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CONS_ARATH
ID   CONS_ARATH              Reviewed;         373 AA.
AC   Q39057; Q2V373;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Zinc finger protein CONSTANS {ECO:0000303|PubMed:7697715};
GN   Name=CO {ECO:0000303|PubMed:7697715};
GN   OrderedLocusNames=At5g15840 {ECO:0000312|Araport:AT5G15840};
GN   ORFNames=F14F8_220 {ECO:0000312|EMBL:CAC01783.1};
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] (ISOFORM 1), MUTAGENESIS OF ARG-59 AND
RP   96-LEU--ARG-98, AND MUTANTS CO-1 AND CO-2.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=7697715; DOI=10.1016/0092-8674(95)90288-0;
RA   Putterill J.J., Robson F., Lee K., Simon R., Coupland G.;
RT   "The CONSTANS gene of Arabidopsis promotes flowering and encodes a protein
RT   showing similarities to zinc finger transcription factors.";
RL   Cell 80:847-857(1995).
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] (ISOFORM 1).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION.
RX   PubMed=10834834; DOI=10.1126/science.288.5471.1613;
RA   Samach A., Onouchi H., Gold S.E., Ditta G.S., Schwarz-Sommer Z.,
RA   Yanofsky M.F., Coupland G.;
RT   "Distinct roles of CONSTANS target genes in reproductive development of
RT   Arabidopsis.";
RL   Science 288:1613-1616(2000).
RN   [7]
RP   FUNCTION.
RX   PubMed=11323677; DOI=10.1038/35074138;
RA   Suarez-Lopez P., Wheatley K., Robson F., Onouchi H., Valverde F.,
RA   Coupland G.;
RT   "CONSTANS mediates between the circadian clock and the control of flowering
RT   in Arabidopsis.";
RL   Nature 410:1116-1120(2001).
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=12692345; DOI=10.1104/pp.102.016188;
RA   Griffiths S., Dunford R.P., Coupland G., Laurie D.A.;
RT   "The evolution of CONSTANS-like gene families in barley, rice, and
RT   Arabidopsis.";
RL   Plant Physiol. 131:1855-1867(2003).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=15229176; DOI=10.1242/dev.01231;
RA   An H., Roussot C., Suarez-Lopez P., Corbesier L., Vincent C., Pineiro M.,
RA   Hepworth S., Mouradov A., Justin S., Turnbull C., Coupland G.;
RT   "CONSTANS acts in the phloem to regulate a systemic signal that induces
RT   photoperiodic flowering of Arabidopsis.";
RL   Development 131:3615-3626(2004).
RN   [10]
RP   INTERACTION WITH SPA1; SPA2; SPA3 AND SPA4, AND MUTAGENESIS OF
RP   214-VAL-PRO-215; 265-VAL-PRO-266 AND 370-VAL-PRO-371.
RX   PubMed=16854975; DOI=10.1242/dev.02481;
RA   Laubinger S., Marchal V., Le Gourrierec J., Wenkel S., Adrian J., Jang S.,
RA   Kulajta C., Braun H., Coupland G., Hoecker U.;
RT   "Arabidopsis SPA proteins regulate photoperiodic flowering and interact
RT   with the floral inducer CONSTANS to regulate its stability.";
RL   Development 133:3213-3222(2006).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH AS1.
RX   PubMed=21950734; DOI=10.1111/j.1365-313x.2011.04793.x;
RA   Song Y.H., Lee I., Lee S.Y., Imaizumi T., Hong J.C.;
RT   "CONSTANS and ASYMMETRIC LEAVES 1 complex is involved in the induction of
RT   FLOWERING LOCUS T in photoperiodic flowering in Arabidopsis.";
RL   Plant J. 69:332-342(2012).
RN   [12]
RP   INTERACTION WITH ADO3.
RX   PubMed=22628657; DOI=10.1126/science.1219644;
RA   Song Y.H., Smith R.W., To B.J., Millar A.J., Imaizumi T.;
RT   "FKF1 conveys timing information for CONSTANS stabilization in
RT   photoperiodic flowering.";
RL   Science 336:1045-1049(2012).
RN   [13]
RP   INTERACTION WITH PHL, AND SUBCELLULAR LOCATION.
RX   PubMed=24127609; DOI=10.1073/pnas.1310631110;
RA   Endo M., Tanigawa Y., Murakami T., Araki T., Nagatani A.;
RT   "PHYTOCHROME-DEPENDENT LATE-FLOWERING accelerates flowering through
RT   physical interactions with phytochrome B and CONSTANS.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:18017-18022(2013).
