WIP1_ARATH
ID WIP1_ARATH Reviewed; 489 AA.
AC Q8GXA4; O65589;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=WPP domain-interacting protein 1;
GN Name=WIP1; OrderedLocusNames=At4g26455; ORFNames=M3E9.120;
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 [MRNA].
RA Xu X.M., Meulia T., Meier I.;
RT "The kingdom- and tissue-specific anchorage of plant RanGAP to the nuclear
RT envelope involves a novel family of plant nuclear pore-associated
RT transmembrane proteins.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP FUNCTION, AND SUBUNIT.
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 [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP INTERACTION WITH WPP1; WPP2; RANGAP1 AND RANGAP2, NUCLEAR LOCALIZATION
RP SIGNAL, 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 [9]
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 [10]
RP INTERACTION WITH WIT1 AND SUN2.
RX PubMed=23973298; DOI=10.1016/j.cub.2013.07.035;
RA Tamura K., Iwabuchi K., Fukao Y., Kondo M., Okamoto K., Ueda H.,
RA Nishimura M., Hara-Nishimura I.;
RT "Myosin XI-i links the nuclear membrane to the cytoskeleton to control
RT nuclear movement and shape in Arabidopsis.";
RL Curr. Biol. 23:1776-1781(2013).
RN [11]
RP INTERACTION WITH SUN3.
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 [12]
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 [13]
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 [14]
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, PubMed:18591351). As component of the SUN-
CC WIP-WIT2-KAKU1 complex, mediates the transfer of cytoplasmic forces to
CC the nuclear envelope (NE), leading to nuclear shape changes
CC (PubMed:25759303). {ECO:0000269|PubMed:17600715,
CC ECO:0000269|PubMed:18591351, ECO:0000269|PubMed:25759303}.
CC -!- SUBUNIT: Homodimer and heterodimer with WIP2. 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, WPP1/MAF1, and
CC WPP2/MAF2 (PubMed:17600715, PubMed:18591351). Interacts with SUN1 and
CC 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 WIT1 and
CC SUN2 (PubMed:23973298). Interacts with WIT2 (PubMed:25759303).
CC Interacts with SUN3 (PubMed:25217773). {ECO:0000269|PubMed:17600715,
CC ECO:0000269|PubMed:18591351, ECO:0000269|PubMed:22270916,
CC ECO:0000269|PubMed:23973298, ECO:0000269|PubMed:25217773,
CC ECO:0000269|PubMed:25330379, ECO:0000269|PubMed:25759303}.
CC -!- INTERACTION:
CC Q8GXA4; Q84MC7: PYL9; NbExp=3; IntAct=EBI-1779367, EBI-2349513;
CC Q8GXA4; Q9LE82: RANGAP1; NbExp=6; IntAct=EBI-1779367, EBI-1779351;
CC Q8GXA4; Q9FH18: WIP2; NbExp=3; IntAct=EBI-1779367, EBI-1779466;
CC Q8GXA4; Q8L7E5: WIT1; NbExp=4; IntAct=EBI-1779367, 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 -!- 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, vascular tissue
CC around the shoot apex, and in young leaf primodia. In flowers, detected
CC in the stamens and at the 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|PubMed:25217773}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18225.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At4g26450 and At4g26455.; Evidence={ECO:0000305};
CC Sequence=CAB79500.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At4g26450 and At4g26455.; Evidence={ECO:0000305};
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DR EMBL; EF554923; ABU43100.1; -; mRNA.
DR EMBL; AL022223; CAA18225.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79500.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85201.1; -; Genomic_DNA.
DR EMBL; AK118341; BAC42955.1; -; mRNA.
DR EMBL; BT003145; AAO24577.1; -; mRNA.
DR EMBL; AK228147; BAF00103.1; -; mRNA.
DR PIR; T05059; T05059.
DR RefSeq; NP_001154269.1; NM_001160797.2.
DR AlphaFoldDB; Q8GXA4; -.
DR SMR; Q8GXA4; -.
DR BioGRID; 927646; 8.
DR DIP; DIP-46425N; -.
DR IntAct; Q8GXA4; 71.
DR STRING; 3702.AT4G26455.1; -.
DR iPTMnet; Q8GXA4; -.
DR PaxDb; Q8GXA4; -.
DR PRIDE; Q8GXA4; -.
DR ProteomicsDB; 242642; -.
DR EnsemblPlants; AT4G26455.1; AT4G26455.1; AT4G26455.
DR GeneID; 7922386; -.
DR Gramene; AT4G26455.1; AT4G26455.1; AT4G26455.
DR KEGG; ath:AT4G26455; -.
DR Araport; AT4G26455; -.
DR TAIR; locus:5019474842; AT4G26455.
DR eggNOG; ENOG502QTZN; Eukaryota.
DR HOGENOM; CLU_057777_0_0_1; -.
DR OMA; PKARYES; -.
DR OrthoDB; 1230226at2759; -.
DR PhylomeDB; Q8GXA4; -.
DR PRO; PR:Q8GXA4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GXA4; 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; IPI:TAIR.
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..489
FT /note="WPP domain-interacting protein 1"
FT /id="PRO_0000347196"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 459..489
FT /note="KASH"
FT /evidence="ECO:0000305|PubMed:25217773"
FT REGION 49..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 323..446
FT /evidence="ECO:0000255"
FT MOTIF 80..81
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000269|PubMed:17600715"
FT MOTIF 83..84
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000269|PubMed:17600715"
FT MOTIF 104..105
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000269|PubMed:17600715"
FT COMPBIAS 207..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 53902 MW; 3DCD663768750292 CRC64;
MDLESESSAL ESVDDNVLIQ QSASNVCDDG RSLDNGSCSD ESVKLLSTSN SVELGKPMSF
DSPGDGGGAY SPVLKGQGLR KWRRIRRDLV KDTSANMENS KALKRGLSGV AHSHGKQMQF
QSPEVEQESQ GSVGSVNMLK SSGDGFDILG SSGYDSRFVA GVGFSAGMDL EIDDDRSSKS
STVARAPKVI RYEKPMISSG QGGNIRVENS KKHRGESVDF EKENSYSSLE SDSRKQSGRM
MDYNGENGET SMRKDDAGGE GGESINTDNR YSDEMDPLTE AINGFLALQD ALEKEVQQFQ
EIGNEPMPQH HEQVSEANSP HPEIVTLVNN VEQLENMLEE TRSMLEVKES HIRDLESTTN
QSKHSWGGTE IVVEDIFRQK IEAEIEYLIY SRSIDNLNSQ MKLIDEQESL AEEQTHETLN
KLGRVQTKAA NFTNRAQDLQ NDCIEITGTI KKRACKITSY VLIQLVLLST VVLLLLSQLL
PEPDTVVPT
