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 24-JAN-2024, entry version 93. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q94AV5; -. DR BioGRID; 5870; 2. DR IntAct; Q94AV5; 4. DR STRING; 3702.Q94AV5; -. DR iPTMnet; Q94AV5; -. DR PaxDb; 3702-AT3G13360-1; -. 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; AT3G13360; WIP3. DR eggNOG; ENOG502QTZN; Eukaryota. DR HOGENOM; CLU_057777_0_0_1; -. DR InParanoid; Q94AV5; -. DR OMA; HENCRED; -. DR PhylomeDB; Q94AV5; -. DR PRO; PR:Q94AV5; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q94AV5; baseline and differential. 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; WPP DOMAIN-INTERACTING PROTEIN 2; 1. DR PANTHER; PTHR34562:SF9; WPP DOMAIN-INTERACTING PROTEIN 3; 1. DR Genevisible; Q94AV5; AT. 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 //