SIC_ARATH
ID SIC_ARATH Reviewed; 319 AA.
AC Q9SB47; Q8H0Z3; Q94AJ0;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein SICKLE {ECO:0000303|PubMed:23071326};
DE AltName: Full=Protein ROTUNDA 3 {ECO:0000303|PubMed:26888284};
GN Name=SIC {ECO:0000303|PubMed:23071326};
GN Synonyms=RON3 {ECO:0000303|PubMed:26888284};
GN OrderedLocusNames=At4g24500 {ECO:0000312|Araport:AT4G24500};
GN ORFNames=F22K18.300 {ECO:0000312|EMBL:CAA23013.1};
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=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] (ISOFORMS 1 AND 2).
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 FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23071326; DOI=10.1073/pnas.1216199109;
RA Zhan X., Wang B., Li H., Liu R., Kalia R.K., Zhu J.-K., Chinnusamy V.;
RT "Arabidopsis proline-rich protein important for development and abiotic
RT stress tolerance is involved in microRNA biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18198-18203(2012).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH UBP12; UBP13; PP2AB1; PP2AB2;
RP PP2A3; PP2A4; PP2AA1 AND PP2AA2.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=26888284; DOI=10.1073/pnas.1501343112;
RA Karampelias M., Neyt P., De Groeve S., Aesaert S., Coussens G., Rolcik J.,
RA Bruno L., De Winne N., Van Minnebruggen A., Van Montagu M., Ponce M.R.,
RA Micol J.L., Friml J., De Jaeger G., Van Lijsebettens M.;
RT "ROTUNDA3 function in plant development by phosphatase 2A-mediated
RT regulation of auxin transporter recycling.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:2768-2773(2016).
CC -!- FUNCTION: Involved in miRNAs and siRNAs biogenesis and thus promotes
CC gene silencing (PubMed:23071326). Modulates auxin (IAA) transport-
CC related developmental programs by regulating protein phosphatase 2A
CC (PP2As)-driven auxin efflux carrier PIN proteins recycling and polarity
CC (PubMed:26888284). Required during development (PubMed:23071326,
CC PubMed:26888284). Necessary for abiotic stress (e.g. chilling and salt)
CC tolerance (PubMed:23071326). {ECO:0000269|PubMed:23071326,
CC ECO:0000269|PubMed:26888284}.
CC -!- SUBUNIT: Interacts with ubiquitin thioesterases UBP12 and UBP13, and
CC with protein phosphatase 2A subunits PP2AB1, PP2AB2, PP2A3, PP2A4,
CC PP2AA1 and PP2AA2. {ECO:0000269|PubMed:26888284}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23071326,
CC ECO:0000269|PubMed:26888284}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:26888284}. Note=Colocalizes with miRNA biogenesis
CC components in distinct subnuclear bodies (PubMed:23071326). Localized
CC in the nuclei, excluding the nucleolus, in all cells of the root apical
CC meristem. In young cortical cells of the root, localized in the nucleus
CC and cytosol (PubMed:26888284). {ECO:0000269|PubMed:23071326,
CC ECO:0000269|PubMed:26888284}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SB47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SB47-2; Sequence=VSP_059075;
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apical meristem (SAM),
CC embryos, seedlings, root tips, and root and leaf primordia.
CC {ECO:0000269|PubMed:26888284}.
CC -!- DEVELOPMENTAL STAGE: Localized in the shoot apical meristem (SAM) dome,
CC the emerging leaf and root primordia, the provascular strands of
CC developing seedlings, and the epidermis and cortex of the meristematic
CC and elongation zones of the primary root tip, and in the protoderm of
CC heart- and torpedo- stage embryos. {ECO:0000269|PubMed:26888284}.
CC -!- DISRUPTION PHENOTYPE: Developmental defects due to abnormal miRNAs and
CC siRNAs biogenesis including serrated, sickle-like leaf margin, reduced
CC height, delayed flowering, and abnormal inflorescence phyllotaxy.
CC Hypersensitivity to chilling and salt stresses (PubMed:23071326).
CC Several symptoms associated with alteration in auxin (IAA) signaling
CC such as increased IAA levels in shoot apices and reduced IAA
CC accumulation in root meristems, reduced apical dominance and abnormal
CC root gravitropism, growth and emergence. Altered PIN polarity and
CC endocytosis in specific cells (PubMed:26888284).
