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ATO_ARATH
ID   ATO_ARATH               Reviewed;         504 AA.
AC   Q9FG01;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 149.
DE   RecName: Full=Splicing factor SF3a60 homolog {ECO:0000305};
DE   AltName: Full=Protein ATROPOS {ECO:0000303|PubMed:18702672};
DE   AltName: Full=Splicing factor ATO {ECO:0000305};
GN   Name=ATO {ECO:0000303|PubMed:18702672};
GN   OrderedLocusNames=At5g06160 {ECO:0000312|Araport:AT5G06160};
GN   ORFNames=MBL20.3 {ECO:0000312|EMBL:BAB09681.1};
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 {ECO:0000312|EMBL:BAB09681.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Root;
RX   PubMed=18433157; DOI=10.1021/pr8000173;
RA   de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA   Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA   Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT   spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-411.
RX   PubMed=18702672; DOI=10.1111/j.1365-313x.2008.03650.x;
RA   Moll C., von Lyncker L., Zimmermann S., Kaegi C., Baumann N., Twell D.,
RA   Grossniklaus U., Gross-Hardt R.;
RT   "CLO/GFA1 and ATO are novel regulators of gametic cell fate in plants.";
RL   Plant J. 56:913-921(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Splicing factor homolog to SF3a60 that may be involved in
CC       pre-spliceosome formation. Is necessary for gametic cell fate
CC       determination. {ECO:0000269|PubMed:18702672}.
CC   -!- INTERACTION:
CC       Q9FG01; Q8VZI9: At3g11100; NbExp=4; IntAct=EBI-4475455, EBI-1998580;
CC       Q9FG01; O23090: BHLH14; NbExp=3; IntAct=EBI-4475455, EBI-15193049;
CC       Q9FG01; Q8S3D2: BHLH87; NbExp=3; IntAct=EBI-4475455, EBI-15194565;
CC       Q9FG01; Q9SK91: BHLH94; NbExp=3; IntAct=EBI-4475455, EBI-15192173;
CC       Q9FG01; Q94KL5: BLH4; NbExp=3; IntAct=EBI-4475455, EBI-1153797;
CC       Q9FG01; O80438: MAK3; NbExp=3; IntAct=EBI-4475455, EBI-15205450;
CC       Q9FG01; O82277: TCP10; NbExp=3; IntAct=EBI-4475455, EBI-3133327;
CC       Q9FG01; Q93Z00: TCP14; NbExp=3; IntAct=EBI-4475455, EBI-4424563;
CC       Q9FG01; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-4475455, EBI-4426144;
CC       Q9FG01; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-4475455, EBI-15192325;
CC       Q9FG01; O64722: ZHD3; NbExp=3; IntAct=EBI-4475455, EBI-1806244;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}.
CC   -!- TISSUE SPECIFICITY: Expressed at moderate levels in all sporophytic
CC       tissues with strongest expression in gametophytes.
CC       {ECO:0000269|PubMed:18702672}.
CC   -!- SIMILARITY: Belongs to the SF3A3 family. {ECO:0000305}.
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DR   EMBL; AP002544; BAB09681.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90977.1; -; Genomic_DNA.
DR   EMBL; AY039944; AAK64048.1; -; mRNA.
DR   EMBL; AY113862; AAM44910.1; -; mRNA.
DR   RefSeq; NP_196234.3; NM_120698.5.
DR   AlphaFoldDB; Q9FG01; -.
DR   SMR; Q9FG01; -.
DR   IntAct; Q9FG01; 52.
DR   MINT; Q9FG01; -.
DR   STRING; 3702.AT5G06160.1; -.
DR   iPTMnet; Q9FG01; -.
DR   PaxDb; Q9FG01; -.
DR   PRIDE; Q9FG01; -.
DR   ProteomicsDB; 246655; -.
DR   EnsemblPlants; AT5G06160.1; AT5G06160.1; AT5G06160.
DR   GeneID; 830503; -.
DR   Gramene; AT5G06160.1; AT5G06160.1; AT5G06160.
DR   KEGG; ath:AT5G06160; -.
DR   Araport; AT5G06160; -.
DR   TAIR; locus:2152855; AT5G06160.
DR   eggNOG; KOG2636; Eukaryota.
DR   HOGENOM; CLU_027160_2_0_1; -.
DR   InParanoid; Q9FG01; -.
DR   OMA; KDAHRRN; -.
DR   OrthoDB; 383503at2759; -.
DR   PhylomeDB; Q9FG01; -.
DR   PRO; PR:Q9FG01; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FG01; baseline and differential.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   GO; GO:0045694; P:regulation of embryo sac egg cell differentiation; IMP:TAIR.
DR   InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR   InterPro; IPR031774; SF3A3_dom.
DR   InterPro; IPR024598; SF3a60/Prp9_C.
DR   InterPro; IPR021966; SF3a60_bindingd.
DR   Pfam; PF16837; SF3A3; 1.
DR   Pfam; PF12108; SF3a60_bindingd; 1.
DR   Pfam; PF11931; SF3a60_Prp9_C; 1.
DR   PROSITE; PS50171; ZF_MATRIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Spliceosome; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..504
FT                   /note="Splicing factor SF3a60 homolog"
FT                   /id="PRO_0000436559"
FT   ZN_FING         409..440
FT                   /note="Matrin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT   REGION          293..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..374
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18433157,
FT                   ECO:0007744|PubMed:19245862"
FT   MUTAGEN         411
FT                   /note="C->Y: In ato; gametophytic lethality."
FT                   /evidence="ECO:0000269|PubMed:18702672"
SQ   SEQUENCE   504 AA;  58972 MW;  64E569113345E8D9 CRC64;
     MSSTLLEQTR SNHEEVERLE RLVVEDLQKE PPSSKDRLVQ GHRVRHMIES IMLTTEKLVE
     TYEDKDGAWD DEIAALGGQT ATGTNVFSEF YDRLKEIREY HKRHPSGRLV DANEDYEARL
     KEEPIIAFSG EEGNGRYLDL HDMYNQYINS KFGERVEYSA YLDVFSQPEK IPRKLKLSRQ
     YMKYMEALLE YLVYFFQRTE PLQDLDRILS KVCSDFEEQY ADGIVEGLDN ELIPSQHTVI
     DLDYYSTVEE LVDVGPEKLK EALGALGLKV GGTPQQRAER LFLTKHTPLE KLDKKHFARP
     PHNGKQNGDA KSTHESENAK EIALTEAKVK KLCNLLDETI ERTKQNIVKK QSLTYEEMEG
     EREGEEANTE LESDDEDGLI YNPLKLPIGW DGKPIPYWLY KLHGLGQEFK CEICGNYSYW
     GRRAFERHFK EWRHQHGMRC LGIPNTKNFN EITSIEEAKE LWKRIQERQG VNKWRPELEE
     EYEDREGNIY NKKTYSDLQR QGLI
 
 
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