ID   QKIL3_ARATH             Reviewed;         286 AA.
AC   Q9ZVI3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=KH domain-containing protein At2g38610;
DE   AltName: Full=Quaking-like protein 3;
GN   OrderedLocusNames=At2g38610; ORFNames=T6A23.19;
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   GENE FAMILY.
RX   PubMed=11809873; DOI=10.1093/nar/30.3.623;
RA   Lorkovic Z.J., Barta A.;
RT   "Genome analysis: RNA recognition motif (RRM) and K homology (KH) domain
RT   RNA-binding proteins from the flowering plant Arabidopsis thaliana.";
RL   Nucleic Acids Res. 30:623-635(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-273, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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   -!- INTERACTION:
CC       Q9ZVI3; Q9SHZ6: UBA1A; NbExp=3; IntAct=EBI-4440478, EBI-346271;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; AC005499; AAC67357.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09555.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09556.1; -; Genomic_DNA.
DR   EMBL; AY042804; AAK68744.1; -; mRNA.
DR   EMBL; AY064682; AAL47387.1; -; mRNA.
DR   EMBL; AY065112; AAL38288.1; -; mRNA.
DR   EMBL; BT000084; AAN15403.1; -; mRNA.
DR   PIR; B84807; B84807.
DR   RefSeq; NP_181395.1; NM_129418.3.
DR   RefSeq; NP_850296.1; NM_179965.4.
DR   AlphaFoldDB; Q9ZVI3; -.
DR   SMR; Q9ZVI3; -.
DR   BioGRID; 3785; 4.
DR   IntAct; Q9ZVI3; 4.
DR   STRING; 3702.Q9ZVI3; -.
DR   iPTMnet; Q9ZVI3; -.
DR   PaxDb; 3702-AT2G38610-1; -.
DR   ProteomicsDB; 225935; -.
DR   EnsemblPlants; AT2G38610.1; AT2G38610.1; AT2G38610.
DR   EnsemblPlants; AT2G38610.2; AT2G38610.2; AT2G38610.
DR   GeneID; 818443; -.
DR   Gramene; AT2G38610.1; AT2G38610.1; AT2G38610.
DR   Gramene; AT2G38610.2; AT2G38610.2; AT2G38610.
DR   KEGG; ath:AT2G38610; -.
DR   Araport; AT2G38610; -.
DR   TAIR; AT2G38610; -.
DR   eggNOG; KOG1588; Eukaryota.
DR   HOGENOM; CLU_065679_0_1_1; -.
DR   InParanoid; Q9ZVI3; -.
DR   OMA; QMGGMRT; -.
DR   OrthoDB; 1397at2759; -.
DR   PhylomeDB; Q9ZVI3; -.
DR   PRO; PR:Q9ZVI3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZVI3; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   InterPro; IPR045071; BBP-like.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR032377; STAR_dimer.
DR   PANTHER; PTHR11208:SF42; KH DOMAIN-CONTAINING PROTEIN SPIN1; 1.
DR   PANTHER; PTHR11208; RNA-BINDING PROTEIN RELATED; 1.
DR   Pfam; PF16544; STAR_dimer; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   Genevisible; Q9ZVI3; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..286
FT                   /note="KH domain-containing protein At2g38610"
FT                   /id="PRO_0000357030"
FT   DOMAIN          141..208
FT                   /note="KH"
FT   REGION          256..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   286 AA;  31721 MW;  12ABFC0228E6877E CRC64;
     MSGLYNNSSY FSPARAASPQ IRSTPEIDSS QYLTELLAEH QKLTPFMQVL PICSRLLNQE
     MFRVSGMMSN QGFGDFDRLR HRSPSPMASS NLMSNVSNTG LGGWNGLSQE RLSGTPGMTM
     DWQGAPGSPS SYTVKRILRL EIPVDNYPNF NFVGRLLGPR GNSLKRVEAT TGCRVFIRGK
     GSIKDPEKED KLRGRPGYEH LNEQLHILIE ADLPASIVEI RLRQAQEIIE ELLKPVDESQ
     DFIKRQQLRE LALLNSNNLR EESPGPSGGG SVSPFNSSGK RPKTGC
//