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FY_ARATH
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   03-AUG-2022, entry version 123.
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; 11.
DR   DIP; DIP-40405N; -.
DR   IntAct; Q6NLV4; 4.
DR   STRING; 3702.AT5G13480.2; -.
DR   PaxDb; Q6NLV4; -.
DR   PRIDE; Q6NLV4; -.
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   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   Gene3D; 2.130.10.10; -; 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; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR22836; PTHR22836; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 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
 
 
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