NPY3_ARATH
ID NPY3_ARATH Reviewed; 579 AA.
AC Q9FN09; Q93Y14;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=BTB/POZ domain-containing protein NPY3;
DE AltName: Full=Protein NAKED PINS IN YUC MUTANTS 3;
GN Name=NPY3; OrderedLocusNames=At5g67440; ORFNames=K8K14.18;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19075219; DOI=10.1073/pnas.0809761106;
RA Cheng Y., Qin G., Dai X., Zhao Y.;
RT "NPY genes and AGC kinases define two key steps in auxin-mediated
RT organogenesis in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:21017-21022(2008).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20833732; DOI=10.1093/mp/ssq052;
RA Li Y., Dai X., Cheng Y., Zhao Y.;
RT "NPY genes play an essential role in root gravitropic responses in
RT Arabidopsis.";
RL Mol. Plant 4:171-179(2011).
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 (By similarity). May play an essential role in auxin-mediated
CC organogenesis and in root gravitropic responses. {ECO:0000250,
CC ECO:0000269|PubMed:19075219, ECO:0000269|PubMed:20833732}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FN09-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the provascular and vascular systems.
CC Highly expressed in primary root tips. {ECO:0000269|PubMed:19075219,
CC ECO:0000269|PubMed:20833732}.
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}.
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DR EMBL; AB007645; BAB09029.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98344.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69406.1; -; Genomic_DNA.
DR EMBL; AY054694; AAK96885.1; -; mRNA.
DR EMBL; AY128721; AAM91121.1; -; mRNA.
DR RefSeq; NP_001331087.1; NM_001345830.1. [Q9FN09-1]
DR RefSeq; NP_201545.1; NM_126144.4. [Q9FN09-1]
DR AlphaFoldDB; Q9FN09; -.
DR BioGRID; 22122; 1.
DR STRING; 3702.AT5G67440.1; -.
DR PaxDb; Q9FN09; -.
DR PRIDE; Q9FN09; -.
DR ProteomicsDB; 251072; -. [Q9FN09-1]
DR EnsemblPlants; AT5G67440.1; AT5G67440.1; AT5G67440. [Q9FN09-1]
DR EnsemblPlants; AT5G67440.3; AT5G67440.3; AT5G67440. [Q9FN09-1]
DR GeneID; 836880; -.
DR Gramene; AT5G67440.1; AT5G67440.1; AT5G67440. [Q9FN09-1]
DR Gramene; AT5G67440.3; AT5G67440.3; AT5G67440. [Q9FN09-1]
DR KEGG; ath:AT5G67440; -.
DR Araport; AT5G67440; -.
DR TAIR; locus:2158182; AT5G67440.
DR eggNOG; ENOG502QSYM; Eukaryota.
DR HOGENOM; CLU_005994_5_2_1; -.
DR InParanoid; Q9FN09; -.
DR OMA; LCDLEMD; -.
DR OrthoDB; 373216at2759; -.
DR PhylomeDB; Q9FN09; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FN09; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN09; baseline and differential.
DR Genevisible; Q9FN09; AT.
DR GO; GO:0071944; C:cell periphery; IDA:TAIR.
DR GO; GO:0009908; P:flower development; IGI:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IGI: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 2: Evidence at transcript level;
KW Alternative splicing; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..579
FT /note="BTB/POZ domain-containing protein NPY3"
FT /id="PRO_0000409565"
FT DOMAIN 29..100
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 205..476
FT /note="NPH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00982"
FT REGION 479..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 417
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMF5"
FT CONFLICT 258
FT /note="D -> N (in Ref. 3; AAK96885/AAM91121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 64765 MW; FD24DB00C95497B1 CRC64;
MKFMKLGSKP DSFQSDEDCV RYVATELATD VVVIVGDVKF HLHKFPLLSK SARLQKLIAT
TTTDEQSDDD EIRIPDIPGG PPAFEICAKF CYGMAVTLNA YNVVAVRCAA EYLEMYESIE
NGNLVYKMEV FLNSSVLRSW KDSIIVLQTT RSFYPWSEDV KLDVRCLESI ALKAAMDPAR
VDWSYTYNRR KLLPPEMNNN SVPRDWWVED LAELSIDLFK RVVSTIRRKG GVLPEVIGEA
LEVYAAKRIP GFMIQNDDND DEEDVMEQRS LLETLVSMLP SEKQSVSCGF LIKLLKSSVS
FECGEEERKE LSRRIGEKLE EANVGDLLIR APEGGETVYD IDIVETLIDE FVTQTEKRDE
LDCSDDINDS SKANVAKLID GYLAEISRIE TNLSTTKFIT IAEKVSTFPR QSHDGVYRAI
DMFLKQHPGI TKSEKKSSSK LMDCRKLSPE ACAHAVQNER LPLRVVVQIL FFEQVRATTK
PSLPPSGSHG SSRTTTEEEC ESVTATEETT TTTRDKTSSS EKTKAKGVVM SRIFSKLWTG
KDKDGVGDVS SSDTSESPGS VTTVGDKSTP STRRRRSSS
