WIP3_ARATH
ID WIP3_ARATH Reviewed; 459 AA.
AC Q94AV5; Q9LTT2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=WPP domain-interacting protein 3;
GN Name=WIP3; OrderedLocusNames=At3g13360; ORFNames=MDC11.15;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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 FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH RANGAP1; WPP1 AND WPP2.
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 [5]
RP IDENTIFICATION BY 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 [6]
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 [7]
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 [8]
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: Component of Ran complexes at least composed of WIT1 or WIT2,
CC RANGAP1 or RANGAP2, and WIP1 or WIP2 or WIP3 (By similarity). Interacts
CC with RANGAP1, WPP1/MAF1, and WPP2/MAF2 (PubMed:17600715). Interacts
CC with SUN1 and SUN2 (PubMed:22270916). 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 WIT2 (PubMed:25759303). {ECO:0000250,
CC ECO:0000269|PubMed:17600715, ECO:0000269|PubMed:22270916,
CC ECO:0000269|PubMed:25759303}.
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}.
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 cauline leaves
CC tips. In flowers, detected in the stamens and at the senescence region
CC of developing siliques. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02805.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024034; BAB02805.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75338.1; -; Genomic_DNA.
DR EMBL; AY045697; AAK74055.1; -; mRNA.
DR EMBL; AY149963; AAN31117.1; -; mRNA.
DR RefSeq; NP_566455.1; NM_112181.5.
DR AlphaFoldDB; Q94AV5; -.
DR BioGRID; 5870; 2.
DR IntAct; Q94AV5; 4.
DR STRING; 3702.AT3G13360.1; -.
DR iPTMnet; Q94AV5; -.
DR PaxDb; Q94AV5; -.
DR PRIDE; Q94AV5; -.
DR ProteomicsDB; 242643; -.
DR EnsemblPlants; AT3G13360.1; AT3G13360.1; AT3G13360.
DR GeneID; 820536; -.
DR Gramene; AT3G13360.1; AT3G13360.1; AT3G13360.
DR KEGG; ath:AT3G13360; -.
DR Araport; AT3G13360; -.
DR TAIR; locus:2088170; AT3G13360.
DR eggNOG; ENOG502QTZN; Eukaryota.
DR HOGENOM; CLU_057777_0_0_1; -.
DR InParanoid; Q94AV5; -.
DR OMA; GTIRSMH; -.
DR PhylomeDB; Q94AV5; -.
DR PRO; PR:Q94AV5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94AV5; baseline and differential.
DR Genevisible; Q94AV5; AT.
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:0006997; P:nucleus organization; IGI:TAIR.
DR InterPro; IPR044696; WIP1/2/3.
DR PANTHER; PTHR34562; PTHR34562; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..459
FT /note="WPP domain-interacting protein 3"
FT /id="PRO_0000347198"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 426..459
FT /note="KASH"
FT /evidence="ECO:0000305"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..375
FT /evidence="ECO:0000255"
FT MOTIF 60..61
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 63..64
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT MOTIF 86..87
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 50274 MW; 6FAD2C63953AAC07 CRC64;
MNESVPDSVE DNGNSVPANG LLVLPDNDHE EGGVGSPQRS NSVESPGGSV HSTRKGFGLK
KWRRIKRDGP VRDEAAPVDD GSKLLKRGLA GLVNPPSKHV EFSSVEARQS SEGSVGSVNM
VHHPGVANGF SPDIGCMFAV GQAFEKSEEH SGNTIGGKNV VGGKVVSGSQ EKLWSDTIKR
ASEERGDIEK EKPCSSLDSD LRSSDFVFST GSVSVGNHGE KDERLTMNYI GGFSNEGQVK
EEVQTYSRSE NGNKEDDGES KKNNNHWADK DALADSIRSF AVLQEVLWKE VQSFQELGKE
SVLLHSNTDE LSSDQPSHQN CKEDNSTSSG SKALILKEKV KLLEHKLEEA RAALEAKEAR
IQELENSKIE SELECIFQRK IETEIEHLML TRSLSSLQVL QETKKLHSLK EDPVSNRGNI
LGKTCKLGFY ILTQLILLVS ILRFLVLQFS PASRLVIPT
