SKP2A_ARATH
ID SKP2A_ARATH Reviewed; 360 AA.
AC Q9LPL4; Q8LDN3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=F-box protein SKP2A;
DE AltName: Full=FBL5-like protein;
DE Short=AtFBL5;
DE AltName: Full=SKP2-like protein 1;
DE Short=AtSKP2;1;
GN Name=SKP2A; OrderedLocusNames=At1g21410; ORFNames=F24J8.5;
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INTERACTION WITH CUL1 AND E2FC.
RX PubMed=12468727; DOI=10.1105/tpc.006791;
RA del Pozo J.C., Boniotti M.B., Gutierrez C.;
RT "Arabidopsis E2Fc functions in cell division and is degraded by the
RT ubiquitin-SCF(AtSKP2) pathway in response to light.";
RL Plant Cell 14:3057-3071(2002).
RN [6]
RP FUNCTION.
RX PubMed=16920782; DOI=10.1105/tpc.105.039651;
RA del Pozo J.C., Diaz-Trivino S., Cisneros N., Gutierrez C.;
RT "The balance between cell division and endoreplication depends on E2FC-DPB,
RT transcription factors regulated by the ubiquitin-SCFSKP2A pathway in
RT Arabidopsis.";
RL Plant Cell 18:2224-2235(2006).
RN [7]
RP FUNCTION, UBIQUITINATION, INDUCTION DURING CELL CYCLE, DEVELOPMENTAL STAGE,
RP TISSUE SPECIFICITY, INTERACTION WITH SKP1A; SKP1B AND ASK18, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18036202; DOI=10.1111/j.1365-313x.2007.03378.x;
RA Jurado S., Diaz-Trivino S., Abraham Z., Manzano C., Gutierrez C.,
RA del Pozo C.;
RT "SKP2A, an F-box protein that regulates cell division, is degraded via the
RT ubiquitin pathway.";
RL Plant J. 53:828-841(2008).
RN [8]
RP FUNCTION, UBIQUITINATION, AND INDUCTION BY AUXIN.
RX PubMed=19704565; DOI=10.4161/psb.3.10.5888;
RA Jurado S., Trivino S.D., Abraham Z., Manzano C., Gutierrez C., Del Pozo C.;
RT "SKP2A protein, an F-box that regulates cell division, is degraded via the
RT ubiquitin pathway.";
RL Plant Signal. Behav. 3:810-812(2008).
RN [9]
RP FUNCTION, INTERACTION WITH DPB AND AUXIN, AND MUTAGENESIS OF LEU-128 AND
RP SER-151.
RX PubMed=21139066; DOI=10.1105/tpc.110.078972;
RA Jurado S., Abraham Z., Manzano C., Lopez-Torrejon G., Pacios L.F.,
RA Del Pozo J.C.;
RT "The Arabidopsis cell cycle F-Box protein SKP2A binds to auxin.";
RL Plant Cell 22:3891-3904(2010).
CC -!- FUNCTION: Component of SCF(SKP2A) E3 ubiquitin ligase complexes, which
CC mediate the ubiquitination and subsequent proteasomal degradation of
CC target proteins (including cell cycle repressors). Acts as an auxin
CC receptor; one active auxin is indole-3-acetate. Regulates the stability
CC of the transcription factors E2FC and DPB, repressors of cell
CC proliferation. Confers increase tolerance to osmotic stress by
CC promoting cell division, especially in meristems. Promotes the
CC formation of lateral root primordia. {ECO:0000269|PubMed:12468727,
CC ECO:0000269|PubMed:16920782, ECO:0000269|PubMed:18036202,
CC ECO:0000269|PubMed:19704565, ECO:0000269|PubMed:21139066}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (ASK-cullin-F-box) protein ligase complex.
CC Interacts with CUL1 (RUB1-modified and non-modified isoforms), SKP1A,
CC SKP1B and ASK18. Recruit DPB and phosphorylated E2FC. Interacts with
CC auxin. Auxin controls the interaction with DPB.
CC {ECO:0000269|PubMed:12468727, ECO:0000269|PubMed:18036202,
CC ECO:0000269|PubMed:21139066}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18036202}.
CC -!- TISSUE SPECIFICITY: Expressed in embryo, seedlings, hypocotyl, roots,
CC leaves and flowers. {ECO:0000269|PubMed:18036202}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed during the first stages of
CC germination. In seedling, more intense in dividing areas, such as
CC meristems and young organs. In leaves, confined to vascular tissue and
CC stomatal cells. In roots, detected in tips, vascular cylinder of the
CC distal part, and in lateral roots emerging primordia. Low levels in
CC specific cells of root meristems. {ECO:0000269|PubMed:18036202}.
