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SWI3C_ARATH
ID   SWI3C_ARATH             Reviewed;         807 AA.
AC   Q9XI07;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=SWI/SNF complex subunit SWI3C;
DE            Short=AtSWI3C;
DE   AltName: Full=Transcription regulatory protein SWI3C;
GN   Name=SWI3C; Synonyms=CHB4; OrderedLocusNames=At1g21700; ORFNames=F8K7.13;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
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   [3]
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   [4]
RP   INTERACTION WITH SWI3B.
RX   PubMed=12140326; DOI=10.1093/nar/gkf458;
RA   Sarnowski T.J., Swiezewski S., Pawlikowska K., Kaczanowski S.,
RA   Jerzmanowski A.;
RT   "AtSWI3B, an Arabidopsis homolog of SWI3, a core subunit of yeast Swi/Snf
RT   chromatin remodeling complex, interacts with FCA, a regulator of flowering
RT   time.";
RL   Nucleic Acids Res. 30:3412-3421(2002).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=14682613; DOI=10.1023/b:plan.0000004305.60407.8b;
RA   Zhou C., Miki B., Wu K.;
RT   "CHB2, a member of the SWI3 gene family, is a global regulator in
RT   Arabidopsis.";
RL   Plant Mol. Biol. 52:1125-1134(2003).
RN   [6]
RP   INTERACTION WITH BRM.
RX   PubMed=15371304; DOI=10.1242/dev.01363;
RA   Farrona S., Hurtado L., Bowman J.L., Reyes J.C.;
RT   "The Arabidopsis thaliana SNF2 homolog AtBRM controls shoot development and
RT   flowering.";
RL   Development 131:4965-4975(2004).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH SWI3A AND BSH.
RX   PubMed=16055636; DOI=10.1105/tpc.105.031203;
RA   Sarnowski T.J., Rios G., Jasik J., Swiezewski S., Kaczanowski S., Li Y.,
RA   Kwiatkowska A., Pawlikowska K., Kozbial M., Kozbial P., Koncz C.,
RA   Jerzmanowski A.;
RT   "SWI3 subunits of putative SWI/SNF chromatin-remodeling complexes play
RT   distinct roles during Arabidopsis development.";
RL   Plant Cell 17:2454-2472(2005).
RN   [8]
RP   INTERACTION WITH MORC6 AND SUVH9.
RX   PubMed=27171427; DOI=10.1371/journal.pgen.1006026;
RA   Liu Z.-W., Zhou J.-X., Huang H.-W., Li Y.-Q., Shao C.-R., Li L., Cai T.,
RA   Chen S., He X.-J.;
RT   "Two components of the RNA-Directed DNA methylation pathway associate with
RT   MORC6 and silence loci targeted by MORC6 in Arabidopsis.";
RL   PLoS Genet. 12:E1006026-E1006026(2016).
CC   -!- FUNCTION: Component of a multiprotein complex equivalent of the SWI/SNF
CC       complex, an ATP-dependent chromatin-remodeling complex, which is
CC       required for the positive and negative regulation of gene expression of
CC       a large number of genes. It changes chromatin structure by altering
CC       DNA-histone contacts within a nucleosome, leading eventually to a
CC       change in nucleosome position, thus facilitating or repressing binding
CC       of gene-specific transcription factors. {ECO:0000269|PubMed:14682613,
CC       ECO:0000269|PubMed:16055636}.
CC   -!- SUBUNIT: Heterodimer. Interacts with SWI3A, SWI3B and BRM, but not with
CC       BSH. Interacts with MORC6 and SUVH9 (PubMed:27171427).
CC       {ECO:0000269|PubMed:12140326, ECO:0000269|PubMed:15371304,
CC       ECO:0000269|PubMed:16055636, ECO:0000269|PubMed:27171427}.
CC   -!- INTERACTION:
CC       Q9XI07; Q84JG2: SWI3B; NbExp=4; IntAct=EBI-1102300, EBI-1102271;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:14682613}.
CC   -!- DISRUPTION PHENOTYPE: Plants are viable but have alterations in leaf,
CC       root and flower development, and are early flowering.
CC       {ECO:0000269|PubMed:16055636}.
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DR   EMBL; AC007727; AAD41423.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30144.1; -; Genomic_DNA.
DR   EMBL; AY091026; AAM13847.1; -; mRNA.
