SKIP_ARATH
ID SKIP_ARATH Reviewed; 613 AA.
AC O80653; F4I5L6; Q67YK1;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=SNW/SKI-interacting protein;
DE Short=AtSKIP;
DE AltName: Full=Protein EARLY FLOWERING AND INSENSITIVE TO PHOTOPERIOD 1;
DE AltName: Full=SNW domain-containing protein;
GN Name=SKIP; Synonyms=EIP1; OrderedLocusNames=At1g77180; ORFNames=T14N5.5;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-243, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY ABIOTIC STRESS AND ABSCISIC
RP ACID, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19765229; DOI=10.1111/j.1469-8137.2009.03032.x;
RA Lim G.H., Zhang X., Chung M.S., Lee D.J., Woo Y.M., Cheong H.S., Kim C.S.;
RT "A putative novel transcription factor, AtSKIP, is involved in abscisic
RT acid signalling and confers salt and osmotic tolerance in Arabidopsis.";
RL New Phytol. 185:103-113(2010).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, AND INTERACTION WITH SR45.
RX PubMed=22942380; DOI=10.1105/tpc.112.100081;
RA Wang X., Wu F., Xie Q., Wang H., Wang Y., Yue Y., Gahura O., Ma S., Liu L.,
RA Cao Y., Jiao Y., Puta F., McClung C.R., Xu X., Ma L.;
RT "SKIP is a component of the spliceosome linking alternative splicing and
RT the circadian clock in Arabidopsis.";
RL Plant Cell 24:3278-3295(2012).
CC -!- FUNCTION: Splicing factor involved in post-transcriptional regulation
CC of circadian clock and flowering time genes. Associates with the pre-
CC mRNA of PRR7, PRR9, ELF3 and GI, and is necessary for the regulation of
CC their alternative splicing and mRNA maturation. Probably involved in
CC splice site recognition. {ECO:0000269|PubMed:19765229,
CC ECO:0000269|PubMed:22942380}.
CC -!- SUBUNIT: Component of the spliceosome. Interacts with SR45.
CC {ECO:0000269|PubMed:22942380}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19765229,
CC ECO:0000269|PubMed:22942380}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O80653-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O80653-2; Sequence=VSP_053506;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, seedlings, siliques,
CC cotyledons, leaves, inflorescences, seeds and shoot apical meristem.
CC {ECO:0000269|PubMed:19765229, ECO:0000269|PubMed:22942380}.
CC -!- DEVELOPMENTAL STAGE: Expressed in every developmental stage. Up-
CC regulated by senescence. {ECO:0000269|PubMed:19765229}.
CC -!- INDUCTION: Expressed constitutively. Up-regulated by abiotic stress and
CC abscisic acid. {ECO:0000269|PubMed:19765229,
CC ECO:0000269|PubMed:22942380}.
CC -!- DISRUPTION PHENOTYPE: Longer circadian period. Severely dwarfed and
CC infertile when homozygous. {ECO:0000269|PubMed:22942380}.
CC -!- SIMILARITY: Belongs to the SNW family. {ECO:0000305}.
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DR EMBL; AC004260; AAC34351.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35945.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35946.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35947.1; -; Genomic_DNA.
DR EMBL; AF386950; AAK62395.1; -; mRNA.
DR EMBL; AY058079; AAL24187.1; -; mRNA.
DR EMBL; AY081520; AAM10082.1; -; mRNA.
DR EMBL; AK175914; BAD43677.1; -; mRNA.
DR EMBL; AK176196; BAD43959.1; -; mRNA.
DR EMBL; AK176338; BAD44101.1; -; mRNA.
DR EMBL; AK176413; BAD44176.1; -; mRNA.
DR EMBL; AK176837; BAD44600.1; -; mRNA.
DR EMBL; AK221263; BAD93926.1; -; mRNA.
DR EMBL; AK176467; BAD44230.1; -; mRNA.
DR PIR; T00448; T00448.
DR RefSeq; NP_001031291.1; NM_001036214.3. [O80653-1]
DR RefSeq; NP_001185416.1; NM_001198487.1. [O80653-2]
DR RefSeq; NP_565151.1; NM_106368.5. [O80653-1]
DR AlphaFoldDB; O80653; -.
