CRWN4_ARATH
ID CRWN4_ARATH Reviewed; 1010 AA.
AC Q9FLH0; F4JXK1; O49539;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Protein CROWDED NUCLEI 4 {ECO:0000303|PubMed:24308514};
DE AltName: Full=Protein LITTLE NUCLEI 4 {ECO:0000303|PubMed:17873096};
GN Name=CRWN4 {ECO:0000303|PubMed:24308514};
GN Synonyms=LINC4 {ECO:0000303|PubMed:17873096};
GN OrderedLocusNames=At5g65770 {ECO:0000312|Araport:AT5G65770};
GN ORFNames=F6H11.110 {ECO:0000312|EMBL:CAA16682.1},
GN MPA24.12 {ECO:0000312|EMBL:BAB10684.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP 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).
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). Involved in the maintenance of interphase
CC chromocenter integrity and organization (PubMed:24308514).
CC {ECO:0000250|UniProtKB:Q6ZWR6, ECO:0000269|PubMed:23396599,
CC 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 (By similarity). Binds to KAKU4 (PubMed:24824484).
CC {ECO:0000250|UniProtKB:F4HRT5, ECO:0000269|PubMed:24824484}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:23396599};
CC Peripheral membrane protein {ECO:0000269|PubMed:23396599}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:F4HRT5}. Nucleus lamina
CC {ECO:0000269|PubMed:23396599}. Cytoplasm {ECO:0000269|PubMed:23396599}.
CC Note=Recruited to the nucleus envelope (NE) by SUN proteins and is
CC immobilised therein (By similarity). Localized frequently to the
CC nuclear periphery as punctate structures of different sizes. During
CC prometaphase to anaphase, localized diffusely in the cytoplasm. Later
CC assembled into punctate structures in the cytoplasm and then to the
CC chromatin surface. Relocalized in part to the nuclear periphery during
CC late telophase, the other part is still localized on the punctate
CC structures (PubMed:23396599). {ECO:0000250|UniProtKB:F4HRT5,
CC ECO:0000269|PubMed:23396599}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000312|EMBL:AED98104.1};
CC Name=1;
CC IsoId=Q9FLH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FLH0-2; Sequence=VSP_057581, VSP_057582;
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 associated with reduced
CC chromocenter number and altered nuclear morphology. Plants lacking both
CC CRWN1 and CRWN4 or both CRWN2 and CRWN4 exhibit slightly smaller
CC rosettes. Plants lacking CRWN1, CRWN2 and CRWN4 or CRWN1, CRWN3 and
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16682.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At5g65770 and At5g65780.; Evidence={ECO:0000305};
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DR EMBL; AB010075; BAB10684.1; -; Genomic_DNA.
DR EMBL; AL021684; CAA16682.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98103.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98104.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98105.1; -; Genomic_DNA.
DR RefSeq; NP_001154799.1; NM_001161327.1. [Q9FLH0-2]
DR RefSeq; NP_001190626.1; NM_001203697.1. [Q9FLH0-1]
DR RefSeq; NP_201378.5; NM_125974.5. [Q9FLH0-1]
DR AlphaFoldDB; Q9FLH0; -.
DR SMR; Q9FLH0; -.
DR BioGRID; 21948; 2.
DR STRING; 3702.AT5G65780.2; -.
DR iPTMnet; Q9FLH0; -.
DR PaxDb; Q9FLH0; -.
DR PRIDE; Q9FLH0; -.
DR ProteomicsDB; 220316; -. [Q9FLH0-1]
DR EnsemblPlants; AT5G65770.1; AT5G65770.1; AT5G65770. [Q9FLH0-1]
DR EnsemblPlants; AT5G65770.2; AT5G65770.2; AT5G65770. [Q9FLH0-2]
DR EnsemblPlants; AT5G65770.3; AT5G65770.3; AT5G65770. [Q9FLH0-1]
DR GeneID; 836706; -.
