SPA4_ARATH
ID SPA4_ARATH Reviewed; 794 AA.
AC Q94BM7; Q9LNN4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein SPA1-RELATED 4;
GN Name=SPA4; OrderedLocusNames=At1g53090; ORFNames=F8L10.5;
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 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).
RN [9]
RP INTERACTION WITH CRY1, AND DISRUPTION PHENOTYPE.
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).
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 (PubMed:12887588, PubMed:16854975).
CC Binds to CRY1 in response to blue light, this interaction prevents
CC SPA1/COP1 complex formation and thus avoid COP1-dependent degradation
CC of the transcription factor HY5 by the proteasome and promotes
CC hypocotyl elongation (PubMed:21511871). {ECO:0000269|PubMed:12887588,
CC ECO:0000269|PubMed:16854975, ECO:0000269|PubMed:21511871}.
CC -!- INTERACTION:
CC Q94BM7; O50055: COL1; NbExp=7; IntAct=EBI-626943, EBI-1112154;
CC Q94BM7; P43254: COP1; NbExp=14; IntAct=EBI-626943, EBI-301649;
CC Q94BM7; Q9SYX2: SPA1; NbExp=9; IntAct=EBI-626943, EBI-626992;
CC Q94BM7; Q9LJR3: SPA3; NbExp=6; IntAct=EBI-626943, EBI-626921;
CC Q94BM7; Q94BM7: SPA4; NbExp=2; IntAct=EBI-626943, EBI-626943;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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 -!- DISRUPTION PHENOTYPE: Reduced hypocotyl elongation in blue light.
CC {ECO:0000269|PubMed:21511871}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87859.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022520; AAF87859.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32888.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32889.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59146.1; -; Genomic_DNA.
DR EMBL; AY040023; AAK64180.1; -; mRNA.
DR EMBL; AY133883; AAM91817.1; -; mRNA.
DR PIR; E96571; E96571.
DR RefSeq; NP_001321533.1; NM_001333576.1.
DR RefSeq; NP_175717.1; NM_104188.4.
DR RefSeq; NP_849802.1; NM_179471.2.
DR AlphaFoldDB; Q94BM7; -.
DR SMR; Q94BM7; -.
DR BioGRID; 26968; 11.
DR IntAct; Q94BM7; 4.
DR STRING; 3702.AT1G53090.2; -.
DR iPTMnet; Q94BM7; -.
DR PaxDb; Q94BM7; -.
DR PRIDE; Q94BM7; -.
DR ProteomicsDB; 232522; -.
DR EnsemblPlants; AT1G53090.1; AT1G53090.1; AT1G53090.
DR EnsemblPlants; AT1G53090.2; AT1G53090.2; AT1G53090.
DR EnsemblPlants; AT1G53090.3; AT1G53090.3; AT1G53090.
DR GeneID; 841743; -.
DR Gramene; AT1G53090.1; AT1G53090.1; AT1G53090.
DR Gramene; AT1G53090.2; AT1G53090.2; AT1G53090.
DR Gramene; AT1G53090.3; AT1G53090.3; AT1G53090.
DR KEGG; ath:AT1G53090; -.
DR Araport; AT1G53090; -.
DR TAIR; locus:2037005; AT1G53090.
DR eggNOG; KOG1033; Eukaryota.
DR HOGENOM; CLU_006994_1_1_1; -.
DR InParanoid; Q94BM7; -.
DR OMA; CANAYAS; -.
DR OrthoDB; 857220at2759; -.
DR PhylomeDB; Q94BM7; -.
DR PRO; PR:Q94BM7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94BM7; baseline and differential.
DR Genevisible; Q94BM7; 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: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 GO; GO:0009637; P:response to blue light; IMP:UniProtKB.
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; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
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..794
FT /note="Protein SPA1-RELATED 4"
FT /id="PRO_0000363494"
FT DOMAIN 1..268
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 482..521
FT /note="WD 1"
FT REPEAT 531..571
FT /note="WD 2"
FT REPEAT 574..614
FT /note="WD 3"
FT REPEAT 616..656
FT /note="WD 4"
FT REPEAT 660..698
FT /note="WD 5"
FT REPEAT 707..746
FT /note="WD 6"
FT REPEAT 762..794
FT /note="WD 7"
FT REGION 126..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 272..326
FT /evidence="ECO:0000255"
FT MOTIF 635..649
FT /note="DWD box"
FT COMPBIAS 134..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 89071 MW; 5202D640029F512F CRC64;
MKGSSESSSR GLNNTSGVSE FCTDGSKSLS HIDYVRSLLG SHKEANLGGL DDDSIVRALE
CEDVSLRQWL DNPDRSVDAF ECFHVFRQIV EIVNAAHSQG IVVHNVRPSC FVMSSFNNVS
FIESASCSDS GSDEDATTKS REIGSSRQEE ILSERRSKQQ EEVKKQPFPM KQILAMEMSW
YTSHEEDNGS LCNCASDIYR LGVLLFELFC PVSSREEKSR TMSSLRHRVL PPQILLNWPK
EASFCLWLLH PEPSCRPSMS ELLQSEFINE PRENLEEREA AMELRDRIEE QELLLEFLFL
IQQRKQEAAD KLQDTISLLS SDIDQVVKRQ LVLQQKGRDV RSFLASRKRI RQGAETTAAE
EENDDNSIDE ESKLDDTLES TLLESSRLMR NLKKLESVYF ATRYRQIKAA TAAEKPLARY
YSALSCNGRS SEKSSMSQPS KDPINDSRQG GWIDPFLEGL CKYLSFSKLR VKADLKQGDL
LNSSNLVCAI GFDRDGEFFA TAGVNKKIKI FECESIIKDG RDIHYPVVEL ASRSKLSGIC
WNSYIKSQVA SSNFEGVVQV WDVARNQLVT EMKEHEKRVW SIDYSSADPT LLASGSDDGS
VKLWSINQGV SIGTIKTKAN ICCVQFPSET GRSLAFGSAD HKVYYYDLRN PKLPLCTMIG
HHKTVSYVRF VDSSTLVSSS TDNTLKLWDL SMSISGINET PLHSFMGHTN VKNFVGLSVS
DGYIATGSET NEVFVYHKAF PMPVLSYKFK TIDPVSELEV DDASQFISSV CWRGQSSTLV
AANSTGNIKI LEMV
