ID FY_ARATH Reviewed; 647 AA.
AC Q6NLV4; Q9FY53;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 130.
DE RecName: Full=Flowering time control protein FY;
GN Name=FY; OrderedLocusNames=At5g13480; ORFNames=T6I14.10;
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, AND INTERACTION WITH FCA.
RX PubMed=12809608; DOI=10.1016/s0092-8674(03)00425-2;
RA Simpson G.G., Dijkwel P.P., Quesada V., Henderson I., Dean C.;
RT "FY is an RNA 3' end-processing factor that interacts with FCA to control
RT the Arabidopsis floral transition.";
RL Cell 113:777-787(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH FCA, MUTAGENESIS OF
RP GLY-141; 488-PRO--PRO-494 AND 632-PRO--PRO-639, DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RX PubMed=16033802; DOI=10.1242/dev.01924;
RA Henderson I.R., Liu F., Drea S., Simpson G.G., Dean C.;
RT "An allelic series reveals essential roles for FY in plant development in
RT addition to flowering-time control.";
RL Development 132:3597-3607(2005).
RN [6]
RP INTERACTION WITH CPSF73-I; CPSF73-II; CPSF100 AND CPSF160.
RX PubMed=19748916; DOI=10.1104/pp.109.142729;
RA Zhao H., Xing D., Li Q.Q.;
RT "Unique features of plant cleavage and polyadenylation specificity factor
RT revealed by proteomic studies.";
RL Plant Physiol. 151:1546-1556(2009).
RN [7]
RP INTERACTION WITH CPSF100 AND CPSF160, AND MUTAGENESIS OF PRO-488 AND
RP PRO-489.
RX PubMed=19439664; DOI=10.1073/pnas.0903444106;
RA Manzano D., Marquardt S., Jones A.M., Baurle I., Liu F., Dean C.;
RT "Altered interactions within FY/AtCPSF complexes required for Arabidopsis
RT FCA-mediated chromatin silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8772-8777(2009).
CC -!- FUNCTION: Plays a role in the regulation of flowering time in the
CC autonomous flowering pathway by decreasing FLOWERING LOCUS C mRNA
CC levels. Required for the negative autoregulation of FCA expression.
CC Acts probably as an RNA 3' end-processing factor. Required for growth
CC and development in plants. {ECO:0000269|PubMed:12809608,
CC ECO:0000269|PubMed:16033802}.
CC -!- SUBUNIT: Interacts transiently (via the PPLPP motifs) with FCA (via the
CC WW domain). Interacts with CPSF73-I, CPSF73-II, CPSF100 and CPSF160 in
CC the CPSF complex. The FCA/FY interaction leads to changes in FY/CPSF
CC complex composition. {ECO:0000269|PubMed:12809608,
CC ECO:0000269|PubMed:16033802, ECO:0000269|PubMed:19439664,
CC ECO:0000269|PubMed:19748916}.
CC -!- INTERACTION:
CC Q6NLV4; Q9LKF9: CPSF100; NbExp=3; IntAct=EBI-1632908, EBI-1775444;
CC Q6NLV4; Q9FGR0: CPSF160; NbExp=2; IntAct=EBI-1632908, EBI-1775436;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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=Q6NLV4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in embryos, in shoot and root meristems
CC and in the vasculature. {ECO:0000269|PubMed:16033802}.
CC -!- DEVELOPMENTAL STAGE: At globular stage, expressed throughout the
CC embryo, endosperm and surrounding maternal seed tissue. From the heart-
CC stage, expression restricted to the embryo and the funiculus.
CC {ECO:0000269|PubMed:16033802}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000269|PubMed:16033802}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391710; CAC05425.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91899.1; -; Genomic_DNA.
DR EMBL; BT012225; AAS76712.1; -; mRNA.
DR RefSeq; NP_196852.3; NM_121351.5. [Q6NLV4-1]
DR AlphaFoldDB; Q6NLV4; -.
DR SMR; Q6NLV4; -.
DR BioGRID; 16469; 12.
DR DIP; DIP-40405N; -.
DR IntAct; Q6NLV4; 4.
DR STRING; 3702.Q6NLV4; -.
DR PaxDb; 3702-AT5G13480-2; -.
