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HUA2_ARATH
ID   HUA2_ARATH              Reviewed;        1392 AA.
AC   Q9XER9;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 150.
DE   RecName: Full=ENHANCER OF AG-4 protein 2;
DE   AltName: Full=Protein AERIAL ROSETTE 1;
GN   Name=HUA2 {ECO:0000303|PubMed:10198637}; Synonyms=ART1;
GN   OrderedLocusNames=At5g23150 {ECO:0000312|Araport:AT5G23150};
GN   ORFNames=MKD15, MYJ24.14;
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 TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=10198637; DOI=10.1016/s1097-2765(00)80462-1;
RA   Chen X., Meyerowitz E.M.;
RT   "HUA1 and HUA2 are two members of the floral homeotic AGAMOUS pathway.";
RL   Mol. Cell 3:349-360(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT   features of the regions of 1,044,062 bp covered by thirteen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA   Takagi M.;
RT   "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION.
RX   PubMed=12530963; DOI=10.1016/s1534-5807(02)00399-4;
RA   Cheng Y., Kato N., Wang W., Li J., Chen X.;
RT   "Two RNA binding proteins, HEN4 and HUA1, act in the processing of AGAMOUS
RT   pre-mRNA in Arabidopsis thaliana.";
RL   Dev. Cell 4:53-66(2003).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15659097; DOI=10.1111/j.1365-313x.2004.02300.x;
RA   Doyle M.R., Bizzell C.M., Keller M.R., Michaels S.D., Song J., Noh Y.-S.,
RA   Amasino R.M.;
RT   "HUA2 is required for the expression of floral repressors in Arabidopsis
RT   thaliana.";
RL   Plant J. 41:376-385(2005).
RN   [8]
RP   VARIANT GLU-525.
RC   STRAIN=cv. Sy-0;
RX   PubMed=17764945; DOI=10.1016/j.cub.2007.07.059;
RA   Wang Q., Sajja U., Rosloski S., Humphrey T., Kim M.C., Bomblies K.,
RA   Weigel D., Grbic V.;
RT   "HUA2 caused natural variation in shoot morphology of A. thaliana.";
RL   Curr. Biol. 17:1513-1519(2007).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25070081; DOI=10.1111/tpj.12629;
RA   Jali S.S., Rosloski S.M., Janakirama P., Steffen J.G., Zhurov V.,
RA   Berleth T., Clark R.M., Grbic V.;
RT   "A plant-specific HUA2-LIKE (HULK) gene family in Arabidopsis thaliana is
RT   essential for development.";
RL   Plant J. 80:242-254(2014).
RN   [10]
RP   FUNCTION.
RX   PubMed=25425527; DOI=10.1111/nph.13177;
RA   Ilk N., Ding J., Ihnatowicz A., Koornneef M., Reymond M.;
RT   "Natural variation for anthocyanin accumulation under high-light and low-
RT   temperature stress is attributable to the ENHANCER OF AG-4 2 (HUA2) locus
RT   in combination with PRODUCTION OF ANTHOCYANIN PIGMENT1 (PAP1) and PAP2.";
RL   New Phytol. 206:422-435(2015).
CC   -!- FUNCTION: Transcription factor that functions as repressor of flowering
CC       by enhancing the expression of several genes that delay flowering
CC       including FLC, FLM/MAF1, MAF2 and SVP (PubMed:15659097). Also acts in
CC       the floral homeotic AGAMOUS (AG) pathway, specifically by processing
CC       the AGAMOUS pre-mRNA (PubMed:10198637, PubMed:12530963). Functions in
CC       association with HUA1 and HEN4 in AG pre-mRNA processing
CC       (PubMed:12530963). Involved in all three aspects of the AG functions,
CC       the specification of stamen and carpel identities, the control of
CC       floral determinacy, and the spatial restriction of AP1 expression
CC       (PubMed:10198637, PubMed:12530963, PubMed:15659097). Acts as
CC       transcription regulator that controls anthocyanin accumulation
CC       (PubMed:25425527). {ECO:0000269|PubMed:10198637,
CC       ECO:0000269|PubMed:12530963, ECO:0000269|PubMed:15659097,
CC       ECO:0000269|PubMed:25425527}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25070081}.
