ID   SPA2_ARATH              Reviewed;        1036 AA.
AC   Q9T014; O82506; O82507; Q0WP97;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Protein SPA1-RELATED 2;
GN   Name=SPA2; OrderedLocusNames=At4g11110;
GN   ORFNames=F2P3.13, F2P3.14, T22B4.90;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(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;
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12887588; DOI=10.1046/j.1365-313x.2003.01813.x;
RA   Laubinger S., Hoecker U.;
RT   "The SPA1-like proteins SPA3 and SPA4 repress photomorphogenesis in the
RT   light.";
RL   Plant J. 35:373-385(2003).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH COP1, GENE FAMILY, AND
RP   NOMENCLATURE.
RX   PubMed=15308756; DOI=10.1105/tpc.104.024216;
RA   Laubinger S., Fittinghoff K., Hoecker U.;
RT   "The SPA quartet: a family of WD-repeat proteins with a central role in
RT   suppression of photomorphogenesis in Arabidopsis.";
RL   Plant Cell 16:2293-2306(2004).
RN   [6]
RP   FUNCTION, AND INDUCTION BY LIGHT.
RX   PubMed=16813571; DOI=10.1111/j.1365-313x.2006.02812.x;
RA   Fittinghoff K., Laubinger S., Nixdorf M., Fackendahl P., Baumgardt R.-L.,
RA   Batschauer A., Hoecker U.;
RT   "Functional and expression analysis of Arabidopsis SPA genes during
RT   seedling photomorphogenesis and adult growth.";
RL   Plant J. 47:577-590(2006).
RN   [7]
RP   FUNCTION, INTERACTION WITH CO, AND INDUCTION.
RX   PubMed=16854975; DOI=10.1242/dev.02481;
RA   Laubinger S., Marchal V., Le Gourrierec J., Wenkel S., Adrian J., Jang S.,
RA   Kulajta C., Braun H., Coupland G., Hoecker U.;
RT   "Arabidopsis SPA proteins regulate photoperiodic flowering and interact
RT   with the floral inducer CONSTANS to regulate its stability.";
RL   Development 133:3213-3222(2006).
RN   [8]
RP   DWD MOTIF.
RX   PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA   Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA   He Y.J., Xiong Y., Deng X.W.;
RT   "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT   substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL   Plant Cell 20:152-167(2008).
CC   -!- FUNCTION: Involved in suppression of photomorphogenesis in dark-grown
CC       seedlings. Probably part of the COP1/SPA E3 ubiquitin-protein ligase
CC       complex. {ECO:0000269|PubMed:15308756, ECO:0000269|PubMed:16813571,
CC       ECO:0000269|PubMed:16854975}.
CC   -!- SUBUNIT: Interacts with CO and COP1. {ECO:0000269|PubMed:15308756,
CC       ECO:0000269|PubMed:16854975}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15308756}.
CC   -!- INDUCTION: Not induced by red, far-red or blue light.
CC       {ECO:0000269|PubMed:16813571, ECO:0000269|PubMed:16854975}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive. The DWD box is required for interaction with DDB1A (By
CC       similarity). {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC35546.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAC35547.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF01052.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAB43046.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB81212.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF080120; AAC35546.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF080120; AAC35547.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL049876; CAB43046.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161531; CAB81212.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82974.1; -; Genomic_DNA.
DR   EMBL; AK229182; BAF01052.1; ALT_INIT; mRNA.
DR   PIR; T01922; T01922.
DR   PIR; T01923; T01923.
DR   PIR; T08190; T08190.
DR   RefSeq; NP_192849.4; NM_117181.4.
DR   AlphaFoldDB; Q9T014; -.
DR   SMR; Q9T014; -.
DR   BioGRID; 12011; 12.
DR   IntAct; Q9T014; 1.
DR   STRING; 3702.AT4G11110.1; -.
DR   iPTMnet; Q9T014; -.
DR   PaxDb; Q9T014; -.
DR   PRIDE; Q9T014; -.
DR   ProteomicsDB; 232521; -.
DR   EnsemblPlants; AT4G11110.1; AT4G11110.1; AT4G11110.
DR   GeneID; 826712; -.
DR   Gramene; AT4G11110.1; AT4G11110.1; AT4G11110.
DR   KEGG; ath:AT4G11110; -.
