ID   TLP9_ARATH              Reviewed;         380 AA.
AC   Q9SQU1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Tubby-like F-box protein 9;
DE            Short=AtTLP9;
GN   Name=TULP9; OrderedLocusNames=At3g06380; ORFNames=F24P17.15;
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], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, INDUCTION, INTERACTION WITH SKP1A/ASK1, GENE FAMILY, AND
RP   NOMENCLATURE.
RX   PubMed=15064372; DOI=10.1104/pp.103.037820;
RA   Lai C.-P., Lee C.-L., Chen P.-H., Wu S.-H., Yang C.-C., Shaw J.-F.;
RT   "Molecular analyses of the Arabidopsis TUBBY-like protein gene family.";
RL   Plant Physiol. 134:1586-1597(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH XERICO.
RX   PubMed=16792696; DOI=10.1111/j.1365-313x.2006.02782.x;
RA   Ko J.-H., Yang S.H., Han K.-H.;
RT   "Upregulation of an Arabidopsis RING-H2 gene, XERICO, confers drought
RT   tolerance through increased abscisic acid biosynthesis.";
RL   Plant J. 47:343-355(2006).
CC   -!- FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase
CC       complexes, which may mediate the ubiquitination and subsequent
CC       proteasomal degradation of target proteins. Confers sensitivity to ABA
CC       during seed germination and early seedling development.
CC       {ECO:0000269|PubMed:15064372}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       Interacts with SKP1A/ASK1 and XERICO. {ECO:0000269|PubMed:15064372,
CC       ECO:0000269|PubMed:16792696}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15064372}.
CC   -!- DEVELOPMENTAL STAGE: Expressed early during seed germination,
CC       especially in the preemergent radicle. {ECO:0000269|PubMed:15064372}.
CC   -!- INDUCTION: During imbibition of seeds. {ECO:0000269|PubMed:15064372}.
CC   -!- SIMILARITY: Belongs to the TUB family. {ECO:0000305}.
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DR   EMBL; AF487270; AAQ06243.1; -; mRNA.
DR   EMBL; AC011623; AAF08576.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74384.1; -; Genomic_DNA.
DR   EMBL; BT026465; ABH04572.1; -; mRNA.
DR   RefSeq; NP_187289.1; NM_111513.4.
DR   AlphaFoldDB; Q9SQU1; -.
DR   SMR; Q9SQU1; -.
DR   BioGRID; 5147; 6.
DR   IntAct; Q9SQU1; 4.
DR   STRING; 3702.AT3G06380.1; -.
DR   PaxDb; Q9SQU1; -.
DR   PRIDE; Q9SQU1; -.
DR   EnsemblPlants; AT3G06380.1; AT3G06380.1; AT3G06380.
DR   GeneID; 819812; -.
DR   Gramene; AT3G06380.1; AT3G06380.1; AT3G06380.
DR   KEGG; ath:AT3G06380; -.
DR   Araport; AT3G06380; -.
DR   TAIR; locus:2081101; AT3G06380.
DR   eggNOG; KOG2502; Eukaryota.
DR   HOGENOM; CLU_028236_3_0_1; -.
DR   InParanoid; Q9SQU1; -.
DR   OrthoDB; 1445357at2759; -.
DR   PhylomeDB; Q9SQU1; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9SQU1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SQU1; baseline and differential.
DR   Genevisible; Q9SQU1; AT.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR   GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR   Gene3D; 3.20.90.10; -; 1.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR025659; Tubby-like_C.
DR   InterPro; IPR000007; Tubby_C.
DR   InterPro; IPR018066; Tubby_C_CS.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF01167; Tub; 1.
DR   PRINTS; PR01573; SUPERTUBBY.
DR   SUPFAM; SSF54518; SSF54518; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS01200; TUB_1; 1.
PE   1: Evidence at protein level;
KW   Abscisic acid signaling pathway; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..380
FT                   /note="Tubby-like F-box protein 9"
FT                   /id="PRO_0000272237"
FT   DOMAIN          30..76
FT                   /note="F-box"
FT   REGION          258..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   380 AA;  42310 MW;  EDB57859F8B5F51D CRC64;
     MTFRSLLQEM RSRPHRVVHA AASTANSSDP FSWSELPEEL LREILIRVET VDGGDWPSRR
     NVVACAGVCR SWRILTKEIV AVPEFSSKLT FPISLKQSGP RDSLVQCFIK RNRNTQSYHL
     YLGLTTSLTD NGKFLLAASK LKRATCTDYI ISLRSDDISK RSNAYLGRMR SNFLGTKFTV
     FDGSQTGAAK MQKSRSSNFI KVSPRVPQGS YPIAHISYEL NVLGSRGPRR MRCIMDTIPM
     SIVESRGVVA STSISSFSSR SSPVFRSHSK PLRSNSASCS DSGNNLGDPP LVLSNKAPRW
     HEQLRCWCLN FHGRVTVASV KNFQLVAVSD CEAGQTSERI ILQFGKVGKD MFTMDYGYPI
     SAFQAFAICL SSFETRIACE