XCT_ARATH
ID XCT_ARATH Reviewed; 337 AA.
AC Q8H110; Q9SKP8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein XAP5 CIRCADIAN TIMEKEEPER;
GN Name=XCT; OrderedLocusNames=At2g21150; ORFNames=F26H11.9;
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=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 FUNCTION, MUTAGENESIS OF 210-VAL--GLN-212, ALTERNATIVE SPLICING,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18515502; DOI=10.1105/tpc.107.056655;
RA Martin-Tryon E.L., Harmer S.L.;
RT "XAP5 CIRCADIAN TIMEKEEPER coordinates light signals for proper timing of
RT photomorphogenesis and the circadian clock in Arabidopsis.";
RL Plant Cell 20:1244-1259(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP 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 [7]
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 -!- FUNCTION: Involved in light regulation of the circadian clock and
CC photomorphogenesis. May play a global role in coordinating growth in
CC response to the light environment. Acts as a light quality sensor
CC directing both negative and positive transcriptional regulation.
CC Inhibits growth in red light but promote growth in blue light. Inhibits
CC clock gene expression in diurnal cycles. Plays no role in the control
CC of flowering time. {ECO:0000269|PubMed:18515502}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18515502}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q8H110-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves stems, flowers, roots,
CC trichomes and hypocotyls. {ECO:0000269|PubMed:18515502}.
CC -!- DEVELOPMENTAL STAGE: Present in nucleus throughout development.
CC {ECO:0000269|PubMed:18515502}.
CC -!- INDUCTION: Post transcriptionally regulated. No circadian-regulation at
CC the mRNA level, but fluctuation of the protein levels, with the highest
CC level found shortly after dawn.
CC -!- DISRUPTION PHENOTYPE: Shortened circadian period. The clock is
CC hypersensitive to red but shows normal responses to blue light. By
CC contrast, inhibition of hypocotyl elongation is hyposensitive to red
CC light but hypersensitive to blue light. {ECO:0000269|PubMed:18515502}.
CC -!- SIMILARITY: Belongs to the FAM50 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD29801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006264; AAD29801.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07128.1; -; Genomic_DNA.
DR EMBL; BT000912; AAN41312.1; -; mRNA.
DR PIR; G84597; G84597.
DR RefSeq; NP_179711.2; NM_127685.4. [Q8H110-1]
DR AlphaFoldDB; Q8H110; -.
DR STRING; 3702.AT2G21150.1; -.
DR iPTMnet; Q8H110; -.
DR PaxDb; Q8H110; -.
DR PRIDE; Q8H110; -.
DR ProteomicsDB; 242468; -. [Q8H110-1]
DR EnsemblPlants; AT2G21150.1; AT2G21150.1; AT2G21150. [Q8H110-1]
DR GeneID; 816650; -.
DR Gramene; AT2G21150.1; AT2G21150.1; AT2G21150. [Q8H110-1]
DR KEGG; ath:AT2G21150; -.
DR Araport; AT2G21150; -.
DR TAIR; locus:2046987; AT2G21150.
DR eggNOG; KOG2894; Eukaryota.
DR HOGENOM; CLU_037985_1_1_1; -.
DR InParanoid; Q8H110; -.
DR OMA; RMRKGST; -.
DR PhylomeDB; Q8H110; -.
DR PRO; PR:Q8H110; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8H110; baseline and differential.
DR Genevisible; Q8H110; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IMP:TAIR.
DR GO; GO:0035196; P:miRNA processing; IMP:TAIR.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:TAIR.
DR GO; GO:0010099; P:regulation of photomorphogenesis; IMP:TAIR.
DR GO; GO:0009637; P:response to blue light; IMP:TAIR.
DR GO; GO:0010114; P:response to red light; IMP:TAIR.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR007005; XAP5.
DR PANTHER; PTHR12722; PTHR12722; 2.
DR Pfam; PF04921; XAP5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Biological rhythms; Coiled coil;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..337
FT /note="Protein XAP5 CIRCADIAN TIMEKEEPER"
FT /id="PRO_0000388466"
FT REGION 23..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..41
FT /evidence="ECO:0000255"
FT COILED 72..121
FT /evidence="ECO:0000255"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MUTAGEN 210..212
FT /note="Missing: In xct-1; shortened circadian period."
FT /evidence="ECO:0000269|PubMed:18515502"
SQ SEQUENCE 337 AA; 39240 MW; B04FF1F7A2280101 CRC64;
MSGMGDGYVG TAQDAVRIRR LQKQREAERK KIQELKSKSA SGNDQSGLLQ FGTSSCEILD
TAFKKETVGL VTREEYVEKR VNIRNKFEEE EKEKLQKLQQ EEEELQLEKR NKKRKIKGSS
RLSFAEDFEN GSDEDDGENK SSGTGNLRCG KLGKDPSVET NFLPDSEREA EEQAERERLK
KQWLREQEQI KNEPLEITYS YWDGTGHRRV IQVRKGDPIG NFLRAVQQQL APDFREIRTA
SVENLLYVKE DLIIPHQHSF YELIINKARG KSGPLFHFDV HEDVRTIADA TIEKDESHAG
KVVERHWYEK NKHIFPASRW EIYDPTKKWE RYTVHGD