DR   Araport; AT4G11110; -.
DR   TAIR; locus:2136133; AT4G11110.
DR   eggNOG; KOG1033; Eukaryota.
DR   HOGENOM; CLU_006994_1_1_1; -.
DR   InParanoid; Q9T014; -.
DR   OMA; NTSAPWC; -.
DR   OrthoDB; 857220at2759; -.
DR   PhylomeDB; Q9T014; -.
DR   PRO; PR:Q9T014; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9T014; baseline and differential.
DR   Genevisible; Q9T014; AT.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0009640; P:photomorphogenesis; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR044630; SPA1/2/3/4.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR44218; PTHR44218; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Nucleotide-binding; Nucleus; Phytochrome signaling pathway;
KW   Reference proteome; Repeat; Transferase; Ubl conjugation pathway;
KW   WD repeat.
FT   CHAIN           1..1036
FT                   /note="Protein SPA1-RELATED 2"
FT                   /id="PRO_0000363492"
FT   DOMAIN          200..550
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          721..760
FT                   /note="WD 1"
FT   REPEAT          770..810
FT                   /note="WD 2"
FT   REPEAT          813..855
FT                   /note="WD 3"
FT   REPEAT          857..895
FT                   /note="WD 4"
FT   REPEAT          899..937
FT                   /note="WD 5"
FT   REPEAT          948..987
FT                   /note="WD 6"
FT   REPEAT          1004..1036
FT                   /note="WD 7"
FT   COILED          587..611
FT                   /evidence="ECO:0000255"
FT   MOTIF           915..930
FT                   /note="DWD box"
SQ   SEQUENCE   1036 AA;  115006 MW;  AB325211D6228E0A CRC64;
     MMDEGSVGDV SRIDEADVAH LQFKNSEQSF KPENIEVREV KEVQVQREAG SPDCSYGVIA
     DFLDGKNGGD HVELIGNEPC SSRQNTNDEG DVVEELTVKT CEGSSMAIVG RPSSRARLEM
     NRSQFLHRFP LDGDLPGSSS MSKKVIDRGT VSILRNAGKM SLPETSNGQL AIIAVNGEAN
     EHLTNVERNP VPVEALSHEG IKTKMLSQSG FSQFFVRKTL KGKGVTFRGP PNNRSKARNM
     DQQTVASSGS ALVIANTSAK ISSSIPLAAY DGLPCLPSNT SKPSSCANPS DTHRGCGGEG
     LSLREWLKSE RQEVNKAECM YIFRQIVDHV DCSHSQGVVL CDLRPSSFKI FKENAVKYVV
     SGSQRESFDS NMNKETLSQL ENPLVRRRLG DTSSLSIPAK KQKSSGPSSR QWPMFQRAGG
     VNIQTENNDG AIQEFHFRSS QPHCSTVACP FTSVSEQLEE KWYASPEELR GDMRSASSNI
     YSLGILLYEL LSQFQCERAR EAAMSDIRHR ILPPKFLSEN PKEAGFCLWL LHPESSCRPS
     TRDILQSEVV NGIPDLYAEG LSLSIEQEDT ESELLQHFLF LSQEKRQKHA GNLMEEIASV
     EADIEEIVKR RCAIGPPSLE EASSSSPASS VPEMRLIRNI NQLESAYFAA RIDAHLPEAR
     YRLRPDRDLL RNSDNTVAEV ENSETWSSDD RVGAFFDGLC KYARYSKFET RGVLRTSELN
     NTSNVICSLG FDRDEDYFAT AGVSKKIKIY EFNSLFNESV DIHYPAIEMP NRSKLSGVCW
     NNYIRNYLAS SDYDGIVKLW DVTTGQAISH FIEHEKRAWS VDFSEACPTK LASGSDDCSV
     KLWNINERNC LGTIRNIANV CCVQFSPQSS HLLAFGSSDF RTYCYDLRNL RTPWCILSGH
     NKAVSYAKFL DNETLVTAST DNTLKLWDLK KTTHGGLSTN ACSLTFGGHT NEKNFVGLST
     SDGYIACGSE TNEVYAYHRS LPMPITSYKF GSIDPISGKE IEEDNNLFVS SVCWRKRSNM
     VVSASSNGSI KVLQLV