DR Gramene; AT5G65770.1; AT5G65770.1; AT5G65770. [Q9FLH0-1]
DR Gramene; AT5G65770.2; AT5G65770.2; AT5G65770. [Q9FLH0-2]
DR Gramene; AT5G65770.3; AT5G65770.3; AT5G65770. [Q9FLH0-1]
DR KEGG; ath:AT5G65770; -.
DR Araport; AT5G65770; -.
DR TAIR; locus:2169950; AT5G65770.
DR eggNOG; ENOG502QT60; Eukaryota.
DR HOGENOM; CLU_008819_0_0_1; -.
DR InParanoid; Q9FLH0; -.
DR OMA; QDLAITQ; -.
DR OrthoDB; 248811at2759; -.
DR PRO; PR:Q9FLH0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLH0; differential.
DR Genevisible; Q9FLH0; AT.
DR GO; GO:0010369; C:chromocenter; IMP:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; 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:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI: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 Alternative splicing; Coiled coil; Cytoplasm; Membrane; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..1010
FT /note="Protein CROWDED NUCLEI 4"
FT /id="PRO_0000096871"
FT REGION 787..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 82..350
FT /evidence="ECO:0000255"
FT COILED 404..763
FT /evidence="ECO:0000255"
FT MOTIF 445..452
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 679..686
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 839..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 317
FT /note="E -> EVCFYSHNSLLFLVLHYRSSKKFLGDKI (in isoform 2)"
FT /id="VSP_057581"
FT VAR_SEQ 990..1010
FT /note="TGINASETVIHNEAATEDICT -> VVFMNSLKKNCLQTLQQMNNTLWLFL
FT (in isoform 2)"
FT /id="VSP_057582"
SQ SEQUENCE 1010 AA; 117086 MW; BBCE6168FCA00046 CRC64;
MATSSRSERF PITPSTAATN RLTITPNSRV LKSPLTEEIM WKRLKDAGFD EQSIKNRDKA
ALIAYIAKLE SEVYDYQHNM GLLLLEKNEL SSQYEEIKAS VDESDLTHMR EKSAYVSALA
EAKKREESLK KDVGIAKECI SSLEKTLHEM RAECAETKVS AGSTMSEAHV MIEDALKKLA
DAEAKMRAAE ALQAEANRYH RIAERKLKEV ESREDDLTRR LASFKSECET KENEMVIERQ
TLNERRKSLQ QEHERLLDAQ VSLNQREDHI FARSQELAEL EKGLDTAKTT FEEERKAFED
KKSNLEIALA LCAKREEAVS ERESSLLKKE QELLVAEEKI ASKESELIQN VLANQEVILR
KRKSDVEAEL ECKSKSVEVE IESKRRAWEL REVDIKQRED LVGEKEHDLE VQSRALAEKE
KDITEKSFNL DEKEKNLVAT EEDINRKTTM LEDEKERLRK LDLELQQSLT SLEDKRKRVD
SATQKLEALK SETSELSTLE MKLKEELDDL RAQKLEMLAE ADRLKVEKAK FEAEWEHIDV
KREELRKEAE YITRQREAFS MYLKDERDNI KEERDALRNQ HKNDVESLNR EREEFMNKMV
EEHSEWLSKI QRERADFLLG IEMQKRELEY CIENKREELE NSSRDREKAF EQEKKLEEER
IQSLKEMAEK ELEHVQVELK RLDAERLEIK LDRERREREW AELKDSVEEL KVQREKLETQ
RHMLRAERDE IRHEIEELKK LENLKVALDD MSMAKMQLSN LERSWEKVSA LKQKVVSRDD
ELDLQNGVST VSNSEDGYNS SMERQNGLTP SSATPFSWIK RCTNLIFKTS PEKSTLMHHY
EEEGGVPSEK LKLESSRREE KAYTEGLSIA VERLEAGRKR RGNTSGDETS EPSNNKKRKH
DVTQKYSDEA DTQSVISSPQ NVPEDKHELP SSQTQTPSGM VVISETVKIT RVTCETEVTN
KVTTLDCSES PSEAGRKMGE ETEDGDCNQT GINASETVIH NEAATEDICT