CC -!- INDUCTION: Cell-cycle regulated expression with higher levels during
CC early S-phase and G2/M stages. Repressed by auxin through a ubiquitin-
CC dependent pathway (at protein level). Only biologically active auxin
CC promotes proteolysis of SKP2A. {ECO:0000269|PubMed:18036202,
CC ECO:0000269|PubMed:19704565}.
CC -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC {ECO:0000250}.
CC -!- PTM: Polyubiquitinated and subsequently targeted to proteasome. Auxin
CC promotes this ubiquitination-mediated degradation.
CC {ECO:0000269|PubMed:18036202, ECO:0000269|PubMed:19704565}.
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DR EMBL; AC015447; AAF87895.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30100.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58718.1; -; Genomic_DNA.
DR EMBL; AY058081; AAL24189.1; -; mRNA.
DR EMBL; AY090308; AAL90969.1; -; mRNA.
DR EMBL; AY085898; AAM63110.1; -; mRNA.
DR PIR; B86347; B86347.
DR RefSeq; NP_001321134.1; NM_001332504.1.
DR RefSeq; NP_564139.1; NM_101993.4.
DR AlphaFoldDB; Q9LPL4; -.
DR SMR; Q9LPL4; -.
DR BioGRID; 23979; 9.
DR IntAct; Q9LPL4; 1.
DR STRING; 3702.AT1G21410.1; -.
DR PaxDb; Q9LPL4; -.
DR PRIDE; Q9LPL4; -.
DR EnsemblPlants; AT1G21410.1; AT1G21410.1; AT1G21410.
DR EnsemblPlants; AT1G21410.2; AT1G21410.2; AT1G21410.
DR GeneID; 838740; -.
DR Gramene; AT1G21410.1; AT1G21410.1; AT1G21410.
DR Gramene; AT1G21410.2; AT1G21410.2; AT1G21410.
DR KEGG; ath:AT1G21410; -.
DR Araport; AT1G21410; -.
DR TAIR; locus:2027082; AT1G21410.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_032606_0_0_1; -.
DR InParanoid; Q9LPL4; -.
DR OMA; KHEMWAS; -.
DR OrthoDB; 1046098at2759; -.
DR PhylomeDB; Q9LPL4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LPL4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPL4; baseline and differential.
DR Genevisible; Q9LPL4; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071365; P:cellular response to auxin stimulus; IDA:UniProtKB.
DR GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF13516; LRR_6; 2.
DR SMART; SM00367; LRR_CC; 8.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Lipoprotein; Myristate; Nucleus;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..360
FT /note="F-box protein SKP2A"
FT /id="PRO_0000396016"
FT DOMAIN 25..71
FT /note="F-box"
FT BINDING 127..128
FT /ligand="(indol-3-yl)acetate"
FT /ligand_id="ChEBI:CHEBI:30854"
FT BINDING 149..152
FT /ligand="(indol-3-yl)acetate"
FT /ligand_id="ChEBI:CHEBI:30854"
FT BINDING 175..178
FT /ligand="(indol-3-yl)acetate"
FT /ligand_id="ChEBI:CHEBI:30854"
FT BINDING 202
FT /ligand="(indol-3-yl)acetate"
FT /ligand_id="ChEBI:CHEBI:30854"
FT MUTAGEN 128
FT /note="L->S: 60% reduction of auxin binding. 70% reduction
FT of auxin binding and loss of ubiquitination-mediated
FT degradation; when associated with A-151."
FT /evidence="ECO:0000269|PubMed:21139066"
FT MUTAGEN 151
FT /note="S->A: 60% reduction of auxin binding. 70% reduction
FT of auxin binding and loss of ubiquitination-mediated
FT degradation; when associated with S-128."
FT /evidence="ECO:0000269|PubMed:21139066"
FT CONFLICT 266
FT /note="M -> I (in Ref. 4; AAM63110)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="P -> S (in Ref. 4; AAM63110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39614 MW; 2D894F6E6CE4A718 CRC64;
MVMGGEASME LDQCFQKMKM EGISIKEWKD IPVELLMRIL SLVDDRNVIV ASGVCTGWRD
AISFGLTRLR LSWCNNNMNS LVLSLVPKFV KLQTLNLRQD KPQLEDNAVE AIANHCHELQ
ELDLSKSLKI TDRSLYALAH GCPDLTKLNL SGCTSFSDTA IAYLTRFCRK LKVLNLCGCV
KAVTDNALEA IGNNCNQMQS LNLGWCENIS DDGVMSLAYG CPDLRTLDLC GCVLITDESV
VALADWCVHL RSLGLYYCRN ITDRAMYSLA QSGVKNKPGS WKSVKKGKYD EEGLRSLNIS
QCTALTPSAV QAVCDSFPAL HTCSGRHSLV MSGCLNLTTV HCACILQAHR AHNAVPHPAH
