CRWN2_ARATH
ID CRWN2_ARATH Reviewed; 1128 AA.
AC Q9SAF6; F4HP35; Q0WQM6; Q94AW6;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Protein CROWDED NUCLEI 2 {ECO:0000303|PubMed:24308514};
DE AltName: Full=Protein LITTLE NUCLEI 2 {ECO:0000303|PubMed:17873096};
GN Name=CRWN2 {ECO:0000303|PubMed:24308514};
GN Synonyms=LINC2 {ECO:0000303|PubMed:17873096};
GN OrderedLocusNames=At1g13220 {ECO:0000312|Araport:AT1G13220};
GN ORFNames=F3F19.25 {ECO:0000312|EMBL:AAD31075.1};
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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [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 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 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 [8]
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:17873096,
CC PubMed:24308514, PubMed:23396599). {ECO:0000250|UniProtKB:Q6ZWR6,
CC ECO:0000269|PubMed:17873096, 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. {ECO:0000250|UniProtKB:F4HRT5}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:17873096};
CC Peripheral membrane protein {ECO:0000269|PubMed:17873096}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599}.
CC Cytoplasm {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). Mostly
CC localized in the nucleoplasm and, to a lesser extent, at the nuclear
CC periphery (PubMed:17873096). During prometaphase to anaphase, localized
CC diffusely in the cytoplasm. A small population is later transferred
CC from the cytoplasm to the chromatin surface. Relocalized to the nuclear
CC periphery during late telophase (PubMed:23396599).
CC {ECO:0000250|UniProtKB:F4HRT5, ECO:0000269|PubMed:17873096,
CC ECO:0000269|PubMed:23396599}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CRWN2 {ECO:0000303|PubMed:24308514};
CC IsoId=Q9SAF6-1; Sequence=Displayed;
CC Name=2; Synonyms=CRWN2S {ECO:0000303|PubMed:24308514};
CC IsoId=Q9SAF6-2; Sequence=VSP_057578, VSP_057579, VSP_057580;
CC Name=3;
CC IsoId=Q9SAF6-3; Sequence=VSP_057577;
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. In plants lacking
CC both CRWN1 and CRWN2, moderate dwarf and leaf-curling phenotype
CC associated with endoreplication and strongly reduced nuclear size.
CC Plants lacking both CRWN2 and CRWN4 exhibit slightly smaller rosettes.
CC Plants lacking both CRWN1 and CRWN2 exhibit markedly smaller rosettes.
CC Plants lacking CRWN1, CRWN2 and CRWN4 are extremely stunted and set few
CC seed. {ECO:0000269|PubMed:17873096, ECO:0000269|PubMed:23396599,
CC ECO:0000269|PubMed:24308514}.
CC -!- SIMILARITY: Belongs to the CRWN family. {ECO:0000305}.
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DR EMBL; AC007357; AAD31075.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28986.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28987.1; -; Genomic_DNA.
DR EMBL; AY045658; AAK74016.1; -; mRNA.
DR EMBL; BT000576; AAN18145.1; -; mRNA.
DR EMBL; AK228666; BAF00573.1; -; mRNA.
DR PIR; G86266; G86266.
DR RefSeq; NP_563923.1; NM_101193.3. [Q9SAF6-2]
DR RefSeq; NP_563924.1; NM_101194.2. [Q9SAF6-1]
DR AlphaFoldDB; Q9SAF6; -.
DR SMR; Q9SAF6; -.
DR STRING; 3702.AT1G13220.2; -.
DR iPTMnet; Q9SAF6; -.
DR PaxDb; Q9SAF6; -.
DR PRIDE; Q9SAF6; -.
DR ProteomicsDB; 224548; -. [Q9SAF6-1]
DR EnsemblPlants; AT1G13220.1; AT1G13220.1; AT1G13220. [Q9SAF6-2]
DR EnsemblPlants; AT1G13220.2; AT1G13220.2; AT1G13220. [Q9SAF6-1]
DR GeneID; 837882; -.
DR Gramene; AT1G13220.1; AT1G13220.1; AT1G13220. [Q9SAF6-2]
DR Gramene; AT1G13220.2; AT1G13220.2; AT1G13220. [Q9SAF6-1]
DR KEGG; ath:AT1G13220; -.
DR Araport; AT1G13220; -.
