NPY2_ARATH
ID NPY2_ARATH Reviewed; 634 AA.
AC O80970;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=BTB/POZ domain-containing protein NPY2;
DE AltName: Full=Protein NAKED PINS IN YUC MUTANTS 2;
GN Name=NPY2; OrderedLocusNames=At2g14820; ORFNames=F26C24.4;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] OF 55-254.
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
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 -!- TISSUE SPECIFICITY: Specifically expressed in the hypophysis and the
CC root meristems in the embryos. Highly expressed in primary root tips.
CC {ECO:0000269|PubMed:19075219, 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; AC004705; AAC24177.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06336.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61860.1; -; Genomic_DNA.
DR EMBL; DQ069815; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T02594; T02594.
DR RefSeq; NP_001318225.1; NM_001335440.1.
DR RefSeq; NP_179089.1; NM_127046.2.
DR AlphaFoldDB; O80970; -.
DR SMR; O80970; -.
DR STRING; 3702.AT2G14820.1; -.
DR iPTMnet; O80970; -.
DR PaxDb; O80970; -.
DR PRIDE; O80970; -.
DR ProteomicsDB; 250549; -.
DR EnsemblPlants; AT2G14820.1; AT2G14820.1; AT2G14820.
DR EnsemblPlants; AT2G14820.2; AT2G14820.2; AT2G14820.
DR GeneID; 815970; -.
DR Gramene; AT2G14820.1; AT2G14820.1; AT2G14820.
DR Gramene; AT2G14820.2; AT2G14820.2; AT2G14820.
DR KEGG; ath:AT2G14820; -.
DR Araport; AT2G14820; -.
DR TAIR; locus:2046961; AT2G14820.
DR eggNOG; ENOG502QSYM; Eukaryota.
DR HOGENOM; CLU_005994_5_2_1; -.
DR InParanoid; O80970; -.
DR OMA; HPGISKG; -.
DR OrthoDB; 373216at2759; -.
DR PhylomeDB; O80970; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O80970; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80970; baseline and differential.
DR GO; GO:0071944; C:cell periphery; IDA: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; IPR029960; BTB/POZ_NPY2.
DR InterPro; IPR043454; NPH3/RPT2-like.
DR InterPro; IPR027356; NPH3_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR32370; PTHR32370; 1.
DR PANTHER; PTHR32370:SF4; PTHR32370:SF4; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF03000; NPH3; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS51649; NPH3; 1.
PE 2: Evidence at transcript level;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..634
FT /note="BTB/POZ domain-containing protein NPY2"
FT /id="PRO_0000409564"
FT DOMAIN 29..97
FT /note="BTB"
FT DOMAIN 207..488
FT /note="NPH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00982"
FT REGION 492..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 429
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMF5"
FT CONFLICT 217
FT /note="E -> K (in Ref. 3; DQ069815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 634 AA; 70194 MW; 71581B1AEF8D11AE CRC64;
MKFMKIGSKL DSFKTDGNNV RYVENELASD ISVDVEGSRF CLHKFPLLSK CACLQKLLSS
TDKNNIDDID ISGIPGGPTA FETCAKFCYG MTVTLSAYNV VATRCAAEYL GMHETVEKGN
LIYKIDVFLS SSLFRSWKDS IIVLQTTKPF LPLSEDLKLV SLCIDAIATK ACVDVSHVEW
SYTYNKKKLA EENNGADSIK ARDVPHDWWV EDLCELEIDY YKRVIMNIKT KCILGGEVIG
EALKAYGYRR LSGFNKGVME QGDLVKHKTI IETLVWLLPA EKNSVSCGFL LKLLKAVTMV
NSGEVVKEQL VRRIGQQLEE ASMAELLIKS HQGSETLYDV DLVQKIVMEF MRRDKNSEIE
VQDDEDGFEV QEVRKLPGIL SEASKLMVAK VIDSYLTEIA KDPNLPASKF IDVAESVTSI
PRPAHDALYR AIDMFLKEHP GITKGEKKRM CKLMDCRKLS VEACMHAVQN DRLPLRVVVQ
VLFFEQVRAA ASSGSSTPDL PRGMGRELRS CGTYGSSRSV PTVMEDEWEA VATEEEMRAL
KSEIAALKLQ EESGRKSMDR AGVTAISKIR SLIMSKKIFG KKVQLQSKGG GEKNNGGGGG
GSDSSESLGS MNAAEETAKT ATPSRNLTRR VSVS
