CRWN1_ARATH
ID CRWN1_ARATH Reviewed; 1132 AA.
AC F4HRT5; Q0WKV7; Q8GZ88; Q9FYH0;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Protein CROWDED NUCLEI 1 {ECO:0000303|PubMed:24308514};
DE AltName: Full=Protein KAKU2 {ECO:0000303|PubMed:24824484};
DE AltName: Full=Protein LITTLE NUCLEI 1 {ECO:0000303|PubMed:17873096};
GN Name=CRWN1 {ECO:0000303|PubMed:24308514};
GN Synonyms=KAKU2 {ECO:0000303|PubMed:24824484},
GN LINC1 {ECO:0000303|PubMed:17873096};
GN OrderedLocusNames=At1g67230 {ECO:0000312|Araport:AT1G67230};
GN ORFNames=F1N21.5 {ECO:0000312|EMBL:AAG00257.1};
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|Proteomes:UP000006548};
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] OF 1-626.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 630-1132.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=17873096; DOI=10.1105/tpc.107.053231;
RA Dittmer T.A., Stacey N.J., Sugimoto-Shirasu K., Richards E.J.;
RT "LITTLE NUCLEI genes affecting nuclear morphology in Arabidopsis
RT thaliana.";
RL Plant Cell 19:2793-2803(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-865; SER-908;
RP SER-1093; SER-1105 AND SER-1112, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803; SER-865 AND SER-908, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND SER-908, AND
RP IDENTIFICATION BY 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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=24308514; DOI=10.1186/1471-2229-13-200;
RA Wang H., Dittmer T.A., Richards E.J.;
RT "Arabidopsis CROWDED NUCLEI (CRWN) proteins are required for nuclear size
RT control and heterochromatin organization.";
RL BMC Plant Biol. 13:200-200(2013).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23396599; DOI=10.1093/pcp/pct031;
RA Sakamoto Y., Takagi S.;
RT "LITTLE NUCLEI 1 and 4 regulate nuclear morphology in Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 54:622-633(2013).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH KAKU4.
RX PubMed=24824484; DOI=10.1105/tpc.113.122168;
RA Goto C., Tamura K., Fukao Y., Shimada T., Hara-Nishimura I.;
RT "The novel nuclear envelope protein KAKU4 modulates nuclear morphology in
RT Arabidopsis.";
RL Plant Cell 26:2143-2155(2014).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SUN1 AND SUN2.
RX PubMed=24667841; DOI=10.1371/journal.pone.0093406;
RA Graumann K.;
RT "Evidence for LINC1-SUN associations at the plant nuclear periphery.";
RL PLoS ONE 9:E93406-E93406(2014).
RN [13]
RP REVIEW.
RX PubMed=25740919; DOI=10.1093/jxb/erv082;
RA Zhou X., Graumann K., Meier I.;
RT "The plant nuclear envelope as a multifunctional platform LINCed by SUN and
RT KASH.";
RL J. Exp. Bot. 66:1649-1659(2015).
CC -!- FUNCTION: Component of SUN-protein-containing multivariate complexes
CC also called LINC complexes which link the nucleoskeleton and
CC cytoskeleton by providing versatile outer nuclear membrane attachment
CC sites for cytoskeletal filaments (By similarity). Required for nucleus
CC structure organization (e.g. size and shape) (PubMed:17873096,
CC PubMed:24308514, PubMed:23396599, PubMed:24824484).
CC {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:17873096,
CC ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514,
CC ECO:0000269|PubMed:24824484}.
CC -!- SUBUNIT: Core component of the LINC complex which is composed of inner
CC nuclear membrane SUN domain-containing proteins coupled to outer
CC nuclear membrane WIP and WIT proteins. The LINC complex also involves
CC nucleoskeletal proteins CRWN/LINC and possibly KAKU4 and the
CC cytoskeletal myosin KAKU1. Interacts with SUN1 and SUN2
CC (PubMed:24667841). Binds to KAKU4 (PubMed:24824484).
CC {ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:24824484}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:17873096,
CC ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17873096,
CC ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:24667841}.
CC Nucleus lamina {ECO:0000269|PubMed:23396599}. Note=Recruited to the
CC nucleus envelope (NE) by SUN proteins and is immobilised therein
CC (PubMed:24667841). Mostly localized at the nuclear periphery and, to a
CC lesser extent, in the nucleoplasm (PubMed:17873096). Localized on the
CC condensing chromatin during prometaphase to anaphase, but transferred
CC from the decondensing chromatin to the reassembling nuclear envelope
CC during early telophase. Relocalized to the nuclear periphery during
CC late telophase (PubMed:23396599). {ECO:0000269|PubMed:17873096,
CC ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24667841}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, leaves, flowers
CC and flower stalks. {ECO:0000269|PubMed:23396599}.
