STA1_ARATH
ID STA1_ARATH Reviewed; 1029 AA.
AC Q9ZT71; Q0WVN9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Protein STABILIZED1;
DE AltName: Full=Pre-mRNA processing factor 6-like protein;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2770;
GN Name=STA1; Synonyms=EMB2770; OrderedLocusNames=At4g03430; ORFNames=F9H3.5;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 8-619.
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, DISRUPTION PHENOTYPE, MUTAGENESIS OF 417-CYS-PRO-418, INDUCTION
RP BY ABIOTIC STRESS, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16751345; DOI=10.1105/tpc.106.042184;
RA Lee B.H., Kapoor A., Zhu J., Zhu J.K.;
RT "STABILIZED1, a stress-upregulated nuclear protein, is required for pre-
RT mRNA splicing, mRNA turnover, and stress tolerance in Arabidopsis.";
RL Plant Cell 18:1736-1749(2006).
RN [6]
RP FUNCTION.
RX PubMed=23268445; DOI=10.1093/nar/gks1309;
RA Ben Chaabane S., Liu R., Chinnusamy V., Kwon Y., Park J.H., Kim S.Y.,
RA Zhu J.K., Yang S.W., Lee B.H.;
RT "STA1, an Arabidopsis pre-mRNA processing factor 6 homolog, is a new player
RT involved in miRNA biogenesis.";
RL Nucleic Acids Res. 41:1984-1997(2013).
RN [7]
RP FUNCTION, MUTAGENESIS OF GLY-413, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP IN PRE-MRNA SPLICING COMPLEX.
RC STRAIN=cv. C24;
RX PubMed=23877244; DOI=10.1093/nar/gkt639;
RA Dou K., Huang C.F., Ma Z.Y., Zhang C.J., Zhou J.X., Huang H.W., Cai T.,
RA Tang K., Zhu J.K., He X.J.;
RT "The PRP6-like splicing factor STA1 is involved in RNA-directed DNA
RT methylation by facilitating the production of Pol V-dependent scaffold
RT RNAs.";
RL Nucleic Acids Res. 41:8489-8502(2013).
RN [8]
RP INTERACTION WITH ZOP1.
RX PubMed=23524848; DOI=10.1038/emboj.2013.49;
RA Zhang C.J., Zhou J.X., Liu J., Ma Z.Y., Zhang S.W., Dou K., Huang H.W.,
RA Cai T., Liu R., Zhu J.K., He X.J.;
RT "The splicing machinery promotes RNA-directed DNA methylation and
RT transcriptional silencing in Arabidopsis.";
RL EMBO J. 32:1128-1140(2013).
RN [9]
RP INTERACTION WITH PRP31, AND SUBCELLULAR LOCATION.
RX PubMed=25684655; DOI=10.1016/j.molp.2015.02.003;
RA Du J.L., Zhang S.W., Huang H.W., Cai T., Li L., Chen S., He X.J.;
RT "The splicing factor PRP31 is involved in transcriptional gene silencing
RT and stress response in Arabidopsis.";
RL Mol. Plant 8:1053-1068(2015).
CC -!- FUNCTION: Pre-mRNA splicing factor required for splicing and for the
CC turnover of unstable transcripts. May be a U5 snRNP-associated protein
CC involved in the formation of U4/U6-U5 tri-snRNP. Involved in responses
CC to abiotic stresses. Involved in microRNAs (miRNAs) biogenesis by
CC functioning in primary miRNAs (pri-miRNAs) splicing. Required for DNA
CC methylation and transcriptional silencing through the RNA-directed DNA
CC methylation (RdDM) pathway. {ECO:0000269|PubMed:16751345,
CC ECO:0000269|PubMed:23268445, ECO:0000269|PubMed:23877244}.
CC -!- SUBUNIT: Component of a pre-mRNA splicing complex (PubMed:23877244).
CC Interacts with ZOP1 (PubMed:23524848). Interacts with PRP31
CC (PubMed:25684655). {ECO:0000269|PubMed:23524848,
CC ECO:0000269|PubMed:23877244, ECO:0000269|PubMed:25684655}.
