WIP2_ARATH
ID WIP2_ARATH Reviewed; 509 AA.
AC Q9FH18; Q5XUY7; Q5XUY8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=WPP domain-interacting protein 2;
GN Name=WIP2; OrderedLocusNames=At5g56210; ORFNames=K24C1.2;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Xiao Y.-L., Underwood B.A., Moskal W.A. Jr., Wang W., Redman J.C., Wu H.C.,
RA Utterback T., Town C.D.;
RT "Reconstruction of cDNA sequences for hypothetical genes in Arabidopsis
RT thaliana from 5' and 3' RACE products.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP INTERACTION WITH RANGAP1; RANGAP2; WPP1 AND WPP2, AND DIMERIZATION.
RX PubMed=17600715; DOI=10.1016/j.cub.2007.05.076;
RA Xu X.M., Meulia T., Meier I.;
RT "Anchorage of plant RanGAP to the nuclear envelope involves novel nuclear-
RT pore-associated proteins.";
RL Curr. Biol. 17:1157-1163(2007).
RN [6]
RP INTERACTION WITH WIT1.
RX PubMed=18591351; DOI=10.1105/tpc.108.059220;
RA Zhao Q., Brkljacic J., Meier I.;
RT "Two distinct interacting classes of nuclear envelope-associated coiled-
RT coil proteins are required for the tissue-specific nuclear envelope
RT targeting of Arabidopsis RanGAP.";
RL Plant Cell 20:1639-1651(2008).
RN [7]
RP INTERACTION WITH SUN1 AND SUN2, AND SUBCELLULAR 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 INTERACTION WITH KIN1.
RX PubMed=25330379; DOI=10.1371/journal.pgen.1004674;
RA Duroc Y., Lemhemdi A., Larcheveque C., Hurel A., Cuacos M., Cromer L.,
RA Horlow C., Armstrong S.J., Chelysheva L., Mercier R.;
RT "The kinesin AtPSS1 promotes synapsis and is required for proper crossover
RT distribution in meiosis.";
RL PLoS Genet. 10:E1004674-E1004674(2014).
RN [9]
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 [10]
RP FUNCTION, INTERACTION WITH WIT2, 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).
CC -!- FUNCTION: Mediates and enhances the nuclear envelope docking of RANGAP
CC proteins mediated by WIT1 and WIT2 in the undifferentiated cells of
CC root tips (PubMed:17600715). 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:17600715, ECO:0000269|PubMed:25759303}.
CC -!- SUBUNIT: Homodimer, and heterodimer with WIP1. Component of Ran
CC complexes at least composed of WIT1 or WIT2, RANGAP1 or RANGAP2, and
CC WIP1 or WIP2 or WIP3. Interacts with RANGAP1, RANGAP2, WIT1, WPP1/MAF1,
CC and WPP2/MAF2 (PubMed:17600715, PubMed:18591351). Interacts with SUN1
CC and SUN2 (PubMed:22270916). Interacts with KIN1 (PubMed:25330379). Core
CC component of the LINC complex which is composed of inner nuclear
CC membrane SUN domain-containing proteins coupled to outer nuclear
CC membrane WIP and WIT proteins. The LINC complex also involves
CC nucleoskeletal proteins CRWN/LINC and possibly KAKU4 and the
CC cytoskeletal myosin KAKU1 (PubMed:25759303). Interacts with WIT2
CC (PubMed:25759303). {ECO:0000269|PubMed:17600715,
CC ECO:0000269|PubMed:18591351, ECO:0000269|PubMed:22270916,
CC ECO:0000269|PubMed:25330379, ECO:0000269|PubMed:25759303}.
CC -!- INTERACTION:
CC Q9FH18; Q8GXA4: WIP1; NbExp=3; IntAct=EBI-1779466, EBI-1779367;
CC Q9FH18-1; Q8L7E5: WIT1; NbExp=2; IntAct=EBI-1954306, EBI-1796628;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:17600715,
CC ECO:0000269|PubMed:22270916}. Nucleus membrane
CC {ECO:0000269|PubMed:17600715}; Single-pass membrane protein
CC {ECO:0000269|PubMed:17600715}; Cytoplasmic side
CC {ECO:0000269|PubMed:17600715}. Note=Targeted to the nuclear envelope
CC (NE) during interphase. Associated to the cell plate during cytokinesis
CC in root tips.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=WIP2a;
CC IsoId=Q9FH18-1; Sequence=Displayed;
CC Name=2; Synonyms=WIP2b;
CC IsoId=Q9FH18-2; Sequence=VSP_035071;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, leaves, and
CC flowers. {ECO:0000269|PubMed:17600715}.