RN   [14]
RP   INTERACTION WITH NFYC9.
RX   PubMed=25105952; DOI=10.1038/ncomms5601;
RA   Hou X., Zhou J., Liu C., Liu L., Shen L., Yu H.;
RT   "Nuclear factor Y-mediated H3K27me3 demethylation of the SOC1 locus
RT   orchestrates flowering responses of Arabidopsis.";
RL   Nat. Commun. 5:4601-4601(2014).
RN   [15]
RP   INTERACTION WITH MRG1 AND MRG2.
RX   PubMed=25211338; DOI=10.1371/journal.pgen.1004617;
RA   Bu Z., Yu Y., Li Z., Liu Y., Jiang W., Huang Y., Dong A.W.;
RT   "Regulation of arabidopsis flowering by the histone mark readers MRG1/2 via
RT   interaction with CONSTANS to modulate FT expression.";
RL   PLoS Genet. 10:E1004617-E1004617(2014).
RN   [16]
RP   FUNCTION.
RX   PubMed=27255839; DOI=10.1038/nplants.2016.75;
RA   Zhu Y., Liu L., Shen L., Yu H.;
RT   "NaKR1 regulates long-distance movement of FLOWERING LOCUS T in
RT   Arabidopsis.";
RL   Nat. Plants 2:16075-16075(2016).
RN   [17]
RP   INTERACTION WITH MIP1A, AND SUBCELLULAR LOCATION.
RX   PubMed=27015278; DOI=10.1371/journal.pgen.1005959;
RA   Graeff M., Straub D., Eguen T., Dolde U., Rodrigues V., Brandt R.,
RA   Wenkel S.;
RT   "Microprotein-mediated recruitment of CONSTANS into a TOPLESS trimeric
RT   complex represses flowering in Arabidopsis.";
RL   PLoS Genet. 12:E1005959-E1005959(2016).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 290-357.
RX   PubMed=33693873; DOI=10.1093/plcell/koab016;
RA   Lv X., Zeng X., Hu H., Chen L., Zhang F., Liu R., Liu Y., Zhou X., Wang C.,
RA   Wu Z., Kim C., He Y., Du J.;
RT   "Structural insights into the multivalent binding of the Arabidopsis
RT   FLOWERING LOCUS T promoter by the CO-NF-Y master transcription factor
RT   complex.";
RL   Plant Cell 33:1182-1195(2021).
CC   -!- FUNCTION: Transcription factor that acts in the long day flowering
CC       pathway and may mediate between the circadian clock and the control of
CC       flowering. Plays a role in the regulation of flowering time by acting
CC       on 'SUPPRESSOR OF OVEREXPRESSION OF CO1', 'TERMINAL FLOWER 1' and
CC       'FLOWERING LOCUS T'. Also regulates P5CS2 and ACS10 (involved in
CC       proline and ethylene biosynthesis, respectively). Regulates the
CC       expression of NAKR1 by binding to the 5'-TGTG(N2-3)ATG-3' motif
CC       (PubMed:27255839). {ECO:0000269|PubMed:10834834,
CC       ECO:0000269|PubMed:11323677, ECO:0000269|PubMed:21950734,
CC       ECO:0000269|PubMed:27255839}.
CC   -!- SUBUNIT: Interacts with ADO3, SPA1, SPA2, SPA3 and SPA4
CC       (PubMed:16854975, PubMed:22628657). Interacts with MRG1 and MRG2 (via
CC       MRG domain) (PubMed:25211338). Interacts (via B-box) with MIP1A
CC       (PubMed:27015278). Interacts with AS1 to form a functional complex
CC       regulating FT expression (PubMed:21950734). Interacts with NFYC9
CC       (PubMed:25105952). Component of a red light-dependent nuclear complex
CC       made of PHL, PHYB and CO. Interacts directly with PHL in the presence
CC       of PHYB (PubMed:24127609). {ECO:0000269|PubMed:16854975,
CC       ECO:0000269|PubMed:21950734, ECO:0000269|PubMed:22628657,
CC       ECO:0000269|PubMed:24127609, ECO:0000269|PubMed:25105952,
CC       ECO:0000269|PubMed:25211338, ECO:0000269|PubMed:27015278}.