CC -!- INTERACTION:
CC Q9ZT71; Q7XA66: ZOP1; NbExp=2; IntAct=EBI-6921761, EBI-4429233;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16751345,
CC ECO:0000269|PubMed:25684655}. Nucleus, Cajal body
CC {ECO:0000269|PubMed:23877244, ECO:0000269|PubMed:25684655}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16751345}.
CC -!- INDUCTION: Up-regulated by cold stress, but not by abscisic acid or
CC salt treatment. {ECO:0000269|PubMed:16751345}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:16751345}.
CC -!- MISCELLANEOUS: The sta1-1 mutation causes the stabilization of the
CC normally unstable STA1 transcript (PubMed:16751345) and increases the
CC expression levels of miRNA target genes (PubMed:23268445).
CC {ECO:0000305|PubMed:16751345, ECO:0000305|PubMed:23268445}.
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DR EMBL; AF071527; AAD11585.1; -; Genomic_DNA.
DR EMBL; AL161496; CAB77828.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82320.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67973.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67974.1; -; Genomic_DNA.
DR EMBL; AY059720; AAL24077.1; -; mRNA.
DR EMBL; AY142510; AAN13111.1; -; mRNA.
DR EMBL; AK226702; BAE98809.1; -; mRNA.
DR PIR; E85043; E85043.
DR RefSeq; NP_001319859.1; NM_001340448.1.
DR RefSeq; NP_001329764.1; NM_001340449.1.
DR RefSeq; NP_192252.1; NM_116581.2.
DR AlphaFoldDB; Q9ZT71; -.
DR SMR; Q9ZT71; -.
DR BioGRID; 13216; 2.
DR IntAct; Q9ZT71; 1.
DR MINT; Q9ZT71; -.
DR STRING; 3702.AT4G03430.1; -.
DR iPTMnet; Q9ZT71; -.
DR PaxDb; Q9ZT71; -.
DR PRIDE; Q9ZT71; -.
DR ProteomicsDB; 228262; -.
DR EnsemblPlants; AT4G03430.1; AT4G03430.1; AT4G03430.
DR EnsemblPlants; AT4G03430.2; AT4G03430.2; AT4G03430.
DR EnsemblPlants; AT4G03430.3; AT4G03430.3; AT4G03430.
DR GeneID; 827925; -.
DR Gramene; AT4G03430.1; AT4G03430.1; AT4G03430.
DR Gramene; AT4G03430.2; AT4G03430.2; AT4G03430.
DR Gramene; AT4G03430.3; AT4G03430.3; AT4G03430.
DR KEGG; ath:AT4G03430; -.
DR Araport; AT4G03430; -.
DR TAIR; locus:2128751; AT4G03430.
DR eggNOG; KOG0495; Eukaryota.
DR HOGENOM; CLU_007010_0_0_1; -.
DR InParanoid; Q9ZT71; -.
DR OMA; DGWAWYY; -.
DR OrthoDB; 335779at2759; -.
DR PhylomeDB; Q9ZT71; -.
DR PRO; PR:Q9ZT71; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZT71; baseline and differential.
DR Genevisible; Q9ZT71; AT.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:TAIR.
DR GO; GO:2000630; P:positive regulation of miRNA metabolic process; IMP:UniProtKB.
DR GO; GO:2000636; P:positive regulation of primary miRNA processing; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR010491; PRP1_N.
DR InterPro; IPR027108; Prp6/Prp1/STA1.
DR InterPro; IPR045075; Syf1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR PANTHER; PTHR11246; PTHR11246; 1.
DR PANTHER; PTHR11246:SF1; PTHR11246:SF1; 1.
DR Pfam; PF06424; PRP1_N; 1.
DR SMART; SM00386; HAT; 12.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; Spliceosome; TPR repeat.