CC -!- DISRUPTION PHENOTYPE: Reduced nuclear size and altered nuclear
CC morphology. In plants lacking both CRWN1 and CRWN2, moderate dwarf and
CC leaf-curling phenotype associated with endoreplication and strongly
CC reduced nuclear size. Plants lacking both CRWN1 and CRWN4 exhibit
CC slightly smaller rosettes. Plants lacking both CRWN1 and CRWN2 or both
CC CRWN1 and CRWN3 exhibit markedly smaller rosettes. Plants lacking
CC CRWN1, CRWN2 and CRWN4 or CRWN1, CRWN3 and CRWN4 are extremely stunted
CC and set few seed. {ECO:0000269|PubMed:17873096,
CC ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514,
CC ECO:0000269|PubMed:24824484}.
CC -!- SIMILARITY: Belongs to the CRWN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG00257.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC41822.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AC002130; AAG00257.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34615.1; -; Genomic_DNA.
DR EMBL; AK230454; BAF02250.1; -; mRNA.
DR EMBL; AK117144; BAC41822.1; ALT_INIT; mRNA.
DR RefSeq; NP_176892.1; NM_105392.5.
DR AlphaFoldDB; F4HRT5; -.
DR SMR; F4HRT5; -.
DR STRING; 3702.AT1G67230.1; -.
DR iPTMnet; F4HRT5; -.
DR PaxDb; F4HRT5; -.
DR PRIDE; F4HRT5; -.
DR ProteomicsDB; 222646; -.
DR EnsemblPlants; AT1G67230.1; AT1G67230.1; AT1G67230.
DR GeneID; 843043; -.
DR Gramene; AT1G67230.1; AT1G67230.1; AT1G67230.
DR KEGG; ath:AT1G67230; -.
DR Araport; AT1G67230; -.
DR TAIR; locus:2019529; AT1G67230.
DR eggNOG; ENOG502QUGA; Eukaryota.
DR HOGENOM; CLU_004241_0_0_1; -.
DR InParanoid; F4HRT5; -.
DR OMA; QEAHEST; -.
DR OrthoDB; 162808at2759; -.
DR PRO; PR:F4HRT5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HRT5; baseline and differential.
DR Genevisible; F4HRT5; AT.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IDA:TAIR.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0097298; P:regulation of nucleus size; IMP:UniProtKB.
DR InterPro; IPR040418; CRWN.
DR PANTHER; PTHR31908; PTHR31908; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1132
FT /note="Protein CROWDED NUCLEI 1"
FT /id="PRO_0000432819"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..714
FT /evidence="ECO:0000255"
FT MOTIF 379..386
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 693..700
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 856..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT MOD_RES 1112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 717
FT /note="E -> G (in Ref. 4; BAC41822)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1132 AA; 129093 MW; C8EBB673B212971B CRC64;
MSTPLKVWQR WSTPTKATNP DSNGSSHGTG LDMVTPVSGR VSEIQFDDPR ILPEKISELE
KELFEYQHSM GLLLIEKKEW SSQYEALQQA FEEVNECLKQ ERNAHLIAIA DVEKREEGLR
KALGIEKQCA LDLEKALKEL RAENAEIKFT ADSKLTEANA LVRSVEEKSL EVEAKLRAVD
AKLAEVSRKS SDVERKAKEV EARESSLQRE RFSYIAEREA DEATLSKQRE DLREWERKLQ
EGEERVAKSQ MIVKQREDRA NESDKIIKQK GKELEEAQKK IDAANLAVKK LEDDVSSRIK
DLALREQETD VLKKSIETKA RELQALQEKL EAREKMAVQQ LVDEHQAKLD STQREFELEM
EQKRKSIDDS LKSKVAEVEK REAEWKHMEE KVAKREQALD RKLEKHKEKE NDFDLRLKGI
SGREKALKSE EKALETEKKK LLEDKEIILN LKALVEKVSG ENQAQLSEIN KEKDELRVTE
EERSEYLRLQ TELKEQIEKC RSQQELLQKE AEDLKAQRES FEKEWEELDE RKAKIGNELK
NITDQKEKLE RHIHLEEERL KKEKQAANEN MERELETLEV AKASFAETME YERSMLSKKA
ESERSQLLHD IEMRKRKLES DMQTILEEKE RELQAKKKLF EEEREKELSN INYLRDVARR
EMMDMQNERQ RIEKEKLEVD SSKNHLEEQQ TEIRKDVDDL VALTKKLKEQ REQFISERSR
FLSSMESNRN CSRCGELLSE LVLPEIDNLE MPNMSKLANI LDNEAPRQEM RDISPTAAGL
GLPVTGGKVS WFRKCTSKML KLSPIKMTEP SVTWNLADQE PQSTEQANVG GPSTTVQAAT
TYSFDVQKAE SETGTKEVEV TNVNSDGDQS DINSKAQEVA ADSLSNLDVD GQSRMKGKGK
ARTRRTRSVK DVVDDAKALY GESINLYEPN DSTENVDDST KASTGETGRS DKAISKNGRK
RGRVGSLRTC TTEQDGNESD GKSDSVTGGA HQRKRRQKVA SEQQGEVVGQ RYNLRRPRRV
TGEPALSKKN EDIGGVQQEE GIHCTQATAT ASVGVAVSDN GVSTNVVQHE ATADSEDTDA
GSPKRTDESE AMSEDVNKTP LRADSDGEDD ESDAEHPGKV SIGKKLWTFL TT