DR   EMBL; AY117245; AAM51320.1; -; mRNA.
DR   PIR; D86350; D86350.
DR   RefSeq; NP_173589.1; NM_102019.4.
DR   AlphaFoldDB; Q9XI07; -.
DR   BioGRID; 24013; 163.
DR   DIP; DIP-37816N; -.
DR   IntAct; Q9XI07; 4.
DR   STRING; 3702.AT1G21700.1; -.
DR   iPTMnet; Q9XI07; -.
DR   PaxDb; Q9XI07; -.
DR   PRIDE; Q9XI07; -.
DR   ProteomicsDB; 226556; -.
DR   EnsemblPlants; AT1G21700.1; AT1G21700.1; AT1G21700.
DR   GeneID; 838774; -.
DR   Gramene; AT1G21700.1; AT1G21700.1; AT1G21700.
DR   KEGG; ath:AT1G21700; -.
DR   Araport; AT1G21700; -.
DR   TAIR; locus:2036942; AT1G21700.
DR   eggNOG; KOG1279; Eukaryota.
DR   HOGENOM; CLU_004447_4_1_1; -.
DR   InParanoid; Q9XI07; -.
DR   OMA; CFLQGRM; -.
DR   OrthoDB; 683891at2759; -.
DR   PhylomeDB; Q9XI07; -.
DR   PRO; PR:Q9XI07; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XI07; baseline and differential.
DR   Genevisible; Q9XI07; AT.
DR   GO; GO:0016514; C:SWI/SNF complex; ISS:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:TAIR.
DR   CDD; cd00167; SANT; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR032451; SMARCC_C.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   Pfam; PF16495; SWIRM-assoc_1; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS51293; SANT; 1.
DR   PROSITE; PS50934; SWIRM; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Coiled coil; Developmental protein;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..807
FT                   /note="SWI/SNF complex subunit SWI3C"
FT                   /id="PRO_0000344529"
FT   DOMAIN          176..274
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT   DOMAIN          398..449
FT                   /note="SANT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   ZN_FING         340..394
FT                   /note="ZZ-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          458..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..807
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          598..656
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        30..53
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         345
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         348
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         368
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT   BINDING         371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ   SEQUENCE   807 AA;  88250 MW;  DAB17C104E4B287F CRC64;
     MPASEDRRGK WKRKKRGGLS AARKPKQEEE DMEEEDEENN NNNNEEMDDV ENADELQQNG
     GATPDPGLGI GEVVEDSGSR ISDFPAVVKR VVIRPHASVM AVVAAERAGL IGETRGQGSL
     PALENISFGQ LQALSTVPAD SLDLERSDGS SSAYVISPPP IMDGEGVVKR FGDLVHVLPM
     HSDWFAPNTV DRLERQVVPQ FFSGKSPNHT PESYMEFRNA IVSKYVENPE KTLTISDCQG
     LVDGVDIEDF ARVFRFLDHW GIINYCATAQ SHPGPLRDVS DVREDTNGEV NVPSAALTSI
     DSLIKFDKPN CRHKGGEVYS SLPSLDGDSP DLDIRIREHL CDSHCNHCSR PLPTVYFQSQ
     KKGDILLCCD CFHHGRFVVG HSCLDFVRVD PMKFYGDQDG DNWTDQETLL LLEAVELYNE
     NWVQIADHVG SKSKAQCILH FLRLPVEDGL LDNVEVSGVT NTENPTNGYD HKGTDSNGDL
     PGYSEQGSDT EIKLPFVKSP NPVMALVAFL ASAVGPRVAA SCAHESLSVL SEDDRMKSEG
     MQGKEASLLD GENQQQDGAH KTSSQNGAEA QTPLPQDKVM AAFRAGLSAA ATKAKLFADH
     EEREIQRLSA NIVNHQLKRM ELKLKQFAEI ETLLMKECEQ VEKTRQRFSA ERARMLSARF
     GSPGGISPQT NNLQGMSLST GGNNINSLMH QQHQQQQASA TSQPSIIPGF SNNPQVQAQM
     HFMARQQQQQ QQQQQQQQQA FSFGPRLPLN AIQTNAGSTA SPNVMFGNNQ LNNPAAAGAA
     SINQPSFSHP MVRSSTGSGS GSGLGLN
 
 
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