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THAL_ARATH
ID   THAL_ARATH              Reviewed;         654 AA.
AC   Q8L3P4; O22838; Q0WVP9;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Protein THALLO {ECO:0000303|PubMed:27792779};
DE   AltName: Full=Protein EMBRYO DEFECTIVE 2777 {ECO:0000303|PubMed:15266054};
GN   Name=THAL {ECO:0000303|PubMed:27792779};
GN   Synonyms=EMB2777 {ECO:0000303|PubMed:15266054};
GN   OrderedLocusNames=At2g43650 {ECO:0000312|Araport:AT2G43650};
GN   ORFNames=F18O19.24 {ECO:0000312|EMBL:AAB64041.1};
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 [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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-383.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15266054; DOI=10.1104/pp.104.045179;
RA   Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA   Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT   "Identification of genes required for embryo development in Arabidopsis.";
RL   Plant Physiol. 135:1206-1220(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND INTERACTION WITH NUCL1; NUCL2; JMJ14; NOF1 AND
RP   MPP10.
RC   STRAIN=cv. Columbia;
RX   PubMed=27792779; DOI=10.1371/journal.pgen.1006408;
RA   Chen Y.-J.C., Wang H.-J., Jauh G.-Y.;
RT   "Dual role of a SAS10/C1D family protein in ribosomal RNA gene expression
RT   and processing is essential for reproduction in Arabidopsis thaliana.";
RL   PLoS Genet. 12:e1006408-e1006408(2016).
CC   -!- FUNCTION: Essential protein during embryogenesis (PubMed:15266054,
CC       PubMed:27792779). Involved both in gene transcription regulation and in
CC       processing events critical for proper rRNA biogenesis and nucleolar
CC       organization during reproduction; contributes to pre-rRNA processing at
CC       the 5' external transcribed spacer (PubMed:27792779). Binds RNA (By
CC       similarity). {ECO:0000250|UniProtKB:Q9I7W5,
CC       ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:27792779}.
CC   -!- SUBUNIT: Interacts with NUCL1, NUCL2, JMJ14, NOF1 and MPP10 in the
CC       nucleus. {ECO:0000269|PubMed:27792779}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC       Nucleus, nucleolus {ECO:0000269|PubMed:27792779}.
CC   -!- TISSUE SPECIFICITY: Mainly present in tissues undergoing rapid cellular
CC       growth and differentiation (PubMed:27792779). Mostly expressed in
CC       shoots and flowers, and, to a lower extent, in leaves, siliques, roots
CC       and seedlings (PubMed:27792779). {ECO:0000269|PubMed:27792779}.
CC   -!- DEVELOPMENTAL STAGE: In seedlings, observed in the subapical region of
CC       primary roots, lateral root primordia, leaf veins and around guard
CC       cells (PubMed:27792779). In flowers, present in ovules, pollen, embryos
CC       and endosperm (PubMed:27792779). {ECO:0000269|PubMed:27792779}.
CC   -!- DISRUPTION PHENOTYPE: Embryo defective arrested at the cotyledon stage,
CC       associated with enlarged nucleoli probably due to the over-accumulation
CC       of pre-rRNAs. {ECO:0000269|PubMed:15266054,
CC       ECO:0000269|PubMed:27792779}.
CC   -!- MISCELLANEOUS: 'Thallo' is the Greek goddess of buds and shoots.
CC       {ECO:0000305|PubMed:27792779}.
CC   -!- SIMILARITY: Belongs to the SAS10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB64041.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
CC       URL="http://seedgenes.org/MutantList";
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DR   EMBL; AC002333; AAB64041.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC10301.1; -; Genomic_DNA.
DR   EMBL; AY099689; AAM20540.1; -; mRNA.
DR   EMBL; AY128870; AAM91270.1; -; mRNA.
DR   EMBL; AK226692; BAE98799.1; -; mRNA.
DR   PIR; G84868; G84868.
DR   RefSeq; NP_850397.1; NM_180066.3.
DR   AlphaFoldDB; Q8L3P4; -.
DR   SMR; Q8L3P4; -.
DR   IntAct; Q8L3P4; 2.
DR   STRING; 3702.AT2G43650.1; -.
DR   iPTMnet; Q0WVP9; -.
DR   PaxDb; Q8L3P4; -.
DR   PRIDE; Q8L3P4; -.
DR   ProteomicsDB; 251949; -.
DR   EnsemblPlants; AT2G43650.1; AT2G43650.1; AT2G43650.
DR   GeneID; 818967; -.
DR   Gramene; AT2G43650.1; AT2G43650.1; AT2G43650.
DR   KEGG; ath:AT2G43650; -.
DR   Araport; AT2G43650; -.
DR   TAIR; locus:2044014; AT2G43650.
DR   eggNOG; KOG3118; Eukaryota.
DR   HOGENOM; CLU_029301_0_0_1; -.
DR   InParanoid; Q8L3P4; -.
DR   OMA; AQKANKR; -.
DR   OrthoDB; 1451774at2759; -.
DR   PhylomeDB; Q8L3P4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8L3P4; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR   GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IMP:TAIR.
DR   InterPro; IPR007146; Sas10/Utp3/C1D.
DR   InterPro; IPR018972; Sas10_C_dom.
DR   PANTHER; PTHR13237; PTHR13237; 1.
DR   Pfam; PF09368; Sas10; 1.
DR   Pfam; PF04000; Sas10_Utp3; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Coiled coil; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribonucleoprotein; RNA-binding.
FT   CHAIN           1..654
FT                   /note="Protein THALLO"
FT                   /id="PRO_0000454729"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          35..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          140..160
FT                   /evidence="ECO:0000255"
FT   COILED          243..263
FT                   /evidence="ECO:0000255"
FT   MOTIF           2..9
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           608..615
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        45..81
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..397
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..543
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..621
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  73973 MW;  FEB7CE72DC73952A CRC64;
     MGKKGGTLKR SSKSTKTRKD IVEDQYDDEI DAFHKQRDIV PLDVNDDTDE SDEDDVQPVF
     DLQGVDDESE EDEDTEDEEE AENGLTAKMI RQKKYLRAKF GDGDDEMADD DKDKEEDKRS
     TWGGRSGLYH SGDNVDFDIL SSDDEDIKAE EEEVIRLRAE QLGSITAADA GLDDDSEEDS
     DRELTMEEIS DKGKQATKSI TDKKEKGDKD THVEEIKKDI NSLSKEEQMD VVYSSAPEIV
     GLLSELNDAV EELESKINPV MNKLKEGEIS LNGLARYLEV KQLLLLTYCQ SITFYLLLKS
     EGQPIRDHPV LARLVEIKSL LDKIKELDEE LPPGFEESLA RSIANGAVQK VVKEDQLTSP
     VSDSVDRITQ DTAKPMKIDN AREEKKKKGE KRKHQNDLVD VQSEEMLKLR AALEGKLRTN
     GVLGSTVSKS DKAQKRQKLA NRKLETFDDY VDDADNSTHN VTADKLTKLV STKRKPKTIS
     GDDDLPQRDD IGERRRKFEL RVLAGAGVKS SEGDGRNKNG AFASDDEDDN DGDNNDMVDN
     DGESEDEFYK QVKQKQQAKR AAKAEIYSRK PHLMPSSPEH VDGKRHISNQ MVSNRGLTRQ
     RNRDLKNPRK KYRKNYEKKV TRRKGQVRDI RKQTGPYAGE ARGINPNTSR SIRM
 
 
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