DR ProteomicsDB; 230555; -. [Q6NLV4-1]
DR EnsemblPlants; AT5G13480.1; AT5G13480.1; AT5G13480. [Q6NLV4-1]
DR GeneID; 831191; -.
DR Gramene; AT5G13480.1; AT5G13480.1; AT5G13480. [Q6NLV4-1]
DR KEGG; ath:AT5G13480; -.
DR Araport; AT5G13480; -.
DR TAIR; AT5G13480; FY.
DR eggNOG; KOG0284; Eukaryota.
DR InParanoid; Q6NLV4; -.
DR PhylomeDB; Q6NLV4; -.
DR PRO; PR:Q6NLV4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q6NLV4; baseline and differential.
DR Genevisible; Q6NLV4; AT.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR045245; Pfs2-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR22836:SF0; PRE-MRNA 3' END PROCESSING PROTEIN WDR33; 1.
DR PANTHER; PTHR22836; WD40 REPEAT PROTEIN; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation; Flowering;
KW Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..647
FT /note="Flowering time control protein FY"
FT /id="PRO_0000391779"
FT REPEAT 121..160
FT /note="WD 1"
FT REPEAT 163..202
FT /note="WD 2"
FT REPEAT 205..244
FT /note="WD 3"
FT REPEAT 247..286
FT /note="WD 4"
FT REPEAT 289..328
FT /note="WD 5"
FT REPEAT 331..371
FT /note="WD 6"
FT REPEAT 375..414
FT /note="WD 7"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 488..492
FT /note="PPLPP motif 1"
FT MOTIF 632..636
FT /note="PPLPP motif 2"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..558
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 141
FT /note="G->S: In fy-3; late flowering."
FT /evidence="ECO:0000269|PubMed:16033802"
FT MUTAGEN 488..494
FT /note="PPLPPGP->AAAAAAA: No effect on FCA binding; when
FT associated with 632-AAAAAGAA-639, loss of binding to FCA."
FT /evidence="ECO:0000269|PubMed:16033802"
FT MUTAGEN 488
FT /note="P->S: Increased FLC levels and late flowering."
FT /evidence="ECO:0000269|PubMed:19439664"
FT MUTAGEN 489
FT /note="P->S: Increased FLC levels and late flowering."
FT /evidence="ECO:0000269|PubMed:19439664"
FT MUTAGEN 632..639
FT /note="PPLPPGPP->AAAAAGAA: No effect on FCA binding; when
FT associated with 488-AAAAAAA-494, loss of binding to FCA."
FT /evidence="ECO:0000269|PubMed:16033802"
SQ SEQUENCE 647 AA; 72242 MW; 74569D2178BEA5C7 CRC64;
MYAGGDMHRG SQMPQPPMMR QSSASSTNIN PDYHHPSGPF DPNVDSFGAK RMRKHTQRRA
VDYTSTVVRY IQARTWQRDS RDRTTLQPTP AAAVDMLPTV AYSDNPSTSF AAKFVHASLN
KNRCSINRVL WTPSGRRLIT GSQSGEFTLW NGQSFNFEMI LQAHDQPIRS MVWSHNENYM
VSGDDGGTLK YWQNNMNNVK ANKTAHKESI RDLSFCKTDL KFCSCSDDTT VKVWDFTKCV
DESSLTGHGW DVKSVDWHPT KSLLVSGGKD QLVKLWDTRS GRELCSLHGH KNIVLSVKWN
QNGNWLLTAS KDQIIKLYDI RTMKELQSFR GHTKDVTSLA WHPCHEEYFV SGSSDGSICH
WIVGHENPQI EIPNAHDNSV WDLAWHPIGY LLCSGSNDHT TKFWCRNRPA DNPRDVLMQN
QGYNEQGFGR QPDNFQPSEA SPIPGAFVPG LTRNEGTIPG IGIAMPFDAS SQGDHKQPLP
GSMALGAPPL PPGPHPSLLG SGQQQGYQQQ QQHQGHPQQM LPMPNMPHHQ LPPSSHMPLH
PHHLPRPMQM PPHGHMPPPS MPMSHQMPGS MGMQGGMNPQ MSQSHFMGAP SGVFQGQPNS
GGPQMYPQGR GGFNRPQMIP GYNNPFQQQQ QPPLPPGPPP NNNQQHQ
//
