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STI_ARATH
ID   STI_ARATH               Reviewed;        1218 AA.
AC   O64728; Q9LKQ4;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Protein STICHEL;
GN   Name=STI; OrderedLocusNames=At2g02480; ORFNames=T8K22.22;
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. Columbia;
RA   Marks M.D., Prigge M., Shi H.;
RT   "The Arabidopsis STI gene is a member of the replication factor C-like gene
RT   family.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   DISRUPTION PHENOTYPE, AND MUTANT STICHEL.
RX   PubMed=8313475; DOI=10.1016/0092-8674(94)90118-x;
RA   Huelskamp M., Misra S., Juergens G.;
RT   "Genetic dissection of trichome cell development in Arabidopsis.";
RL   Cell 76:555-566(1994).
RN   [5]
RP   FUNCTION.
RX   PubMed=9367433; DOI=10.1242/dev.124.19.3779;
RA   Folkers U., Berger J., Huelskamp M.;
RT   "Cell morphogenesis of trichomes in Arabidopsis: differential control of
RT   primary and secondary branching by branch initiation regulators and cell
RT   growth.";
RL   Development 124:3779-3786(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=10572032; DOI=10.1242/dev.126.24.5547;
RA   Luo D., Oppenheimer D.G.;
RT   "Genetic control of trichome branch number in Arabidopsis: the roles of the
RT   FURCA loci.";
RL   Development 126:5547-5557(1999).
RN   [7]
RP   GENE FAMILY, PEST MOTIF, NUCLEAR LOCALIZATION SIGNAL, DISRUPTION PHENOTYPE,
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12586888; DOI=10.1104/pp.014209;
RA   Ilgenfritz H., Bouyer D., Schnittger A., Mathur J., Kirik V., Schwab B.,
RA   Chua N.H., Juergens G., Huelskamp M.;
RT   "The Arabidopsis STICHEL gene is a regulator of trichome branch number and
RT   encodes a novel protein.";
RL   Plant Physiol. 131:643-655(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=18477400; DOI=10.1186/1471-2229-8-54;
RA   Exner V., Gruissem W., Hennig L.;
RT   "Control of trichome branching by chromatin assembly factor-1.";
RL   BMC Plant Biol. 8:54-54(2008).
RN   [9]
RP   INTERACTION WITH BLT.
RX   PubMed=21558384; DOI=10.1242/dev.058982;
RA   Kasili R., Huang C.C., Walker J.D., Simmons L.A., Zhou J., Faulk C.,
RA   Huelskamp M., Larkin J.C.;
RT   "BRANCHLESS TRICHOMES links cell shape and cell cycle control in
RT   Arabidopsis trichomes.";
RL   Development 138:2379-2388(2011).
RN   [10]
RP   INDUCTION BY GA3, AND FUNCTION.
RX   PubMed=22210898; DOI=10.1093/pcp/pcr192;
RA   An L., Zhou Z., Su S., Yan A., Gan Y.;
RT   "GLABROUS INFLORESCENCE STEMS (GIS) is required for trichome branching
RT   through gibberellic acid signaling in Arabidopsis.";
RL   Plant Cell Physiol. 53:457-469(2012).
CC   -!- FUNCTION: Acts as a key regulator of trichome branching through an
CC       endoreduplication-independent pathway. {ECO:0000269|PubMed:10572032,
CC       ECO:0000269|PubMed:12586888, ECO:0000269|PubMed:18477400,
CC       ECO:0000269|PubMed:22210898, ECO:0000269|PubMed:9367433}.
CC   -!- SUBUNIT: Interacts with BLT. {ECO:0000269|PubMed:21558384}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12586888}.
CC   -!- INDUCTION: By gibberellin A3 (GA3). {ECO:0000269|PubMed:22210898}.
CC   -!- DOMAIN: PEST motif is known to mediate rapid protein degradation.
CC   -!- DISRUPTION PHENOTYPE: Shows trichomes with exclusively no branching.
CC       {ECO:0000269|PubMed:12586888, ECO:0000269|PubMed:8313475}.
CC   -!- SIMILARITY: Belongs to the DnaX/STICHEL family. {ECO:0000305}.
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DR   EMBL; AF264023; AAF82285.1; -; mRNA.
DR   EMBL; AC004136; AAC18938.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05585.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62557.1; -; Genomic_DNA.
DR   PIR; T00615; T00615.
DR   RefSeq; NP_001324706.1; NM_001335120.1.
DR   RefSeq; NP_565285.1; NM_126303.3.
DR   AlphaFoldDB; O64728; -.
DR   SMR; O64728; -.
DR   BioGRID; 180; 2.
DR   IntAct; O64728; 1.
DR   STRING; 3702.AT2G02480.1; -.
DR   iPTMnet; O64728; -.
DR   PaxDb; O64728; -.
DR   PRIDE; O64728; -.
DR   ProteomicsDB; 228423; -.
