSB4-2; Sequence=VSP_056758;
CC -!- TISSUE SPECIFICITY: Expressed in roots. Detected in shoot apex.
CC {ECO:0000269|PubMed:15964904}.
CC -!- INDUCTION: Induced by NAI1. {ECO:0000269|PubMed:18780803}.
CC -!- DOMAIN: Contains a N-terminal NAI2 domain (472-772).
CC {ECO:0000269|PubMed:18780803}.
CC -!- DISRUPTION PHENOTYPE: Loss of ER bodies accumulation in all parts of
CC the seedling and alteration of PYK10 localization.
CC {ECO:0000269|PubMed:18780803}.
CC -!- MISCELLANEOUS: 'Nai' means 'nothing' in Japanese. Homologous proteins
CC are found only in Brassicales plants (PubMed:18780803).
CC {ECO:0000305|PubMed:18780803}.
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DR EMBL; AB026653; BAB02881.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75751.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75752.1; -; Genomic_DNA.
DR EMBL; AY120750; AAM53308.1; -; mRNA.
DR EMBL; BT001207; AAN65094.1; -; mRNA.
DR EMBL; AJ271471; CAC81061.1; -; mRNA.
DR RefSeq; NP_001030708.1; NM_001035631.2. [Q9LSB4-2]
DR RefSeq; NP_188216.2; NM_112465.4. [Q9LSB4-1]
DR AlphaFoldDB; Q9LSB4; -.
DR SMR; Q9LSB4; -.
DR BioGRID; 6173; 6.
DR STRING; 3702.AT3G15950.1; -.
DR MetOSite; Q9LSB4; -.
DR SwissPalm; Q9LSB4; -.
DR PaxDb; Q9LSB4; -.
DR PRIDE; Q9LSB4; -.
DR ProteomicsDB; 251272; -. [Q9LSB4-1]
DR EnsemblPlants; AT3G15950.1; AT3G15950.1; AT3G15950. [Q9LSB4-1]
DR EnsemblPlants; AT3G15950.2; AT3G15950.2; AT3G15950. [Q9LSB4-2]
DR GeneID; 820839; -.
DR Gramene; AT3G15950.1; AT3G15950.1; AT3G15950. [Q9LSB4-1]
DR Gramene; AT3G15950.2; AT3G15950.2; AT3G15950. [Q9LSB4-2]
DR KEGG; ath:AT3G15950; -.
DR Araport; AT3G15950; -.
DR TAIR; locus:2093930; AT3G15950.
DR HOGENOM; CLU_021185_0_0_1; -.
DR InParanoid; Q9LSB4; -.
DR OMA; HAYEEYH; -.
DR OrthoDB; 399814at2759; -.
DR PhylomeDB; Q9LSB4; -.
DR PRO; PR:Q9LSB4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSB4; baseline and differential.
DR Genevisible; Q9LSB4; AT.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0010168; C:ER body; IDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0080119; P:ER body organization; IMP:TAIR.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..772
FT /note="TSA1-like protein"
FT /id="PRO_0000430465"
FT REPEAT 98..138
FT /note="EFE repeat 1"
FT REPEAT 139..176
FT /note="EFE repeat 2"
FT REPEAT 177..213
FT /note="EFE repeat 3"
FT REPEAT 214..251
FT /note="EFE repeat 4"
FT REPEAT 252..292
FT /note="EFE repeat 5"
FT REPEAT 293..330
FT /note="EFE repeat 6"
FT REPEAT 331..368
FT /note="EFE repeat 7"
FT REPEAT 369..407
FT /note="EFE repeat 8"
FT REPEAT 408..439
FT /note="EFE repeat 9"
FT REPEAT 440..472
FT /note="EFE repeat 10"
FT REGION 49..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..472
FT /note="10 X approximate EFE repeat"
FT REGION 465..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..476
FT /evidence="ECO:0000255"
FT COILED 688..748
FT /evidence="ECO:0000255"
FT COMPBIAS 466..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 184..221
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056758"
FT CONFLICT 523
FT /note="S -> P (in Ref. 4; CAC81061)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 85016 MW; 8A2CD740BDA557A6 CRC64;
MGTKFLALGL SLCLVLSSFY QVSCQDEGTG SLSTLDLIEH EYQTSVNSLQ GNEAVDQTET
SGQKNSTVSD NNTISLSLSE EPALETLKES VDTSAELGAV TDEVDKPSSM LDHIELEFEA
HINELKEAGS DGINKVEESK DDEEAARRHK MLEAIEREFE AAHAGFEQLK TDDSAQGLDD
EQSAKRQSML DEIERDFEAA TKGLEQLKAD DLTGINDEEH AAKRQKMLEE IEREFEEATK
GLEELRHSTS STDDEAQSAK RQNMLDEIER EFEAATSGLK ELKINAHTVK DDVDDKEQDA
KRQSMLDAIE REFEAVTESF KQLEDIADNK AEGDDESAKR QSMLDEIERE FEAATNSLKQ
LNLDDFSEGD DSAESARRNS MLEAIEREFE AATKGLEELK ANDSTGDKDD DEHVARRKIM
LEAIEREFEA ATKGLEELKN ESEQAENKRN SMLEAFEREF EAATNAKANG ENSAKNPSTI
STTVQKSSGG YNAGLEGLLK PADGVCGCFN KDKDGLQADT DSSINIAEIL AEESKLQGSG
TSRLTTSLNN LVDTHRKETS SKVGSVLGSS SSVTSTTSES AATSESIESL KQTLRKLRGL
SARDLVNHPN FDAIIAAGTR YEVLSSASIG YISLLAKYKT VIKEGLEASQ RVQIAQTRAK
LLKETAMEKQ RTVDSVFAAA KTTAQRGDAL HIRIVAIKKL LAKLEAEKVD VDSKFTSLTT
SLSELLKEAS QAYEEYHEAV HKAKDEQAAE EFAVETTKRA EHIWVEFLSS LN
