CRWN3_ARATH
ID CRWN3_ARATH Reviewed; 1085 AA.
AC Q9CA42;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Protein CROWDED NUCLEI 3 {ECO:0000303|PubMed:24308514};
DE AltName: Full=Protein LITTLE NUCLEI 3 {ECO:0000303|PubMed:17873096};
GN Name=CRWN3 {ECO:0000303|PubMed:24308514};
GN Synonyms=LINC3 {ECO:0000303|PubMed:17873096};
GN OrderedLocusNames=At1g68790 {ECO:0000312|Araport:AT1G68790};
GN ORFNames=F14K14.10 {ECO:0000312|EMBL:AAG52034.1};
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 1-1059.
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-318 AND LYS-661, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [5]
RP GENE FAMILY, AND 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-843 AND SER-910, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, 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 [8]
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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).
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:24308514,
CC PubMed:23396599). {ECO:0000250|UniProtKB:Q6ZWR6,
CC ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514}.
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 proteins, the nucleoskeletal CRWN/LINC proteins,
CC and, possibly, KAKU4. {ECO:0000250|UniProtKB:F4HRT5}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:F4HRT5};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:F4HRT5}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:23396599}. Cytoplasm
CC {ECO:0000269|PubMed:23396599}. Nucleus lamina
CC {ECO:0000250|UniProtKB:F4HRT5}. Note=Recruited to the nucleus envelope
CC (NE) by SUN proteins and is immobilised therein (By similarity).
CC Punctate or bundle-like structures are detected, especially in
CC trichomes where bundle-shape localization pattern along the long axis
CC of the nucleus is observed. During prometaphase to anaphase, localized
CC diffusely in the cytoplasm. Later transferred from the cytoplasm to the
CC chromatin surface, preferentially assembling to the distal surface of
CC the chromatin. Relocalized to the nuclear periphery during late
CC telophase (PubMed:23396599). {ECO:0000250|UniProtKB:F4HRT5,
CC ECO:0000269|PubMed:23396599}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, leaves, flowers
CC and flower stalks. {ECO:0000269|PubMed:23396599}.
CC -!- DISRUPTION PHENOTYPE: Altered nuclear morphology. Plants lacking both
CC CRWN1 and CRWN3 exhibit markedly smaller rosettes. Plants lacking
CC CRWN1, CRWN3 and CRWN4 are extremely stunted and set few seed.
CC {ECO:0000269|PubMed:23396599, ECO:0000269|PubMed:24308514}.
CC -!- SIMILARITY: Belongs to the CRWN family. {ECO:0000305}.
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DR EMBL; AC011914; AAG52034.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34839.1; -; Genomic_DNA.
DR EMBL; AY072196; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; F96712; F96712.
DR RefSeq; NP_177046.1; NM_105552.3.
DR AlphaFoldDB; Q9CA42; -.
DR SMR; Q9CA42; -.
DR IntAct; Q9CA42; 2.
DR STRING; 3702.AT1G68790.1; -.
DR iPTMnet; Q9CA42; -.
DR PaxDb; Q9CA42; -.
DR PRIDE; Q9CA42; -.
DR ProteomicsDB; 224502; -.
DR EnsemblPlants; AT1G68790.1; AT1G68790.1; AT1G68790.
DR GeneID; 843210; -.
DR Gramene; AT1G68790.1; AT1G68790.1; AT1G68790.
DR KEGG; ath:AT1G68790; -.
DR Araport; AT1G68790; -.
DR TAIR; locus:2012423; AT1G68790.
DR eggNOG; ENOG502QUGA; Eukaryota.
DR HOGENOM; CLU_004241_0_0_1; -.
DR InParanoid; Q9CA42; -.
DR OMA; EKKEWTA; -.
DR OrthoDB; 162808at2759; -.
DR PhylomeDB; Q9CA42; -.
DR PRO; PR:Q9CA42; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CA42; baseline and differential.
DR Genevisible; Q9CA42; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR InterPro; IPR040418; CRWN.
DR PANTHER; PTHR31908; PTHR31908; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1085
FT /note="Protein CROWDED NUCLEI 3"
FT /id="PRO_0000432821"
FT REGION 801..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..149
FT /evidence="ECO:0000255"
FT COILED 185..695
FT /evidence="ECO:0000255"
FT MOTIF 404..411
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 809..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1068
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4HRT5"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4HRT5"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4HRT5"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 910
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT CROSSLNK 318
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
FT CROSSLNK 661
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
SQ SEQUENCE 1085 AA; 127204 MW; ED0F40CA45BE355B CRC64;
MFTPQRNRWP ETDRKGKAIA FSDEIITPPP QRVLLREDDD WQKFKEVGLL DEASLERKDR
DALIEKILKL EKELFDYQHN MGLLLIEKKQ WTSTNNELQQ AYDEAMEMLK REKTSNAITL
NEADKREENL RKALIDEKQF VAELENDLKY WQREHSVVKS TSEAKLEEAN ALVIGMKEKA
LEVDRERAIA EEKFSVMNRK SSELERKLKE VETREKVHQR EHLSLVTERE AHEAVFYKQR
EDLQEWEKKL TLEEDRLSEV KRSINHREER VMENERTIEK KEKILENLQQ KISVAKSELT
EKEESIKIKL NDISLKEKDF EAMKAKVDIK EKELHEFEEN LIEREQMEIG KLLDDQKAVL
DSRRREFEME LEQMRRSLDE ELEGKKAEIE QLQVEISHKE EKLAKREAAL EKKEEGVKKK
EKDLDARLKT VKEKEKALKA EEKKLHMENE RLLEDKECLR KLKDEIEEIG TETTKQESRI
REEHESLRIT KEERVEFLRL QSELKQQIDK VKQEEELLLK EREELKQDKE RFEKEWEALD
KKRANITREQ NEVAEENEKL RNLQISEKHR LKREEMTSRD NLKRELDGVK MQKESFEADM
EDLEMQKRNL DMEFQRQEEA GERDFNERAR TYEKRSQEEL DNINYTKKLA QREMEEMQYE
KLALEREREQ ISVRKKLLKE QEAEMHKDIT ELDVLRSSLK EKRKEFICER ERFLVFLEKL
KSCSSCGEIT ENFVLSDLRL PDVEDGDKRF GKQKLKAEEA LNISPSAENS KRTSLLGKIA
SKLLSISPIG KTDKVTDLGI TVKLPESSQP DDSLDRVSGE DHEPSATEQS FTDSRIQEGP
EGSLQSEMKS DKPRRGRGRG RGRGKSVRGR SQATKAVSRD SKPSDGETPR KRQREQTSRI
TESEQAAGDS DEGVDSITTG GRRKKRQIAV PVSQTPGQTR YQLRRHRNVG TEEDKAQASK
GATEKQERVN DDIRKVPSPK ETRTPPEGEN RENGKAEVLV ETVTHEEIVT VETETVFKVN
NTGKNPVEDP QLEVGGSGEI REHGEEDDEN ISMIEEENEG EEEEETERQG NDASIGKKIW
VFFTT