DR TAIR; locus:2031875; AT1G13220.
DR eggNOG; ENOG502QUGA; Eukaryota.
DR HOGENOM; CLU_004241_0_0_1; -.
DR InParanoid; Q9SAF6; -.
DR PhylomeDB; Q9SAF6; -.
DR PRO; PR:Q9SAF6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SAF6; baseline and differential.
DR Genevisible; Q9SAF6; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005652; C:nuclear lamina; IEA:UniProtKB-SubCell.
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: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; Isopeptide bond; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1128
FT /note="Protein CROWDED NUCLEI 2"
FT /id="PRO_0000432820"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..365
FT /evidence="ECO:0000255"
FT COILED 391..730
FT /evidence="ECO:0000255"
FT MOTIF 966..973
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 902..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4HRT5"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F4HRT5"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9CA42"
FT VAR_SEQ 1..385
FT /note="Missing (in isoform 3)"
FT /id="VSP_057577"
FT VAR_SEQ 1
FT /note="M -> MFTPQRKQWMSPAM (in isoform 2)"
FT /id="VSP_057578"
FT VAR_SEQ 369..378
FT /note="TEIQKLIDDQ -> VILGYSFCRL (in isoform 2)"
FT /id="VSP_057579"
FT VAR_SEQ 379..1128
FT /note="Missing (in isoform 2)"
FT /id="VSP_057580"
FT CONFLICT 66
FT /note="F -> L (in Ref. 3; AAK74016/AAN18145)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="N -> I (in Ref. 3; AAK74016/AAN18145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1128 AA; 129924 MW; AB68E50F7C1DBFCA CRC64;
MTPRSETHKI GGVTNPRNAD RKGKAVAFSD DLVIPTLPPP PIGTLTGQGV SRGHTDDMDM
GDWRRFREVG LLNEASMEKK DQEALLEKIS TLEKELYGYQ HNMGLLLMEN KELVSKHEQL
NQAFQEAQEI LKREQSSHLY ALTTVEQREE NLRKALGLEK QCVQELEKAL REIQEENSKI
RLSSEAKLVE ANALVASVNG RSSDVENKIY SAESKLAEAT RKSSELKLRL KEVETRESVL
QQERLSFTKE RESYEGTFQK QREYLNEWEK KLQGKEESIT EQKRNLNQRE EKVNEIEKKL
KLKEKELEEW NRKVDLSMSK SKETEEDITK RLEELTTKEK EAHTLQITLL AKENELRAFE
EKLIAREGTE IQKLIDDQKE VLGSKMLEFE LECEEIRKSL DKELQRKIEE LERQKVEIDH
SEEKLEKRNQ AMNKKFDRVN EKEMDLEAKL KTIKEREKII QAEEKRLSLE KQQLLSDKES
LEDLQQEIEK IRAEMTKKEE MIEEECKSLE IKKEEREEYL RLQSELKSQI EKSRVHEEFL
SKEVENLKQE KERFEKEWEI LDEKQAVYNK ERIRISEEKE KFERFQLLEG ERLKKEESAL
RVQIMQELDD IRLQRESFEA NMEHERSALQ EKVKLEQSKV IDDLEMMRRN LEIELQERKE
QDEKDLLDRM AQFEDKRMAE LSDINHQKQA LNREMEEMMS KRSALQKESE EIAKHKDKLK
EQQVEMHNDI SELSTLSINL KKRREVFGRE RSRFLAFVQK LKDCGSCGQL VNDFVLSDLQ
LPSNDEVAIL PPIGVLNDLP GSSNASDSCN IKKSLDGDAS GSGGSRRPSM SILQKCTSII
FSPSKRVEHG IDTGKPEQRL SSSVAVGMET KGEKPLPVDL RLRPSSSSIP EEDEEYTDSR
VQETSEGSQL SEFQSSRRGR GRPRKAKPAL NPTSSVKHAS LEESSKDELS GHVSVTSKKT
TGGGGRKRQH IDDTATGGKR RRQQTVAVLP QTPGQRHYNL RRKKTVDQVP ADVEDNAAAG
EDDADIAASA PSKDTVEETV VETLRARRIE TNADVVSAEN NGDVPVANVE PTVNEDTNED
GDEEEDEAQD DDNEENQDDD DDDDGDDDGS PRPGEGSIRK KLWTFLTT