CC {ECO:0000269|PubMed:23071326, ECO:0000269|PubMed:26888284}.
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DR EMBL; AL035356; CAA23013.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79360.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84915.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84916.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84917.1; -; Genomic_DNA.
DR EMBL; AY046010; AAK76684.1; -; mRNA.
DR EMBL; AY142488; AAN13039.1; -; mRNA.
DR EMBL; BT001099; AAN64163.1; -; mRNA.
DR PIR; T05584; T05584.
DR RefSeq; NP_001190822.1; NM_001203893.1. [Q9SB47-1]
DR RefSeq; NP_001320056.1; NM_001341679.1. [Q9SB47-2]
DR RefSeq; NP_567704.1; NM_118583.4. [Q9SB47-1]
DR AlphaFoldDB; Q9SB47; -.
DR IntAct; Q9SB47; 3.
DR STRING; 3702.AT4G24500.3; -.
DR PaxDb; Q9SB47; -.
DR PRIDE; Q9SB47; -.
DR ProteomicsDB; 232634; -. [Q9SB47-1]
DR EnsemblPlants; AT4G24500.1; AT4G24500.1; AT4G24500. [Q9SB47-1]
DR EnsemblPlants; AT4G24500.2; AT4G24500.2; AT4G24500. [Q9SB47-2]
DR EnsemblPlants; AT4G24500.3; AT4G24500.3; AT4G24500. [Q9SB47-1]
DR GeneID; 828552; -.
DR Gramene; AT4G24500.1; AT4G24500.1; AT4G24500. [Q9SB47-1]
DR Gramene; AT4G24500.2; AT4G24500.2; AT4G24500. [Q9SB47-2]
DR Gramene; AT4G24500.3; AT4G24500.3; AT4G24500. [Q9SB47-1]
DR KEGG; ath:AT4G24500; -.
DR Araport; AT4G24500; -.
DR TAIR; locus:2121870; AT4G24500.
DR eggNOG; ENOG502RYUD; Eukaryota.
DR HOGENOM; CLU_800261_0_0_1; -.
DR InParanoid; Q9SB47; -.
DR OMA; SPDQRMY; -.
DR OrthoDB; 1554506at2759; -.
DR PhylomeDB; Q9SB47; -.
DR PRO; PR:Q9SB47; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB47; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0016604; C:nuclear body; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007623; P:circadian rhythm; IMP:TAIR.
DR GO; GO:0009649; P:entrainment of circadian clock; IMP:TAIR.
DR GO; GO:0035196; P:miRNA processing; IMP:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:TAIR.
DR GO; GO:1901703; P:protein localization involved in auxin polar transport; IGI:TAIR.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:TAIR.
DR GO; GO:2000012; P:regulation of auxin polar transport; IGI:TAIR.
DR GO; GO:1903730; P:regulation of phosphatidate phosphatase activity; IGI:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0030422; P:siRNA processing; IMP:UniProtKB.
DR InterPro; IPR039292; SICKLE.
DR PANTHER; PTHR36054; PTHR36054; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Auxin signaling pathway; Cytoplasm;
KW Developmental protein; Nucleus; Reference proteome;
KW RNA-mediated gene silencing; Stress response.
FT CHAIN 1..319
FT /note="Protein SICKLE"
FT /id="PRO_0000441628"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 58..86
FT /note="Missing (in isoform 2)"
FT /id="VSP_059075"
FT CONFLICT 208
FT /note="Y -> H (in Ref. 3; AAK76684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 35051 MW; 559912A615690A54 CRC64;
MEDSEKRKQM LKAMRMEAAA QNDDDATTGT ETSMSTGHLS NPLAETSNHQ QDSFETQRFD
YYTDPMAAYS SFKKNKTPKQ QYISSPSHQG SSPVPPQFPP SVPPGSLCSE YQAQTNHGGF
HAAHYEPRGM AHLSPSHRGP PAGWNNNFRP PPVNHSGPPQ WVPRPFPFSQ EMPNMGNNRF
GGRGSYNNTP PQFSNYGRQN ANWGGNTYPN SGRGRSRGRG MNTSFGRDGG RRPMEPGAER
FYSNSMAEDP WKHLKPVLWK NCSDASSSSS TGQAWLPKSI APKKSVTSEA THKTSSNQQS
LAEYLAASLD GATCDESSN