CC   -!- INTERACTION:
CC       Q39057; O82617: BBX23; NbExp=4; IntAct=EBI-1639724, EBI-15191793;
CC       Q39057; Q6NLH4: BBX29; NbExp=4; IntAct=EBI-1639724, EBI-15192709;
CC       Q39057; Q9LJB7: BBX32; NbExp=3; IntAct=EBI-1639724, EBI-4425264;
CC       Q39057; P43254: COP1; NbExp=8; IntAct=EBI-1639724, EBI-301649;
CC       Q39057; Q9LQT8: GAI; NbExp=4; IntAct=EBI-1639724, EBI-963606;
CC       Q39057; Q9SLG0: NFYB1; NbExp=6; IntAct=EBI-1639724, EBI-2126009;
CC       Q39057; Q9SMP0: NFYC1; NbExp=8; IntAct=EBI-1639724, EBI-2125944;
CC       Q39057; Q8L4B2: NFYC9; NbExp=3; IntAct=EBI-1639724, EBI-2466050;
CC       Q39057; Q9SLH3: RGA; NbExp=3; IntAct=EBI-1639724, EBI-963624;
CC       Q39057; Q39162: TGA4; NbExp=3; IntAct=EBI-1639724, EBI-541600;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24127609,
CC       ECO:0000269|PubMed:27015278}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q39057-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q39057-2; Sequence=VSP_036312, VSP_036313;
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, shoots and shoot apical
CC       meristem. Detected in the vascular tissue of the hypocotyl, the
CC       cotyledons and the leaves. Restricted to the protoxylem and phloem in
CC       young inflorescence stems and to the phloem only in older
CC       inflorescences. Also detected in the vascular tissue of the root.
CC       {ECO:0000269|PubMed:15229176}.
CC   -!- INDUCTION: Expressed with a circadian rhythm showing a broad peak
CC       between 12 hours and dawn. Higher expression under long days.
CC   -!- DOMAIN: The CCT domain is essential for the interaction with SPA1.
CC   -!- MISCELLANEOUS: The GIGANTEA-CONSTANS-FLOWER LOCUS T (GI-CO-FT) pathway
CC       to control photoperiodic flowering under LD is conserved between
CC       Arabidopsis and rice, but the regulation of the downstream gene by the
CC       upstream regulatory gene is reversed in the two species. In
CC       Arabidopsis, GI acts as an activator of CO, which in turn activates the
CC       floral activator FT under LD conditions. In rice, GI activates HD1/CO
CC       in a similar manner to that in Arabidopsis. However, under LD
CC       conditions, HD1 suppresses HD3A/FT expression, causing the suppression
CC       of flowering.
CC   -!- SIMILARITY: Belongs to the CONSTANS family. {ECO:0000305}.
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DR   EMBL; X94937; CAA64407.1; -; mRNA.
DR   EMBL; AL391144; CAC01783.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92213.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED92214.1; -; Genomic_DNA.
DR   EMBL; BT001926; AAN71925.1; -; mRNA.
DR   EMBL; AY086574; AAM63636.1; -; mRNA.
DR   PIR; A56133; A56133.
DR   RefSeq; NP_001031887.1; NM_001036810.2. [Q39057-2]
DR   RefSeq; NP_197088.1; NM_121589.2. [Q39057-1]
DR   PDB; 7CVO; X-ray; 2.60 A; A/F=290-357.
DR   PDB; 7CVQ; X-ray; 3.30 A; A/F/K/P=290-357.
DR   PDB; 7VSQ; X-ray; 2.70 A; A/B/C=10-110.
DR   PDB; 7WSJ; X-ray; 2.40 A; A/B/C=2-110.
DR   PDBsum; 7CVO; -.
DR   PDBsum; 7CVQ; -.
DR   PDBsum; 7VSQ; -.
DR   PDBsum; 7WSJ; -.
DR   AlphaFoldDB; Q39057; -.
DR   SMR; Q39057; -.
DR   BioGRID; 16717; 112.
DR   IntAct; Q39057; 97.
DR   MINT; Q39057; -.
DR   STRING; 3702.AT5G15840.1; -.
DR   PaxDb; Q39057; -.
DR   PRIDE; Q39057; -.
DR   EnsemblPlants; AT5G15840.1; AT5G15840.1; AT5G15840. [Q39057-1]
DR   EnsemblPlants; AT5G15840.2; AT5G15840.2; AT5G15840. [Q39057-2]
DR   GeneID; 831441; -.