DR SMR; O80653; -.
DR BioGRID; 29274; 7.
DR IntAct; O80653; 3.
DR STRING; 3702.AT1G77180.2; -.
DR iPTMnet; O80653; -.
DR PaxDb; O80653; -.
DR PRIDE; O80653; -.
DR ProteomicsDB; 234570; -. [O80653-1]
DR EnsemblPlants; AT1G77180.1; AT1G77180.1; AT1G77180. [O80653-1]
DR EnsemblPlants; AT1G77180.2; AT1G77180.2; AT1G77180. [O80653-1]
DR EnsemblPlants; AT1G77180.3; AT1G77180.3; AT1G77180. [O80653-2]
DR GeneID; 844055; -.
DR Gramene; AT1G77180.1; AT1G77180.1; AT1G77180. [O80653-1]
DR Gramene; AT1G77180.2; AT1G77180.2; AT1G77180. [O80653-1]
DR Gramene; AT1G77180.3; AT1G77180.3; AT1G77180. [O80653-2]
DR KEGG; ath:AT1G77180; -.
DR Araport; AT1G77180; -.
DR TAIR; locus:2195970; AT1G77180.
DR eggNOG; KOG2441; Eukaryota.
DR HOGENOM; CLU_006601_2_1_1; -.
DR InParanoid; O80653; -.
DR OMA; WRDSNTL; -.
DR OrthoDB; 1455730at2759; -.
DR PhylomeDB; O80653; -.
DR PRO; PR:O80653; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80653; baseline and differential.
DR Genevisible; O80653; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0036002; F:pre-mRNA binding; IPI:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IPI:TAIR.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IEA:EnsemblPlants.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IEA:EnsemblPlants.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0042752; P:regulation of circadian rhythm; IGI:TAIR.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0010555; P:response to mannitol; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR InterPro; IPR017862; SKI-int_prot_SKIP.
DR InterPro; IPR004015; SKI-int_prot_SKIP_SNW-dom.
DR PANTHER; PTHR12096; PTHR12096; 1.
DR Pfam; PF02731; SKIP_SNW; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Coiled coil; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Transcription; Transcription regulation.
FT CHAIN 1..613
FT /note="SNW/SKI-interacting protein"
FT /id="PRO_0000424790"
FT REGION 186..350
FT /note="SNW"
FT REGION 219..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..170
FT /evidence="ECO:0000255"
FT COILED 318..349
FT /evidence="ECO:0000255"
FT COILED 391..421
FT /evidence="ECO:0000255"
FT COMPBIAS 315..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT VAR_SEQ 453..554
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053506"
FT CONFLICT 395
FT /note="E -> G (in Ref. 4; BAD44230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 69423 MW; 84414C45298FF844 CRC64;
MKSLNDLPAP KSTTTTYYDH SNDAWFKNRV TESETVKSSS IKFKVVPAYL NRQGLRPKNP
EDFGDGGAFP EIHLPQYPLL MGKNKSNKPG AKTLPVTVDA QGNVVFDAIV RQNENSRKIV
YSQHKDIIPK FLKNEGDLGT VVDEEEELQK EIQETAEETK AAIEKIVNVR LSAAQPSNIA
RQSGDSQYIK YKPSQQSSAF NSGAKERIIR MVEMPVDPLD PPKFKHKRVP RASGSPPVPV
MHSPPRPVTV KDQQDWKIPP CISNWKNPKG YTIPLDKRLA ADGRGLQDVQ INDNFAKLSE
ALYVAEQKAR EAVSMRSKVQ KEMVMKDKER KEQELRALAQ KARSERTGAA MSMPVSSDRG
RSESVDPRGD YDNYDQDRGR EREREEPQET REEREKRIQR EKIREERRRE RERERRLDAK
DAAMGKKSKI TRDRDRDISE KVALGMASTG GKGGGEVMYD QRLFNQDKGM DSGFAADDQY
NLYDKGLFTA QPTLSTLYKP KKDNDEEMYG NADEQLDKIK NTERFKPDKA FTGASERVGS
KRDRPVEFEK EEEQDPFGLE KWVSDLKKGK KPLDKIGSGG TMRASGGGGS SSRDDDHGGS
GRTKINFERS DRR
