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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};
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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
 
 
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