DR   Gramene; AT5G15840.1; AT5G15840.1; AT5G15840. [Q39057-1]
DR   Gramene; AT5G15840.2; AT5G15840.2; AT5G15840. [Q39057-2]
DR   KEGG; ath:AT5G15840; -.
DR   Araport; AT5G15840; -.
DR   TAIR; locus:2143206; AT5G15840.
DR   eggNOG; KOG1601; Eukaryota.
DR   HOGENOM; CLU_028225_3_2_1; -.
DR   InParanoid; Q39057; -.
DR   OMA; YRMQEQH; -.
DR   PhylomeDB; Q39057; -.
DR   PRO; PR:Q39057; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q39057; baseline and differential.
DR   Genevisible; Q39057; AT.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IPI:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0010018; P:far-red light signaling pathway; IMP:TAIR.
DR   GO; GO:0009908; P:flower development; IMP:TAIR.
DR   GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR   GO; GO:0010218; P:response to far red light; IMP:TAIR.
DR   InterPro; IPR010402; CCT_domain.
DR   InterPro; IPR045281; CONSTANS-like.
DR   InterPro; IPR000315; Znf_B-box.
DR   PANTHER; PTHR31319; PTHR31319; 1.
DR   Pfam; PF06203; CCT; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   SMART; SM00336; BBOX; 2.
DR   PROSITE; PS51017; CCT; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Developmental protein; Differentiation;
KW   DNA-binding; Flowering; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..373
FT                   /note="Zinc finger protein CONSTANS"
FT                   /id="PRO_0000113277"
FT   DOMAIN          306..348
FT                   /note="CCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00357"
FT   ZN_FING         15..57
FT                   /note="B box-type 1; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   ZN_FING         58..108
FT                   /note="B box-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          109..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   VAR_SEQ         255..274
FT                   /note="AYISSMETGVVPESTACVTT -> VRLLYICYPFNLASSHNAAG (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036312"
FT   VAR_SEQ         275..373
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036313"
FT   MUTAGEN         59
FT                   /note="R->H: In co-2; late-flowering under long day
FT                   condition."
FT                   /evidence="ECO:0000269|PubMed:7697715"
FT   MUTAGEN         96..98
FT                   /note="Missing: In co-1; late-flowering under long day
FT                   condition."
FT                   /evidence="ECO:0000269|PubMed:7697715"
FT   MUTAGEN         214..215
FT                   /note="VP->AA: In COmVP1-3; no effect on binding to SPA1;
FT                   when associated with 265-A-A-266 and 370-A-A-371."
FT                   /evidence="ECO:0000269|PubMed:16854975"
FT   MUTAGEN         265..266
FT                   /note="VP->AA: In COmVP1-3; no effect on binding to SPA1;
FT                   when associated with 214-A-A-215 and 370-A-A-371."
FT                   /evidence="ECO:0000269|PubMed:16854975"
FT   MUTAGEN         370..371
FT                   /note="VP->AA: In COmVP1-3; no effect on binding to SPA1;
FT                   when associated with 214-A-A-215 and 265-A-A-266."
FT                   /evidence="ECO:0000269|PubMed:16854975"
FT   HELIX           303..316
FT                   /evidence="ECO:0007829|PDB:7CVO"
FT   HELIX           317..319
FT                   /evidence="ECO:0007829|PDB:7CVO"
FT   HELIX           329..335
FT                   /evidence="ECO:0007829|PDB:7CVO"
SQ   SEQUENCE   373 AA;  41986 MW;  56C84CF9CD45E4A6 CRC64;
     MLKQESNDIG SGENNRARPC DTCRSNACTV YCHADSAYLC MSCDAQVHSA NRVASRHKRV
     RVCESCERAP AAFLCEADDA SLCTACDSEV HSANPLARRH QRVPILPISG NSFSSMTTTH
     HQSEKTMTDP EKRLVVDQEE GEEGDKDAKE VASWLFPNSD KNNNNQNNGL LFSDEYLNLV
     DYNSSMDYKF TGEYSQHQQN CSVPQTSYGG DRVVPLKLEE SRGHQCHNQQ NFQFNIKYGS
     SGTHYNDNGS INHNAYISSM ETGVVPESTA CVTTASHPRT PKGTVEQQPD PASQMITVTQ
     LSPMDREARV LRYREKRKTR KFEKTIRYAS RKAYAEIRPR VNGRFAKREI EAEEQGFNTM
     LMYNTGYGIV PSF
 
 
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