COIL_ARATH
ID COIL_ARATH Reviewed; 608 AA.
AC Q8RWK8; Q9SAD8;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Coilin {ECO:0000303|PubMed:16624863};
DE AltName: Full=Atcoilin {ECO:0000303|PubMed:16624863};
GN Name=COIL {ECO:0000303|PubMed:16624863};
GN OrderedLocusNames=At1g13030 {ECO:0000312|Araport:AT1G13030};
GN ORFNames=F3F19.5 {ECO:0000312|EMBL:AAD31056.1};
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:AAM13027.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-106.
RX PubMed=16624863; DOI=10.1091/mbc.e05-12-1157;
RA Collier S., Pendle A., Boudonck K., van Rij T., Dolan L., Shaw P.;
RT "A distant coilin homologue is required for the formation of cajal bodies
RT in Arabidopsis.";
RL Mol. Biol. Cell 17:2942-2951(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION BY
RP 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 [6]
RP FUNCTION, DOMAIN, MUTAGENESIS OF ARG-15; ARG-16; LYS-20; LYS-23; LYS-24;
RP ARG-36; LYS-37; HIS-39 AND ARG-40, SUBUNIT, AND 3D-STRUCTURE MODELING.
RX PubMed=23320094; DOI=10.1371/journal.pone.0053571;
RA Makarov V., Rakitina D., Protopopova A., Yaminsky I., Arutiunian A.,
RA Love A.J., Taliansky M., Kalinina N.;
RT "Plant coilin: structural characteristics and RNA-binding properties.";
RL PLoS ONE 8:E53571-E53571(2013).
CC -!- FUNCTION: Probable component of nuclear coiled bodies, also known as
CC Cajal bodies or CBs, which are involved in the modification and
CC assembly of nucleoplasmic snRNPs (Probable). Required for CBs formation
CC (PubMed:16624863). Binds snRNAs and non-specific artificial RNA via the
CC N-terminal part of the NOD domain and via the NLS2 region (212-282) of
CC the IDD domain (PubMed:23320094). The two sites are able to function
CC independently and provide effective RNA-binding in a non-cooperative
CC manner (PubMed:23320094). {ECO:0000269|PubMed:16624863,
CC ECO:0000269|PubMed:23320094, ECO:0000305|PubMed:16624863}.
CC -!- SUBUNIT: Homooligomer. Interaction with RNA results in multimerization
CC due to structural alteration in the NOD domain.
CC {ECO:0000269|PubMed:23320094}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC Nucleus, Cajal body {ECO:0000305|PubMed:16624863}.
CC -!- DOMAIN: Contains a N-terminal ordered domain (NOD) (1-117), central
CC internal disordered domain (IDD) (118-349) and a C-terminal domain
CC (CTD) (350-608) with an atypical Tudor domain containing probably two
CC large unstructured loops. {ECO:0000269|PubMed:23320094}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but loss of Cajal bodies.
CC {ECO:0000269|PubMed:16624863}.
CC -!- SIMILARITY: Belongs to the coilin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD31056.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007357; AAD31056.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28961.1; -; Genomic_DNA.
DR EMBL; AY093028; AAM13027.1; -; mRNA.
DR EMBL; AY128933; AAM91333.1; -; mRNA.
DR PIR; C86264; C86264.
DR RefSeq; NP_172762.2; NM_101173.5.
DR AlphaFoldDB; Q8RWK8; -.
DR IntAct; Q8RWK8; 4.
DR STRING; 3702.AT1G13030.1; -.
DR iPTMnet; Q8RWK8; -.
DR PaxDb; Q8RWK8; -.
DR PRIDE; Q8RWK8; -.
DR ProteomicsDB; 241093; -.
DR EnsemblPlants; AT1G13030.1; AT1G13030.1; AT1G13030.
DR GeneID; 837860; -.
DR Gramene; AT1G13030.1; AT1G13030.1; AT1G13030.
DR KEGG; ath:AT1G13030; -.
DR Araport; AT1G13030; -.
DR TAIR; locus:2031810; AT1G13030.
DR eggNOG; ENOG502QVBB; Eukaryota.
DR HOGENOM; CLU_018167_1_0_1; -.
DR InParanoid; Q8RWK8; -.
DR OMA; RKITVFW; -.
DR OrthoDB; 488445at2759; -.
DR PhylomeDB; Q8RWK8; -.
DR PRO; PR:Q8RWK8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RWK8; baseline and differential.
DR Genevisible; Q8RWK8; AT.
DR GO; GO:0015030; C:Cajal body; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:TAIR.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:TAIR.
DR GO; GO:0006396; P:RNA processing; IMP:TAIR.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR DisProt; DP02248; -.
DR InterPro; IPR024822; Coilin.
DR InterPro; IPR031722; Coilin_N.
DR PANTHER; PTHR15197; PTHR15197; 1.
DR Pfam; PF15862; Coilin_N; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..608
FT /note="Coilin"
FT /id="PRO_0000434410"
FT DOMAIN 410..510
FT /note="Tudor; atypical"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT REGION 134..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 163..170
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 253..260
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 175..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 15
FT /note="R->A: In NOD-RK1; Decreased RNA-binding; when
FT associated with A-16; A-20; A-23 and A-24. In NOD-RK1-2;
FT Loss of RNA-binding; when associated with A-16; A-20; A-23;
FT A-24; A-36; A-37; A-39 and A-40."
