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SEP1_ARATH
ID   SEP1_ARATH              Reviewed;         251 AA.
AC   P29382; Q9LFU6;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Developmental protein SEPALLATA 1;
DE   AltName: Full=Agamous-like MADS-box protein AGL2;
GN   Name=SEP1; Synonyms=AGL2; OrderedLocusNames=At5g15800; ORFNames=F14F8_180;
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].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=1672119; DOI=10.1101/gad.5.3.484;
RA   Ma H., Yanofsky M.F., Meyerowitz E.M.;
RT   "AGL1-AGL6, an Arabidopsis gene family with similarity to floral homeotic
RT   and transcription factor genes.";
RL   Genes Dev. 5:484-495(1991).
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;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
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   [6]
RP   CHARACTERIZATION.
RX   PubMed=9418042; DOI=10.1046/j.1365-313x.1997.12050999.x;
RA   Fan H.-Y., Hu Y., Tudor M., Ma H.;
RT   "Specific interactions between the K domains of AG and AGLs, members of the
RT   MADS domain family of DNA binding proteins.";
RL   Plant J. 12:999-1010(1997).
RN   [7]
RP   CHARACTERIZATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10821278; DOI=10.1038/35012103;
RA   Pelaz S., Ditta G.S., Baumann E., Wisman E., Yanofsky M.F.;
RT   "B and C floral organ identity functions require SEPALLATA MADS-box
RT   genes.";
RL   Nature 405:200-203(2000).
RN   [8]
RP   INTERACTION WITH TT16/AGL32.
RX   PubMed=16080001; DOI=10.1007/s00438-005-0010-y;
RA   Kaufmann K., Anfang N., Saedler H., Theissen G.;
RT   "Mutant analysis, protein-protein interactions and subcellular localization
RT   of the Arabidopsis B sister (ABS) protein.";
RL   Mol. Genet. Genomics 274:103-118(2005).
RN   [9]
RP   INTERACTION WITH AGL16.
RX   PubMed=15805477; DOI=10.1105/tpc.105.031831;
RA   de Folter S., Immink R.G.H., Kieffer M., Parenicova L., Henz S.R.,
RA   Weigel D., Busscher M., Kooiker M., Colombo L., Kater M.M., Davies B.,
RA   Angenent G.C.;
RT   "Comprehensive interaction map of the Arabidopsis MADS Box transcription
RT   factors.";
RL   Plant Cell 17:1424-1433(2005).
CC   -!- FUNCTION: Probable transcription factor. Functions with SEPALLATA2/AGL4
CC       and SEPALLATA3/AGL9 to ensure proper development of petals, stamens and
CC       carpels, and to prevent the indeterminate growth of the flower
CC       meristem. Forms a heterodimer via the K-box domain with AGAMOUS, that
CC       could be involved in genes regulation during floral meristem
CC       development.
CC   -!- SUBUNIT: Heterodimer with AGAMOUS capable of binding to CArG-box
CC       sequences. Interacts with AGL16 (PubMed:15805477). Interacts with
CC       TT16/AGL32 (PubMed:16080001). {ECO:0000269|PubMed:15805477,
CC       ECO:0000269|PubMed:16080001}.
CC   -!- INTERACTION:
CC       P29382; O82794: AGL24; NbExp=3; IntAct=EBI-632935, EBI-592083;
CC       P29382; P29385: AGL5; NbExp=3; IntAct=EBI-632935, EBI-621949;
CC       P29382; P35631: AP1; NbExp=4; IntAct=EBI-632935, EBI-592003;
CC       P29382; Q9M0U1: ARF46; NbExp=3; IntAct=EBI-632935, EBI-15194131;
CC       P29382; Q9LV59: At3g24490; NbExp=3; IntAct=EBI-632935, EBI-15191981;
CC       P29382; F4KCU5: TT16; NbExp=3; IntAct=EBI-632935, EBI-15197443;
CC       P29382; Q8RYD9: TT16; NbExp=3; IntAct=EBI-632935, EBI-621993;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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=P29382-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in carpels, and weakly in stamens.
