NPY1_ARATH
ID NPY1_ARATH Reviewed; 571 AA.
AC Q8H1D3; Q8RWY9; Q9SZ49;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=BTB/POZ domain-containing protein NPY1;
DE AltName: Full=Protein ENHANCER OF PINOID;
DE AltName: Full=Protein MACCHI-BOU 4;
DE AltName: Full=Protein NAKED PINS IN YUC MUTANTS 1;
GN Name=NPY1; Synonyms=ENP, MAB4; OrderedLocusNames=At4g31820;
GN ORFNames=F11C18.20;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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].
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 FUNCTION.
RX PubMed=16107478; DOI=10.1242/dev.01969;
RA Treml B.S., Winderl S., Radykewicz R., Herz M., Schweizer G., Hutzler P.,
RA Glawischnig E., Ruiz R.A.;
RT "The gene ENHANCER OF PINOID controls cotyledon development in the
RT Arabidopsis embryo.";
RL Development 132:4063-4074(2005).
RN [5]
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 [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=17913786; DOI=10.1242/dev.009654;
RA Furutani M., Kajiwara T., Kato T., Treml B.S., Stockum C.,
RA Torres-Ruiz R.A., Tasaka M.;
RT "The gene MACCHI-BOU 4/ENHANCER OF PINOID encodes a NPH3-like protein and
RT reveals similarities between organogenesis and phototropism at the
RT molecular level.";
RL Development 134:3849-3859(2007).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18000043; DOI=10.1073/pnas.0708506104;
RA Cheng Y., Qin G., Dai X., Zhao Y.;
RT "NPY1, a BTB-NPH3-like protein, plays a critical role in auxin-regulated
RT organogenesis in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18825-18829(2007).
RN [8]
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 [9]
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). Coregulates with PID the auxin-mediated plant
CC organogenesis. Regulates cotyledon development through control of PIN1
CC polarity. May play an essential role in root gravitropic responses.
CC {ECO:0000250, ECO:0000269|PubMed:16107478, ECO:0000269|PubMed:17913786,
CC ECO:0000269|PubMed:18000043, ECO:0000269|PubMed:19075219,
CC ECO:0000269|PubMed:20833732}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:17913786}.
CC Note=Colocalized with PID.
CC -!- TISSUE SPECIFICITY: Expressed mainly in the apical regions of embryos
CC including cotyledon tips and the apical meristem. Highly expressed in
CC primary root tips. {ECO:0000269|PubMed:19075219,
CC ECO:0000269|PubMed:20833732}.
CC -!- DEVELOPMENTAL STAGE: Detected in globular-stage embryos in the
CC epidermis with the highest concentration at the apical region. At early
CC heart stage, expression is restricted to the two cotyledon primordia
CC and the meristem. In the late heart to torpedo stages, expression is
CC restricted to the meristem and the cotyledon tips. In mature embryos,
CC stricly expressed at the apical meristem. During seedling development,
CC highly expressed in young leaf primordia and the apical meristems.
CC Detected in the protodermal cell layer of the embryo and the meristem
CC L1 layer at the site of organ initiation. After transition to the
CC reproductive phase, detected in the inflorescence meristem and at
CC various stages of floral development. {ECO:0000269|PubMed:17913786,
CC ECO:0000269|PubMed:18000043}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- DISRUPTION PHENOTYPE: Seedlings with abnormal cotyledons.
CC {ECO:0000269|PubMed:18000043}.
CC -!- SIMILARITY: Belongs to the NPH3 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00982}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40752.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79900.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049607; CAB40752.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161579; CAB79900.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85964.1; -; Genomic_DNA.
DR EMBL; AY091021; AAM13843.1; -; mRNA.
DR EMBL; AY150514; AAN13030.1; -; mRNA.
DR PIR; T06304; T06304.
DR RefSeq; NP_194910.2; NM_119332.4.
DR AlphaFoldDB; Q8H1D3; -.
DR SMR; Q8H1D3; -.
DR STRING; 3702.AT4G31820.1; -.
DR iPTMnet; Q8H1D3; -.
DR PaxDb; Q8H1D3; -.
DR PRIDE; Q8H1D3; -.
DR ProteomicsDB; 250548; -.
DR EnsemblPlants; AT4G31820.1; AT4G31820.1; AT4G31820.
DR GeneID; 829311; -.
DR Gramene; AT4G31820.1; AT4G31820.1; AT4G31820.
DR KEGG; ath:AT4G31820; -.
DR Araport; AT4G31820; -.
DR TAIR; locus:2116752; AT4G31820.
DR eggNOG; ENOG502QQX7; Eukaryota.
DR HOGENOM; CLU_005994_5_2_1; -.
DR InParanoid; Q8H1D3; -.
DR OMA; KATSNPC; -.
DR OrthoDB; 395689at2759; -.
DR PhylomeDB; Q8H1D3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8H1D3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8H1D3; baseline and differential.
DR Genevisible; Q8H1D3; AT.
DR GO; GO:0005770; C:late endosome; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0045176; P:apical protein localization; IGI:TAIR.
DR GO; GO:0010540; P:basipetal auxin transport; IGI:TAIR.
DR GO; GO:0048825; P:cotyledon development; IGI:TAIR.
DR GO; GO:0009908; P:flower development; IGI:TAIR.
DR GO; GO:0010229; P:inflorescence development; IGI:TAIR.
DR GO; GO:0009911; P:positive regulation of flower development; 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; IPR029961; BTB/POZ_NPY1.
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:SF7; PTHR32370:SF7; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF03000; NPH3; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS51649; NPH3; 1.
PE 2: Evidence at transcript level;
KW Endosome; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..571
FT /note="BTB/POZ domain-containing protein NPY1"
FT /id="PRO_0000409563"
FT DOMAIN 29..97
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 210..468
FT /note="NPH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00982"
FT REGION 475..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 409
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMF5"
FT CONFLICT 226
FT /note="R -> G (in Ref. 3; AAM13843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 571 AA; 64402 MW; AE03D3C1C50194D7 CRC64;
MKFMKLGSKP DTFESDGKFV KYAVSDLDSD VTIHVGEVTF HLHKFPLLSK SNRMQRLVFE
ASEEKTDEIT ILDMPGGYKA FEICAKFCYG MTVTLNAYNI TAVRCAAEYL EMTEDADRGN
LIYKIEVFLN SGIFRSWKDS IIVLQTTRSL LPWSEDLKLV GRCIDSVSAK ILVNPETITW
SYTFNRKLSG PDKIVEYHRE KREENVIPKD WWVEDVCELE IDMFKRVISV VKSSGRMNNG
VIAEALRYYV ARWLPESMES LTSEASSNKD LVETVVFLLP KVNRAMSYSS CSFLLKLLKV
SILVGADETV REDLVENVSL KLHEASVKDL LIHEVELVHR IVDQFMADEK RVSEDDRYKE
FVLGNGILLS VGRLIDAYLA LNSELTLSSF VELSELVPES ARPIHDGLYK AIDTFMKEHP
ELTKSEKKRL CGLMDVRKLT NEASTHAAQN ERLPLRVVVQ VLYFEQLRAN HSPVASVAAS
SHSPVEKTEE NKGEEATKKV ELSKKSRGSK STRSGGGAQL MPSRSRRIFE KIWPGKGEIS
NKSSEVSSGS SQSPPAKSSS SSSRRRRHSI S
