SUN1_ARATH
ID SUN1_ARATH Reviewed; 471 AA.
AC Q9FF75;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=SUN domain-containing protein 1 {ECO:0000303|PubMed:19807882};
DE Short=AtSUN1 {ECO:0000303|PubMed:19807882};
GN Name=SUN1 {ECO:0000303|PubMed:19807882};
GN OrderedLocusNames=At5g04990 {ECO:0000312|Araport:AT5G04990};
GN ORFNames=MUG13.15 {ECO:0000312|EMBL:BAB11521.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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 [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=19807882; DOI=10.1111/j.1365-313x.2009.04038.x;
RA Graumann K., Runions J., Evans D.E.;
RT "Characterization of SUN-domain proteins at the higher plant nuclear
RT envelope.";
RL Plant J. 61:134-144(2010).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21294795; DOI=10.1111/j.1365-313x.2011.04523.x;
RA Oda Y., Fukuda H.;
RT "Dynamics of Arabidopsis SUN proteins during mitosis and their involvement
RT in nuclear shaping.";
RL Plant J. 66:629-641(2011).
RN [7]
RP FUNCTION, INTERACTION WITH WIP1; WIP2 AND WIP3, SUN DOMAIN, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22270916; DOI=10.1083/jcb.201108098;
RA Zhou X., Graumann K., Evans D.E., Meier I.;
RT "Novel plant SUN-KASH bridges are involved in RanGAP anchoring and nuclear
RT shape determination.";
RL J. Cell Biol. 196:203-211(2012).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP INTERACTION WITH SINE1; SINE2; SINE3 AND SINE4, AND MUTAGENESIS OF HIS-439
RP AND TYR-443.
RX PubMed=24891605; DOI=10.1083/jcb.201401138;
RA Zhou X., Graumann K., Wirthmueller L., Jones J.D., Meier I.;
RT "Identification of unique SUN-interacting nuclear envelope proteins with
RT diverse functions in plants.";
RL J. Cell Biol. 205:677-692(2014).
RN [10]
RP SUBUNIT, AND INTERACTION WITH SUN3; SUN4 AND TIK.
RX PubMed=25217773; DOI=10.1093/jxb/eru368;
RA Graumann K., Vanrobays E., Tutois S., Probst A.V., Evans D.E., Tatout C.;
RT "Characterization of two distinct subfamilies of SUN-domain proteins in
RT Arabidopsis and their interactions with the novel KASH-domain protein
RT AtTIK.";
RL J. Exp. Bot. 65:6499-6512(2014).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH LINC1.
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 [12]
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).
RN [13]
RP FUNCTION, AND SUBUNIT.
RX PubMed=25759303; DOI=10.1080/19491034.2014.1003512;
RA Zhou X., Groves N.R., Meier I.;
RT "Plant nuclear shape is independently determined by the SUN-WIP-WIT2-myosin
RT XI-i complex and CRWN1.";
RL Nucleus 6:144-153(2015).
RN [14]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25412930; DOI=10.1111/tpj.12730;
RA Varas J., Graumann K., Osman K., Pradillo M., Evans D.E., Santos J.L.,
RA Armstrong S.J.;
RT "Absence of SUN1 and SUN2 proteins in Arabidopsis thaliana leads to a delay
RT in meiotic progression and defects in synapsis and recombination.";
RL Plant J. 81:329-346(2015).
RN [15]
RP INTERACTION WITH NEAP1; NEAP2 AND NEAP3.
RX PubMed=27630107; DOI=10.1093/jxb/erw332;
RA Pawar V., Poulet A., Detourne G., Tatout C., Vanrobays E., Evans D.E.,
RA Graumann K.;
RT "A novel family of plant nuclear envelope-associated proteins.";
RL J. Exp. Bot. 67:5699-5710(2016).
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 (PubMed:24667841, PubMed:25759303).
CC Required for the maintenance and/or formation of polarized nuclear
CC shape in root hairs (PubMed:21294795, PubMed:25759303). Modulates the
CC anchoring and mobility of WIP proteins and RANGAP1 in the nuclear
CC envelope (NE) (PubMed:22270916). In association with SUN2, may be
CC involved in telomere attachment to nuclear envelope in the prophase of
CC meiosis (PubMed:25412930). As component of the SUN-WIP-WIT2-KAKU1
CC complex, mediates the transfer of cytoplasmic forces to the nuclear
CC envelope (NE), leading to nuclear shape changes (PubMed:25759303).
CC {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:22270916,
CC ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930,
CC ECO:0000269|PubMed:25759303}.
CC -!- SUBUNIT: Forms homomers (e.g. dimers, trimers and tetramers) and
CC heteromers with SUN2 (PubMed:19807882, PubMed:25217773). Interacts with
CC SUN3, SUN4 and TIK (PubMed:25217773). Core component of the LINC
CC complex which is composed of inner nuclear membrane SUN domain-
CC containing proteins coupled to outer nuclear membrane WIP and WIT
CC proteins. The LINC complex also involves nucleoskeletal proteins
CC CRWN/LINC and possibly KAKU4 and the cytoskeletal myosin KAKU1
CC (PubMed:25759303). Interacts with LINC1, WIP1, WIP2 and WIP3 at the
CC nuclear envelope (NE) (PubMed:22270916, PubMed:24667841). Interacts
CC with SINE1, SINE2, SINE3 AND SINE4 (PubMed:24891605). Interacts with
CC NEAP1, NEA2 and NEAP3 (PubMed:27630107). {ECO:0000269|PubMed:19807882,
CC ECO:0000269|PubMed:22270916, ECO:0000269|PubMed:24667841,
CC ECO:0000269|PubMed:24891605, ECO:0000269|PubMed:25217773,
CC ECO:0000269|PubMed:25759303, ECO:0000269|PubMed:27630107}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:19807882, ECO:0000269|PubMed:21294795,
CC ECO:0000269|PubMed:24667841, ECO:0000269|PubMed:25412930}; Single-pass
CC type II membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton,
CC phragmoplast {ECO:0000269|PubMed:21294795}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:21294795}; Single-pass type II membrane
CC protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:22270916}.