CC   -!- TISSUE SPECIFICITY: Expressed in the inflorescence meristem, floral
CC       primordia, inflorescence stem, and floral pedicels. Also detected in
CC       the shoot apical meristem, stems, leaves, embryos, and roots.
CC       {ECO:0000269|PubMed:10198637}.
CC   -!- DISRUPTION PHENOTYPE: Hua2 mutations enhance the phenotype of mild ag-4
CC       and elf4 alleles and also induce early flowering by reducing the
CC       expression of several MADS genes that act as floral repressors like
CC       FLC, FLM/MAF1, MAF2 and SVP. {ECO:0000269|PubMed:15659097}.
CC   -!- MISCELLANEOUS: In cv. Sy-0, a naturally occurring allele K525E, termed
CC       ART1, together with active FRI and FLC alleles causes delayed flowering
CC       of primary and axillary meristems, resulting in the distinctive Sy-0
CC       morphology (PubMed:17764945). {ECO:0000305|PubMed:17764945}.
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DR   EMBL; AF116556; AAD31171.1; -; mRNA.
DR   EMBL; AB007648; BAB11170.1; -; Genomic_DNA.
DR   EMBL; AB006708; BAB11170.1; JOINED; Genomic_DNA.
DR   EMBL; CP002688; AED93127.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM69147.1; -; Genomic_DNA.
DR   EMBL; AB493755; BAH30593.1; -; mRNA.
DR   PIR; T51947; T51947.
DR   RefSeq; NP_001330848.1; NM_001343792.1.
DR   RefSeq; NP_197706.1; NM_122221.3.
DR   AlphaFoldDB; Q9XER9; -.
DR   SMR; Q9XER9; -.
DR   BioGRID; 17654; 6.
DR   STRING; 3702.AT5G23150.1; -.
DR   iPTMnet; Q9XER9; -.
DR   PaxDb; Q9XER9; -.
DR   PRIDE; Q9XER9; -.
DR   ProteomicsDB; 230254; -.
DR   EnsemblPlants; AT5G23150.1; AT5G23150.1; AT5G23150.
DR   EnsemblPlants; AT5G23150.3; AT5G23150.3; AT5G23150.
DR   GeneID; 832379; -.
DR   Gramene; AT5G23150.1; AT5G23150.1; AT5G23150.
DR   Gramene; AT5G23150.3; AT5G23150.3; AT5G23150.
DR   KEGG; ath:AT5G23150; -.
DR   Araport; AT5G23150; -.
DR   TAIR; locus:2178292; AT5G23150.
DR   eggNOG; KOG1904; Eukaryota.
DR   HOGENOM; CLU_005040_0_0_1; -.
DR   InParanoid; Q9XER9; -.
DR   OMA; GKHENSP; -.
DR   OrthoDB; 143642at2759; -.
DR   PhylomeDB; Q9XER9; -.
DR   PRO; PR:Q9XER9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9XER9; baseline and differential.
DR   Genevisible; Q9XER9; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0043481; P:anthocyanin accumulation in tissues in response to UV light; IMP:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0048497; P:maintenance of floral organ identity; IMP:TAIR.
DR   GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR   GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR   GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:TAIR.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd05834; HDGF_related; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   InterPro; IPR006569; CID_dom.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR035496; HDGF-rel_PWWP.
DR   InterPro; IPR000313; PWWP_dom.