FT CHAIN 1..1029
FT /note="Protein STABILIZED1"
FT /id="PRO_0000429843"
FT DOMAIN 1..85
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REPEAT 367..399
FT /note="HAT 1"
FT REPEAT 401..431
FT /note="HAT 2"
FT REPEAT 432..462
FT /note="HAT 3"
FT REPEAT 463..494
FT /note="HAT 4"
FT REPEAT 496..524
FT /note="HAT 5"
FT REPEAT 526..554
FT /note="HAT 6"
FT REPEAT 625..658
FT /note="TPR 1"
FT REPEAT 639..671
FT /note="HAT 7"
FT REPEAT 673..705
FT /note="HAT 8"
FT REPEAT 707..739
FT /note="HAT 9"
FT REPEAT 741..772
FT /note="HAT 10"
FT REPEAT 774..806
FT /note="HAT 11"
FT REPEAT 794..827
FT /note="TPR 2"
FT REPEAT 808..840
FT /note="HAT 12"
FT REPEAT 842..874
FT /note="HAT 13"
FT REPEAT 876..908
FT /note="HAT 14"
FT REPEAT 926..959
FT /note="TPR 3"
FT REPEAT 940..972
FT /note="HAT 15"
FT REGION 142..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 210..243
FT /evidence="ECO:0000255"
FT CROSSLNK 85
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT MUTAGEN 413
FT /note="G->D: Suppresses the transcriptional silencing of
FT RdDM targets."
FT /evidence="ECO:0000269|PubMed:23877244"
FT MUTAGEN 417..418
FT /note="Missing: In sta1-1; delayed growth, sensitivity to
FT cold and hypersensitivity to abscisic acid. Stabilizes its
FT own transcript."
FT /evidence="ECO:0000269|PubMed:16751345"
FT CONFLICT 72
FT /note="R -> C (in Ref. 4; BAE98809)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="V -> A (in Ref. 4; BAE98809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1029 AA; 115576 MW; 208DF8D3C705AC0B CRC64;
MVFLSIPNGK TLSIDVNPNS TTISAFEQLA HQRSDVPQSF LRYSLRMRNP SRVFVDSKDS
DSILLSDLGV SRFSTVIIHV LLLGGMQAAP PKPRLDFLNS KPPSNYVAGL GRGATGFTTR
SDIGPARAAP DLPDRSALAT AAAPGVGRGA GKPSEAEAED DEEAEEKRYD ENQTFDEFEG
NDVGLFANAE YDEDDKEADA IWESIDQRMD SRRKDRREAK LKEEIEKYRA SNPKITEQFA
DLKRKLHTLS ADEWDSIPEI GDYSLRNKKK KFESFVPIPD TLLEKAKKEK ELVMALDPKS
RAAGGSETPW GQTPVTDLTA VGEGRGTVLS LKLDNLSDSV SGQTVVDPKG YLTDLKSMKR
TTDEEIYDRN RARLLYKSLT QSNPKNPNGW IAAARVEEVD GKIKAARFQI QRGCEECPKN
EDVWLEACRL ANPEDAKGVI AKGVKLIPNS VKLWLEAAKL EHDVENKSRV LRKGLEHIPD
SVRLWKAVVE LANEEDARIL LHRAVECCPL HLELWVALAR LETYAESKKV LNKAREKLPK
EPAIWITAAK LEEANGKLDE ANDNTAMVGK IIDRGIKTLQ REGVVIDREN WMSEAEACER
VGSVATCQAI IKNTIGIGVE EEDRKRTWVA DADECKKRGS IETARAIYAH ALSVFLTKKS
IWLKAAQLEK SHGSRESLDA LLRKAVTYVP QAEVLWLMGA KEKWLAGDVP AARAILQEAY
AAIPNSEEIW LAAFKLEFEN KEPERARMLL AKARERGGTE RVWMKSAIVE RELGNVEEER
RLLNEGLKQF PTFFKLWLML GQLEERFKHL EQARKAYDTG LKHCPHCIPL WLSLADLEEK
VNGLNKARAI LTTARKKNPG GAELWLAAIR AELRHDNKRE AEHLMSKALQ DCPKSGILWA
ADIEMAPRPR RKTKSIDAMK KCDRDPHVTI AVAKLFWQDK KVEKARAWFE RAVTVGPDIG
DFWALFYKFE LQHGSDEDRK EVVAKCVACE PKHGEKWQAI SKAVENAHQP IEVILKRVVN
ALSKEENSA