CC Note=Dynamic localization during mitosis and meosis, tightly coupled
CC with nuclear envelope (NE) dynamics. Localized with the nuclear
CC envelope during meiotic prophase I. NE re-formation during metaphase is
CC temporally and spatially coordinated with plant-specific microtubule
CC structures such as phragmoplasts. During anaphase, after NE breakdown
CC (NEBD), predominantly localized with the endoplasmic reticulum, in the
CC outside of the segregated chromosomes and not in between segregated
CC chromosomes. {ECO:0000269|PubMed:21294795,
CC ECO:0000269|PubMed:25412930}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, cotyledons and
CC leaves and inflorescences. {ECO:0000269|PubMed:19807882,
CC ECO:0000269|PubMed:21294795}.
CC -!- DOMAIN: The SUN domain may play a role in nuclear anchoring and/or
CC migration (By similarity). The SUN domain is required for interactions
CC with WIP proteins (PubMed:22270916). {ECO:0000250|UniProtKB:O94901,
CC ECO:0000269|PubMed:22270916}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. When associated with SUN2
CC disruption, abnormal nuclear shape, rounded instead of elongated, in
CC some cells (e.g. mature root hairs) but also numerous meiotic defects
CC namely a delay in the progression of meiosis, absence of full synapsis
CC and a reduction in the mean cell chiasma frequency.
CC {ECO:0000269|PubMed:21294795, ECO:0000269|PubMed:25412930}.
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DR EMBL; AB005245; BAB11521.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90813.1; -; Genomic_DNA.
DR EMBL; AY056433; AAL08289.1; -; mRNA.
DR EMBL; AY113173; AAM47476.1; -; mRNA.
DR RefSeq; NP_196118.1; NM_120581.5.
DR AlphaFoldDB; Q9FF75; -.
DR SMR; Q9FF75; -.
DR IntAct; Q9FF75; 4.
DR STRING; 3702.AT5G04990.1; -.
DR iPTMnet; Q9FF75; -.
DR PaxDb; Q9FF75; -.
DR PRIDE; Q9FF75; -.
DR ProteomicsDB; 228286; -.
DR EnsemblPlants; AT5G04990.1; AT5G04990.1; AT5G04990.
DR GeneID; 830381; -.
DR Gramene; AT5G04990.1; AT5G04990.1; AT5G04990.
DR KEGG; ath:AT5G04990; -.
DR Araport; AT5G04990; -.
DR TAIR; locus:2175354; AT5G04990.
DR eggNOG; KOG2687; Eukaryota.
DR HOGENOM; CLU_043737_3_0_1; -.
DR InParanoid; Q9FF75; -.
DR OMA; SSYETEM; -.
DR OrthoDB; 1569602at2759; -.
DR PhylomeDB; Q9FF75; -.
DR PRO; PR:Q9FF75; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FF75; baseline and differential.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IEA:InterPro.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IDA:UniProtKB.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; IMP:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IDA:UniProtKB.
DR GO; GO:2000769; P:regulation of establishment or maintenance of cell polarity regulating cell shape; IMP:UniProtKB.
DR InterPro; IPR045119; SUN1-5.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12911; PTHR12911; 1.
DR Pfam; PF07738; Sad1_UNC; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..471
FT /note="SUN domain-containing protein 1"
FT /id="PRO_0000432816"
FT TOPO_DOM 2..105
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..471
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT DOMAIN 288..452
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 19..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 175..225
FT /evidence="ECO:0000255"
FT MOTIF 88..95
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 59..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MUTAGEN 439
FT /note="H->A: Strongly affects binding to SINE1, SINE2,
FT SINE3 and SINE4; when associated with F-443."
FT /evidence="ECO:0000269|PubMed:24891605"
FT MUTAGEN 443
FT /note="Y->F: Strongly affects binding to SINE1, SINE2,
FT SINE3 and SINE4; when associated with A-439."
FT /evidence="ECO:0000269|PubMed:24891605"
SQ SEQUENCE 471 AA; 51502 MW; 04EA132C5D01C5B6 CRC64;
MSASTVSITA NTAAATRRTP ILAGEKKSNF DYPQSESLAN GGVGEAGGTS RDLSRGEATL
DRSQGQDLGP VTRRSVSAAT GTNTTATQRR TRKVATPKSE KARWKTVVRI FAKQLGALLI
IVGLIQLTRK MILKASSPSS PISSYETEMA FSGLESRIAE VDGLVKATTN SMQVQVELLD
KKMEREAKVL RQEIERKASA FQSELKKIES RTESLEKSVD EVNAKPWVTK DELERIYEEL
KKGNVDDSAF SEISIDELRA YARDIMEKEI EKHAADGLGR VDYALASGGA FVMEHSDPYL
VGKGSSWFAT TMRRAHTNAV KMLSPSFGEP GQCFPLKGSE GYVQIRLRGP IIPEAFTLEH
VAKSVAYDRS SAPKDCRVSG SLQGPESSAE TENMQLLTEF TYDLDRSNAQ TFNILESSSS
GLIDTVRLDF TSNHGSDSHT CIYRFRVHGR APDPVPVVGT NLDQDSSPES E