DR   Pfam; PF04818; CID; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SMART; SM00582; RPR; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   PROSITE; PS51391; CID; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Flowering; mRNA processing;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..1392
FT                   /note="ENHANCER OF AG-4 protein 2"
FT                   /id="PRO_0000418856"
FT   DOMAIN          20..77
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   DOMAIN          771..912
FT                   /note="CID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT   REGION          184..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          723..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1014..1356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1369..1392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..418
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..741
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..758
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1131
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1159..1185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1200..1287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1292..1306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         525
FT                   /note="K -> E (in strain: cv. Sy-0; causes late flowering
FT                   phenotype)"
FT                   /evidence="ECO:0000269|PubMed:17764945"
SQ   SEQUENCE   1392 AA;  151078 MW;  D2AC1B0D2AA70F0F CRC64;
     MAPGRKRGAS KAKAKGQLVL GDLVLAKVKG FPAWPAKISR PEDWDRAPDP KKYFVQFFGT
     EEIAFVAPPD IQAFTSEAKS KLLARCQGKT VKYFAQAVEQ ICTAFEGLQN HKSNALGDED
     SLDATEPGLT KAEIVDGTDH IVIESERTDN FNFRVDPCFP KLDENNGEER KAEIRKLDSS
     SFLESKVKTT SPVSESLEHS SFDPKIKKED FDKGTDGSAC NEHFGNGQKK LANGKRIKKE
     AGGSDRKGED TVHRDKSNNS HVPGGRTASG NSDSKKSKGL LTEKTSSKVS ADKHENSPGI
     KVGVSGKKRR LESEQGKLAP RVDESSRAAK KPRCESADNK VKCEIDDGSD STGTVSDIKR
     EIVLGLGARG GNFQYDKEAV AYTKRQRQTM EHATSPSFSG SRDKSGKGHL EQKDRSSPVR
     NVKAPAAQSL KKRRAVCIYD EDDDEDPKTP LHGKPAIVPQ AASVLTDGPK RANVCHSTST
     KAKISAGSTE STEVRKFPLR KHCEDASRVL PSNAENSTNS LPVVKPINEL PPKDVKQILQ
     SPKMSPQLVL TNKHVAGQHK VVKSSVKVSG VVMAKKPQSD SCKEAVAGSD KISSSQSQPA
     NQRHKSASVG ERLTVVSKAA SRLNDSGSRD MSEDLSAAML DLNREKGSAT FTSAKTPDSA
     ASMKDLIAAA QAKRKLAHTQ NSIFGNLNPS FLSISDTQGR SHSPFMVQNA SASAAISMPL
     VVQGHHQQGS SPSNHGHQSL SRNQIETDDN EERRLSSGHK SVGGSLSCST EAAISRDAFE
     GMLETLSRTR ESIGRATRLA IDCAKYGLAS EVVELLIRKL ESESHFHRKV DLFFLVDSIT
     QHSHSQKGIA GASYVPTVQA ALPRLLGAAA PPGTGASDNR RKCLKVLKLW LERKVFPESL
     LRRYIDDIRA SGDDATGGFS LRRPSRSERA VDDPIREMEG MLVDEYGSNA TFQLPGFFSS
     HNFEDDEEDD DLPTSQKEKS TSAGERVSAL DDLEIHDTSS DKCHRVLEDV DHELEMEDVS
     GQRKDVAPSS FCENKTKEQS LDVMEPVAEK STEFNPLPED SPPLPQESPP PLPPLPPSPP
     PPSPPLPPSS LPPPPPAALF PPLPPPPSQP PPPPLSPPPS PPPPPPPPSQ SLTTQLSIAS
     HHQIPFQPGF PPPTYPLSHQ TYPGSMQQDR SSIFTGDQIV QGPGNSSRGG LVEGAGKPEY
     FVQQSSSFSP AGVCSSREPS SFTSSRQLEF GNSDVLFNPE ASSQNHRFQP STPLSQRPMV
     RLPSAPSSHF SYPSHIQSQS QHSYTHPYPF PPQRDDARRY RNEEPWRIPS SGHSAENQNG
     AWIHGRNSHP GLPRVTDSFF RPPPERPPSG TMNYQPSAAS NLQAVPAIPG HTAPQMLPSR
     PDIPTVNCWR PA
 
 
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