FT /evidence="ECO:0000269|PubMed:23320094"
FT MUTAGEN 16
FT /note="R->A: In NOD-RK1; Decreased RNA-binding; when
FT associated with A-15; A-20; A-23 and A-24. In NOD-RK1-2;
FT Loss of RNA-binding; when associated with A-15; A-20; A-23;
FT A-24; A-36; A-37; A-39 and A-40."
FT /evidence="ECO:0000269|PubMed:23320094"
FT MUTAGEN 20
FT /note="K->A: In NOD-RK1; Decreased RNA-binding; when
FT associated with A-15; A-16; A-23 and A-24. In NOD-RK1-2;
FT Loss of RNA-binding; when associated with A-15; A-16; A-23;
FT A-24; A-36; A-37; A-39 and A-40."
FT /evidence="ECO:0000269|PubMed:23320094"
FT MUTAGEN 23
FT /note="K->A: In NOD-RK1; Decreased RNA-binding; when
FT associated with A-15; A-16; A-20 and A-24. In NOD-RK1-2;
FT Loss of RNA-binding; when associated with A-15; A-16; A-20;
FT A-24; A-36; A-37; A-39 and A-40."
FT /evidence="ECO:0000269|PubMed:23320094"
FT MUTAGEN 24
FT /note="K->A: In NOD-RK1; Decreased RNA-binding; when
FT associated with A-15; A-16; A-20 and A-23. In NOD-RK1-2;
FT Loss of RNA-binding; when associated with A-15; A-16; A-20;
FT A-23; A-36; A-37; A-39 and A-40."
FT /evidence="ECO:0000269|PubMed:23320094"
FT MUTAGEN 36
FT /note="R->A: In NOD-RK2; No effect on RNA-binding; when
FT associated with A-37; A39 and A-40. In NOD-RK1-2; Loss of
FT RNA-binding; when associated with A-15; A-16; A-20; A-23;
FT A-24; A-37; A-39 and A-40."
FT /evidence="ECO:0000269|PubMed:23320094"
FT MUTAGEN 37
FT /note="K->A: In NOD-RK2; No effect on RNA-binding; when
FT associated with A-36; A-39 and A-40. In NOD-RK1-2; Loss of
FT RNA-binding; when associated with A-15; A-16; A-20; A-23;
FT A-24; A-36; A-39 and A-40."
FT /evidence="ECO:0000269|PubMed:23320094"
FT MUTAGEN 39
FT /note="H->A: In NOD-RK2; No effect on RNA-binding; when
FT associated with A-36; A-37 and A-40. In NOD-RK1-2; Loss of
FT RNA-binding; when associated with A-15; A-16; A-20; A-23;
FT A-24; A-36; A-37 and A-40."
FT /evidence="ECO:0000269|PubMed:23320094"
FT MUTAGEN 40
FT /note="R->A: In NOD-RK2; No effect on RNA-binding; when
FT associated with A-36; A-37 and A-39. In NOD-RK1-2; Loss of
FT RNA-binding; when associated with A-15; A-16; A-20; A-23;
FT A-24; A-36; A-37 and A-39."
FT /evidence="ECO:0000269|PubMed:23320094"
FT MUTAGEN 106
FT /note="E->K: In ncb-3; Smaller Cajal bodies."
FT /evidence="ECO:0000269|PubMed:16624863"
SQ SEQUENCE 608 AA; 68667 MW; 8734C1CA957CB27E CRC64;
MEEEKVRVRL VFEDRRILSK YQKKQGLTRS WVVLNRKCHR TISEFSDHIF HTFSLCEACP
HGLSLSMEGF VLPPFESSCV LKDKDIVCVK KKKESLLEIV GEDSDENVYN AIEVEERPQI
RPGEMLLANE EFQKETGGYE SESEEDELEE EAEEFVPEKK ASKKRKTSSK NQSTKRKKCK
LDTTEESPDE RENTAVVSNV VKKKKKKKSL DVQSANNDEQ NNDSTKPMTK SKRSSQQEES
KEHNDLCQLS AETKKTPSRS ARRKKAKRQW LREKTKLEKE ELLQTQLVVA PSQKPVITID
HQATKEKHCE TLENQQAEEV SDGFGDEVVP VEVRPGHIRF KPLAGTDEAS LDSEPLVENV
LWNGNMTKKK GQKWGTEKSG FSKRYAQDFN EDATTQPAEA ETLANCPIDY EQLVAYTGSV
KKGDVIAYRL IELTSSWTPE VSSFRVGKIS YYDPDSKMVT LMPVQEFPIE KKTEEDDDFC
MQPDTSLYKE DGSLEIEFSA LLDVRSVKTS SSDSAEVAKS ALPEPDQSAK KPKLSANKEL
QTPAKENGEV SPWEELSEAL SAKKAALSQA NNGWNKKGSS SGGSWSYKAL RGSAMGPVMN
YLRSQKEI