DR   EnsemblPlants; AT2G02480.1; AT2G02480.1; AT2G02480.
DR   EnsemblPlants; AT2G02480.2; AT2G02480.2; AT2G02480.
DR   GeneID; 814777; -.
DR   Gramene; AT2G02480.1; AT2G02480.1; AT2G02480.
DR   Gramene; AT2G02480.2; AT2G02480.2; AT2G02480.
DR   KEGG; ath:AT2G02480; -.
DR   Araport; AT2G02480; -.
DR   TAIR; locus:2065299; AT2G02480.
DR   eggNOG; KOG0989; Eukaryota.
DR   HOGENOM; CLU_009072_0_0_1; -.
DR   InParanoid; O64728; -.
DR   OMA; FMPSIRR; -.
DR   OrthoDB; 97895at2759; -.
DR   PhylomeDB; O64728; -.
DR   PRO; PR:O64728; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O64728; baseline and differential.
DR   Genevisible; O64728; AT.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005663; C:DNA replication factor C complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:0010091; P:trichome branching; IMP:UniProtKB.
DR   GO; GO:0010026; P:trichome differentiation; IMP:TAIR.
DR   CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR   InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR02397; dnaX_nterm; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Nucleotide-binding; Nucleus; Reference proteome;
KW   Repeat.
FT   CHAIN           1..1218
FT                   /note="Protein STICHEL"
FT                   /id="PRO_0000422976"
FT   REGION          24..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          802..828
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          762..788
FT                   /evidence="ECO:0000255"
FT   MOTIF           163..180
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           273..304
FT                   /note="PEST 1"
FT   MOTIF           425..449
FT                   /note="PEST 2"
FT   MOTIF           1178..1195
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           1196..1213
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        32..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         490..497
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1218 AA;  135303 MW;  123D73BD39965CC5 CRC64;
     MSGSRVSDLS KLHLKKELTQ IRKAGRVLRD PGTTSSWKSP LDSSRSVALL ETPASRNGGS
     SSQFPIRGES STNRRGKEKK VFLYNWKTQK SSSEKSGLAK NGKEEEEEEE DASSWTQASV
     NDDDDVSDAR NGGDSYRREI QSASMGFRCR DTNLASQGVS KMRKSNVGSC KKKSKKKISS
     SRLDCLSKYQ PRDDIVARNC NAGSDDTEEE LSNSEDLRKV TGASPLLLKL KQKNWSRSSS
     RLLRANNRKE DSSCTYNSTP ALSTSSYNMY AVRNPSTVGS WDGTTTSVND GDDELDDNLD
     LPGRQGCGIP CYWTKKAMKH RGGCRSCCSP SFSDTLRRTG SSILCGSQSV YRRHNRHSSG
     GYSKQKIACR SAQGVLPLLS YGGDGRGGSS LGTGLSDDEL STNYGELDLE AQSRLDGRRW
     STSYRSQDGL EAVALDGEEE EGSTPETIRS FSQKYRPMFF EELIGQSIVV QSLMNAVKRS
     RIAPVYLFQG PRGTGKTSTA RIFSAALNCV ATEEMKPCGY CKECNDFMSG KSKDFWELDG
     ANKKGADKVR YLLKNLPTIL PRNSSMYKVF VIDECHLLPS KTWLSFLKFL ENPLQKVVFI
     FITTDLENVP RTIQSRCQKF LFDKLKDSDI VVRLKKIASD ENLDVDLHAL DLIAMNADGS
     LRDAETMLEQ LSLLGKRITT ALVNELVGVV SDEKLLELLE LALSSDTAET VKRARELLDL
     GADPIVLMSQ LASLIMDIIA GTYKVVDEKY SNAFFDGRNL TEADMEGLKH ALKLLSEAEK
     QLRVSNDRST WFTATLLQLG SMPSPGTTHT GSSRRQSSRA TDDDPASVSR EVMAYKQRIG
     GLHFSKSASP ASVIKRNGNH SHEAKPFSRV IDNNCYKSSS SSQMIESEGS IASHENSIAS
     TMMLNQRSSE KLNDIWRKCI ERCHSKTLRQ LLYTHGKLIS ISEVEGILVA YIAFGENDIK
     LRAERFLSSI TNSIEMVLRR SVEVRIILLP ETELLVVPHQ TRKPEMTNKS GHLNNIAGLN
     AETDVEVGSS VESRSKLPMQ RIESIIREQR LETAWLQTAD KDTPGSIIRV KPERNQILPQ
     EDTYRQTNVA SAISSSGLTT HQWVDELNNE VKLLKIGDNG ELQENLTGTR GQHCPLSPSL
     LHDTNFGNNK DNLGGYESGS GRVGCNILFC WNTKKTQRRS KSKQVKGTPV RSRRNRKSRF
     SLFNGCAKPR KAEGNIRR
 
 
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