CC -!- DEVELOPMENTAL STAGE: First observed in roots and cotyledons of young
CC developing seedlings. Later confined to root tips and vascular tissue
CC around the shoot apex. In flowers, detected in the stamens and at the
CC senescence region of developing siliques.
CC {ECO:0000269|PubMed:17600715}.
CC -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC mediates the nuclear envelope targeting and is involved in the binding
CC to the SUN proteins. {ECO:0000305}.
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DR EMBL; AB023029; BAB09112.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96735.1; -; Genomic_DNA.
DR EMBL; AY735734; AAU44604.1; -; mRNA.
DR EMBL; AY735735; AAU44605.1; -; mRNA.
DR EMBL; AY924865; AAX23940.1; -; mRNA.
DR RefSeq; NP_200432.1; NM_125004.3. [Q9FH18-1]
DR AlphaFoldDB; Q9FH18; -.
DR SMR; Q9FH18; -.
DR BioGRID; 20964; 6.
DR IntAct; Q9FH18; 8.
DR STRING; 3702.AT5G56210.1; -.
DR iPTMnet; Q9FH18; -.
DR PaxDb; Q9FH18; -.
DR PRIDE; Q9FH18; -.
DR ProteomicsDB; 242658; -. [Q9FH18-1]
DR EnsemblPlants; AT5G56210.1; AT5G56210.1; AT5G56210. [Q9FH18-1]
DR GeneID; 835720; -.
DR Gramene; AT5G56210.1; AT5G56210.1; AT5G56210. [Q9FH18-1]
DR KEGG; ath:AT5G56210; -.
DR Araport; AT5G56210; -.
DR TAIR; locus:2156440; AT5G56210.
DR eggNOG; ENOG502QTZN; Eukaryota.
DR HOGENOM; CLU_032522_0_0_1; -.
DR InParanoid; Q9FH18; -.
DR OMA; KAECKDL; -.
DR PhylomeDB; Q9FH18; -.
DR PRO; PR:Q9FH18; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH18; baseline and differential.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006997; P:nucleus organization; IGI:TAIR.
DR InterPro; IPR044696; WIP1/2/3.
DR PANTHER; PTHR34562; PTHR34562; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="WPP domain-interacting protein 2"
FT /id="PRO_0000347197"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 483..509
FT /note="KASH"
FT /evidence="ECO:0000305"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 277..302
FT /evidence="ECO:0000255"
FT COILED 340..389
FT /evidence="ECO:0000255"
FT COILED 431..470
FT /evidence="ECO:0000255"
FT MOTIF 44..45
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 47..48
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT MOTIF 70..71
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000250"
FT COMPBIAS 132..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..219
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035071"
SQ SEQUENCE 509 AA; 56514 MW; 28500632BE3A4EBB CRC64;
MDLESESSVL ESVEDNNGLI GDLDKELNSP VETSPLISKG FGLRKWKRRL RRDLVKDDTS
VSMENSKALK RVLSGLVDPN AKQMHLPGPE VRQDSVGSVG SVNSVVGFVM GGESYGNGLA
FAAGVDSDNS EDRSSTMSHS WDKHRGKVSG GKSVISSGDS SQQRKSSVEK SNKLRGERIK
IEKENSHSSM ESADSRSSNF VFMQGASYSL SSREQGGRRM MDYDDENSDH DAHTSKRKDN
VEEEEEETED YSQGDCVEES QIKSNGSSDN LDPLIVAVNS FQTLQEALQK ELQKFQELGK
EEPITSLHDG GESSSCIHAG HEGASEASSS YRFGSEKMGE MELTSLDSEI LNLVNNVEHL
EIKLEEAKRI LEVKETQIRE LESTINVSET CNGGTEIGIE DIFQQKVEAE IEYIIFSRSV
GNLKRRIKLI EEEKTLGLSK LDKAETKAEN LKNQAQDLQN HCVEITEIQE VECLKKRAFK
TTRCLLLQLG LLFILYYSLL PEPEIAVPT
