(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 92.
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       Q9LE82:RANGAP1; NbExp=6; IntAct=EBI-1779367, EBI-1779351;
CC       Q9FH18:WIP2; NbExp=3; IntAct=EBI-1779367, EBI-1779466;
CC       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};
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   SMR; Q8GXA4; -.
DR   BioGrid; 927646; 7.
DR   DIP; DIP-46425N; -.
DR   IntAct; Q8GXA4; 70.
DR   STRING; 3702.AT4G26455.1; -.
DR   iPTMnet; Q8GXA4; -.
DR   PaxDb; Q8GXA4; -.
DR   PRIDE; Q8GXA4; -.
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; ENOG410IHEQ; Eukaryota.
DR   eggNOG; ENOG410YHC5; LUCA.
DR   HOGENOM; HOG000093093; -.
DR   OMA; NEHFTEG; -.
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:0006997; P:nucleus organization; IGI:TAIR.
PE   1: Evidence at protein level;
DR   PRODOM; Q8GXA4.
DR   SWISS-2DPAGE; Q8GXA4.
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   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"
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
//

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