CC   -!- DEVELOPMENTAL STAGE: Expressed early during flower development.
CC   -!- DISRUPTION PHENOTYPE: Triple mutations in the SEP1, SEP2 and SEP3 genes
CC       result in the replacement of the stamens and petals by sepals and of
CC       the carpels by a new mutant flower with sepaloid organs.
CC       {ECO:0000269|PubMed:10821278}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC01779.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; M55551; AAA32732.1; -; mRNA.
DR   EMBL; AL391144; CAC01779.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92207.1; -; Genomic_DNA.
DR   EMBL; AK118608; BAC43207.1; -; mRNA.
DR   EMBL; BT006224; AAP12873.1; -; mRNA.
DR   PIR; B39534; B39534.
DR   PIR; T51409; T51409.
DR   RefSeq; NP_001119230.1; NM_001125758.2.
DR   RefSeq; NP_568322.1; NM_121585.4. [P29382-1]
DR   AlphaFoldDB; P29382; -.
DR   SMR; P29382; -.
DR   BioGRID; 16712; 29.
DR   DIP; DIP-34935N; -.
DR   IntAct; P29382; 28.
DR   STRING; 3702.AT5G15800.2; -.
DR   PaxDb; P29382; -.
DR   PRIDE; P29382; -.
DR   ProteomicsDB; 234483; -. [P29382-1]
DR   EnsemblPlants; AT5G15800.1; AT5G15800.1; AT5G15800. [P29382-1]
DR   GeneID; 831436; -.
DR   Gramene; AT5G15800.1; AT5G15800.1; AT5G15800. [P29382-1]
DR   KEGG; ath:AT5G15800; -.
DR   Araport; AT5G15800; -.
DR   eggNOG; KOG0014; Eukaryota.
DR   HOGENOM; CLU_053053_0_2_1; -.
DR   InParanoid; P29382; -.
DR   OMA; LAWDNIG; -.
DR   OrthoDB; 1039681at2759; -.
DR   PhylomeDB; P29382; -.
DR   PRO; PR:P29382; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P29382; baseline and differential.
DR   Genevisible; P29382; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0048481; P:plant ovule development; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00265; MADS_MEF2_like; 1.
DR   Gene3D; 3.40.1810.10; -; 1.
DR   InterPro; IPR033896; MADS_MEF2-like.
DR   InterPro; IPR002487; TF_Kbox.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   Pfam; PF01486; K-box; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SSF55455; 1.
DR   PROSITE; PS51297; K_BOX; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Coiled coil; Developmental protein;
KW   Differentiation; DNA-binding; Flowering; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..251
FT                   /note="Developmental protein SEPALLATA 1"
FT                   /id="PRO_0000199483"
FT   DOMAIN          3..57
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT   DOMAIN          88..178
FT                   /note="K-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00629"
FT   COILED          85..176
FT                   /evidence="ECO:0000255"
FT   CONFLICT        184..186
FT                   /note="Missing (in Ref. 1; AAA32732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="Q -> P (in Ref. 1; AAA32732)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   251 AA;  28657 MW;  867906D8D657621E CRC64;
     MGRGRVELKR IENKINRQVT FAKRRNGLLK KAYELSVLCD AEVALIIFSN RGKLYEFCSS
     SNMLKTLDRY QKCSYGSIEV NNKPAKELEN SYREYLKLKG RYENLQRQQR NLLGEDLGPL
     NSKELEQLER QLDGSLKQVR SIKTQYMLDQ LSDLQNKEQM LLETNRALAM KLDDMIGVRS
     HHMGGGGGWE GGEQNVTYAH HQAQSQGLYQ PLECNPTLQM GYDNPVCSEQ ITATTQAQAQ
     QGNGYIPGWM L
 
 
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