Y1044_ARATH
ID Y1044_ARATH Reviewed; 665 AA.
AC Q9S9Q9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=BTB/POZ domain-containing protein At1g30440;
GN OrderedLocusNames=At1g30440; ORFNames=F26G16.2;
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 DOMAIN BTB.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- SIMILARITY: Belongs to the NPH3 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00982}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19742.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009917; AAF19742.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE31216.1; -; Genomic_DNA.
DR PIR; G86428; G86428.
DR RefSeq; NP_174332.1; NM_102780.3.
DR AlphaFoldDB; Q9S9Q9; -.
DR BioGRID; 25158; 2.
DR IntAct; Q9S9Q9; 1.
DR MINT; Q9S9Q9; -.
DR STRING; 3702.AT1G30440.1; -.
DR iPTMnet; Q9S9Q9; -.
DR PaxDb; Q9S9Q9; -.
DR PRIDE; Q9S9Q9; -.
DR ProteomicsDB; 234309; -.
DR EnsemblPlants; AT1G30440.1; AT1G30440.1; AT1G30440.
DR GeneID; 839923; -.
DR Gramene; AT1G30440.1; AT1G30440.1; AT1G30440.
DR KEGG; ath:AT1G30440; -.
DR Araport; AT1G30440; -.
DR TAIR; locus:2028160; AT1G30440.
DR eggNOG; ENOG502RRH3; Eukaryota.
DR HOGENOM; CLU_005994_6_2_1; -.
DR InParanoid; Q9S9Q9; -.
DR OMA; KIKSQMC; -.
DR OrthoDB; 481589at2759; -.
DR PhylomeDB; Q9S9Q9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9S9Q9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S9Q9; baseline and differential.
DR Genevisible; Q9S9Q9; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR043454; NPH3/RPT2-like.
DR InterPro; IPR027356; NPH3_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR32370; PTHR32370; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF03000; NPH3; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS51649; NPH3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..665
FT /note="BTB/POZ domain-containing protein At1g30440"
FT /id="PRO_0000315354"
FT DOMAIN 28..98
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 214..508
FT /note="NPH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00982"
FT REGION 260..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 281..306
FT /evidence="ECO:0000255"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 449
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMF5"
SQ SEQUENCE 665 AA; 73410 MW; 8EAE7C037AD52E73 CRC64;
MACMKLGSKS DAFQRQGQAW FCTTGLPSDI VVEVGEMSFH LHKFPLLSRS GVMERRIAEA
SKEGDDKCLI EISDLPGGDK TFELVAKFCY GVKLELTASN VVYLRCAAEH LEMTEEHGEG
NLISQTETFF NQVVLKSWKD SIKALHSCDE VLEYADELNI TKKCIESLAM RASTDPNLFG
WPVVEHGGPM QSPGGSVLWN GISTGARPKH TSSDWWYEDA SMLSFPLFKR LITVMESRGI
REDIIAGSLT YYTRKHLPGL KRRRGGPESS GRFSTPLGSG NVLSEEEQKN LLEEIQELLR
MQKGLVPTKF FVDMLRIAKI LKASPDCIAN LEKRIGMQLD QAALEDLVMP SFSHTMETLY
DVDSVQRILD HFLGTDQIMP GGVGSPCSSV DDGNLIGSPQ SITPMTAVAK LIDGYLAEVA
PDVNLKLPKF QALAASIPEY ARLLDDGLYR AIDIYLKHHP WLAETERENL CRLLDCQKLS
LEACTHAAQN ERLPLRIIVQ VLFFEQLQLR TSVAGCFLVS DNLDGGSRQL RSGGYVGGPN
EGGGGGGGWA TAVRENQVLK VGMDSMRMRV CELEKECSNM RQEIEKLGKT TKGGGSASNG
VGSKTWENVS KKLGFGFKLK SHQMCSAQEG SVSKSNNENV KIEKLKDVKE RRGKHKKASS
ISSER
