SPA3_ARATH
ID SPA3_ARATH Reviewed; 845 AA.
AC Q9LJR3; F4IYP4; F4ZN82; F4ZN83;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein SPA1-RELATED 3;
GN Name=SPA3; OrderedLocusNames=At3g15354; ORFNames=K7L4.16;
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 [MRNA] (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING.
RX PubMed=21511871; DOI=10.1101/gad.2025011;
RA Liu B., Zuo Z., Liu H., Liu X., Lin C.;
RT "Arabidopsis cryptochrome 1 interacts with SPA1 to suppress COP1 activity
RT in response to blue light.";
RL Genes Dev. 25:1029-1034(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [3]
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 [4]
RP FUNCTION, INTERACTION WITH COP1, 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 GENE FAMILY, AND 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: Repressor of photomorphogenesis in the light. Probably part
CC of the COP1/SPA E3 ubiquitin-protein ligase complex.
CC {ECO:0000269|PubMed:12887588, ECO:0000269|PubMed:16813571,
CC ECO:0000269|PubMed:16854975}.
CC -!- SUBUNIT: Interacts with COP1 and CO. {ECO:0000269|PubMed:12887588,
CC ECO:0000269|PubMed:16854975}.
CC -!- INTERACTION:
CC Q9LJR3; O50055: COL1; NbExp=7; IntAct=EBI-626921, EBI-1112154;
CC Q9LJR3; P43254: COP1; NbExp=7; IntAct=EBI-626921, EBI-301649;
CC Q9LJR3; Q9SYX2: SPA1; NbExp=7; IntAct=EBI-626921, EBI-626992;
CC Q9LJR3; Q9LJR3: SPA3; NbExp=2; IntAct=EBI-626921, EBI-626921;
CC Q9LJR3; Q94BM7: SPA4; NbExp=6; IntAct=EBI-626921, EBI-626943;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LJR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LJR3-2; Sequence=VSP_042150, VSP_042151;
CC -!- INDUCTION: Up-regulated by red, far-red and 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=AEE75647.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HQ228994; AEC32932.1; -; mRNA.
DR EMBL; HQ228995; AEC32933.1; -; mRNA.
DR EMBL; AP000413; BAB02165.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75647.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; ANM65673.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65674.1; -; Genomic_DNA.
DR RefSeq; NP_001327623.1; NM_001338161.1. [Q9LJR3-2]
DR RefSeq; NP_001327624.1; NM_001338162.1. [Q9LJR3-1]
DR RefSeq; NP_683567.1; NM_148725.4.
DR AlphaFoldDB; Q9LJR3; -.
DR SMR; Q9LJR3; -.
DR BioGRID; 6101; 11.
DR IntAct; Q9LJR3; 4.
DR STRING; 3702.AT3G15354.1; -.
DR iPTMnet; Q9LJR3; -.
DR PaxDb; Q9LJR3; -.
DR PRIDE; Q9LJR3; -.
DR ProteomicsDB; 245333; -. [Q9LJR3-1]
DR EnsemblPlants; AT3G15354.2; AT3G15354.2; AT3G15354. [Q9LJR3-2]
DR EnsemblPlants; AT3G15354.3; AT3G15354.3; AT3G15354. [Q9LJR3-1]
DR GeneID; 820767; -.
DR Gramene; AT3G15354.2; AT3G15354.2; AT3G15354. [Q9LJR3-2]
DR Gramene; AT3G15354.3; AT3G15354.3; AT3G15354. [Q9LJR3-1]
DR KEGG; ath:AT3G15354; -.
DR Araport; AT3G15354; -.
DR eggNOG; KOG1033; Eukaryota.
DR HOGENOM; CLU_006994_1_1_1; -.
DR InParanoid; Q9LJR3; -.
DR OrthoDB; 857220at2759; -.
DR PhylomeDB; Q9LJR3; -.
DR PRO; PR:Q9LJR3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LJR3; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; SM00220; S_TKc; 1.
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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Nucleotide-binding; Nucleus;
KW Phytochrome signaling pathway; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..845
FT /note="Protein SPA1-RELATED 3"
FT /id="PRO_0000363493"
FT DOMAIN 1..297
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 532..571
FT /note="WD 1"
FT REPEAT 581..621
FT /note="WD 2"
FT REPEAT 624..664
FT /note="WD 3"
FT REPEAT 666..706
FT /note="WD 4"
FT REPEAT 710..748
FT /note="WD 5"
FT REPEAT 757..796
FT /note="WD 6"
FT REPEAT 812..845
FT /note="WD 7"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..329
FT /evidence="ECO:0000255"
FT MOTIF 685..699
FT /note="DWD box"
FT VAR_SEQ 659..662
FT /note="GVSI -> AILI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:21511871"
FT /id="VSP_042150"
FT VAR_SEQ 663..845
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:21511871"
FT /id="VSP_042151"
SQ SEQUENCE 845 AA; 94354 MW; EB5AADEDFD16F316 CRC64;
MEGSSNSNSR GFNTSGVSDR NTEFLPVERL TTRSKPSSHV DEYVRSLFGS TSTHKSGEDD
SLGIDPFVRS LEWGDVSLRQ WLDKPERSVD VFECLHVFRQ IVEIVNAAHS QGIVVHNVRP
SCFVMSSFNH VSFIESASCS DSGSDSLEDG PISQKEIGSS RREEAVSKAI AIEEKGVYNK
LLERKIEKLE EEKTQPFPMK HILAMETSWY TSPEEDFGSS STCASDVYRL GVLLFELFCP
VPSREEKSRT MSSLRHRVLP PQILLKCPKE ASFCLWLLHP EPTCRPSMSD LLQSEFITEP
RDNLEEREAA IELRDRIEEQ ESLLEFLLLI QQRKQESAYR LQDTVSLLSS DIEQVVKRQL
ILKKRGSSLS DFSKDDHQYT SGQPLMSFQA NEEPSAFLAS RKRVRQGILA LENGVEVDEE
SQGSTLLESS RLMRNFKKLE SVYFLTRRRQ MKAAASGKSL TRHSPLSSEN GRGSMIVSEK
SSVSNPVAPK AFFNNDSRQG GWIDPFLEGL CRYLSFSQLR VKADLKQGDL LNSSNLVCAL
AFDREGELFA TAGVNKKIKI FECNSIVNDN RDIHYPVVEL AGRSKLSSLC WNSYIKSQIA
SSNFDGVVQI WDVARSQLVT EMKEHKKRVW SIDISSADPT LLASGSDDGT VKLWSINQGV
SIGTIKTKAN VCCVQFPSDS GRSLAFGSAD HKVYYYDLRN PKIPLCTMIG HSKTVSYVKF
VDSSTLVSSS TDNTLKLWDL SMSASGINES PLHSFTGHTN LKNFVGLSVS DGYIATGSET
NEVFVYHKAF PMPVMSYMFN NTDSMSGLEV DDASQFISSI CWRGQSSTLV AANSNGNIKI
LEMMT
