WIT1_ARATH
ID WIT1_ARATH Reviewed; 703 AA.
AC Q8L7E5; Q9LFL8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=WPP domain-interacting tail-anchored protein 1;
GN Name=WIT1; OrderedLocusNames=At5g11390; ORFNames=F2I11.280;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 PROTEIN SEQUENCE OF 285-296; 351-386 AND 645-663, FUNCTION, DIMERIZATION,
RP INTERACTION WITH WIP2; WPP1; WPP2; RANGAP1 AND RANGAP2, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
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 [5]
RP INTERACTION WITH WPP1; WPP2 AND HSP70-1, AND SUBCELLULAR LOCATION.
RX PubMed=19617588; DOI=10.1104/pp.109.143404;
RA Brkljacic J., Zhao Q., Meier I.;
RT "WPP-domain proteins mimic the activity of the HSC70-1 chaperone in
RT preventing mistargeting of RanGAP1-anchoring protein WIT1.";
RL Plant Physiol. 151:142-154(2009).
RN [6]
RP INTERACTION WITH KAKU1 AND WIP1.
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 [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 INTERACTION WITH KAKU1.
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: Together with WIT2, required for the nuclear envelope docking
CC of RANGAP proteins in root tips. {ECO:0000269|PubMed:18591351}.
CC -!- SUBUNIT: Homodimer. Component of Ran complexes at least composed of
CC WIT1 or WIT2, RANGAP1 or RANGAP2, and WIP1 or WIP2 or WIP3. Interacts
CC with WIP2, WPP1/MAF1, WPP2/MAF2, RANGAP1 and RANGAP2. Component of a
CC ternary complex composed of WPP1, HSP70-1 and WIT1. Interacts with
CC KAKU1 (PubMed:23973298, PubMed:25759303). Interacts with WIP1
CC (PubMed:23973298). {ECO:0000269|PubMed:18591351,
CC ECO:0000269|PubMed:19617588, ECO:0000269|PubMed:23973298,
CC ECO:0000269|PubMed:25759303}.
CC -!- INTERACTION:
CC Q8L7E5; Q9LE82: RANGAP1; NbExp=5; IntAct=EBI-1796628, EBI-1779351;
CC Q8L7E5; Q8GXA4: WIP1; NbExp=4; IntAct=EBI-1796628, EBI-1779367;
CC Q8L7E5; Q9FH18-1: WIP2; NbExp=2; IntAct=EBI-1796628, EBI-1954306;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope. Nucleus membrane; Single-pass
CC membrane protein. Note=During cytokinesis, aggregates around nuclear
CC pores at the cell plate.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18591351}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB96674.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL360314; CAB96674.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91671.1; -; Genomic_DNA.
DR EMBL; AY136301; AAM96967.1; -; mRNA.
DR EMBL; BT000394; AAN15713.1; -; mRNA.
DR RefSeq; NP_196700.2; NM_121177.4.
DR AlphaFoldDB; Q8L7E5; -.
DR SMR; Q8L7E5; -.
DR BioGRID; 16288; 9.
DR IntAct; Q8L7E5; 6.
DR STRING; 3702.AT5G11390.1; -.
DR iPTMnet; Q8L7E5; -.
DR PaxDb; Q8L7E5; -.
DR PRIDE; Q8L7E5; -.
DR ProteomicsDB; 243077; -.
DR EnsemblPlants; AT5G11390.1; AT5G11390.1; AT5G11390.
DR GeneID; 831010; -.
DR Gramene; AT5G11390.1; AT5G11390.1; AT5G11390.
DR KEGG; ath:AT5G11390; -.
DR Araport; AT5G11390; -.
DR TAIR; locus:2148057; AT5G11390.
DR eggNOG; ENOG502QPXD; Eukaryota.
DR HOGENOM; CLU_023491_0_0_1; -.
DR InParanoid; Q8L7E5; -.
DR OMA; TMHVATR; -.
DR OrthoDB; 701646at2759; -.
DR PhylomeDB; Q8L7E5; -.
DR PRO; PR:Q8L7E5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L7E5; baseline and differential.
DR Genevisible; Q8L7E5; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR040060; WIT1.
DR InterPro; IPR039976; WIT1/WIT2.
DR PANTHER; PTHR35705; PTHR35705; 1.
DR PANTHER; PTHR35705:SF1; PTHR35705:SF1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Direct protein sequencing; Membrane; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..703
FT /note="WPP domain-interacting tail-anchored protein 1"
FT /id="PRO_0000347194"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..183
FT /evidence="ECO:0000255"
FT COILED 236..265
FT /evidence="ECO:0000255"
FT COILED 318..461
FT /evidence="ECO:0000255"
FT COILED 500..604
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 235
FT /note="M -> I (in Ref. 3; AAN15713/AAM96967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 703 AA; 79048 MW; 71B9509BD03E3EE8 CRC64;
METETEHDRT VSVDDNDSLV PEPSSTKESF FEDLSLTGQV MNPQLSSAGE VLTKVELDFA
FVSEKLVNLS LLTMQLGTRE NDFESFVSKK EEDEEEPSSN VDDDDDSAEK ALEFDLLSSI
LNSEVKELES LLGFLQNEIQ SARVMISPFQ HDGEAFLDLE GKLNDTEQSL GQLMEQVVEM
KKQSSNFQRL SSGLDEQGSW SGGQTSVSQN DGEFGDLSAK INMQTADQQR NVLRMLEKSL
AKEMELEKKL SESRNTEREL EMKLYSSEQD VVYMEEVTED AFSRWLEADN AAEVFKGTSK
EMSGKLQILQ FNLSGSFKRE DNLKSKLVDS KERLEAKECA LHKLDSSNAR LADFLVAQTE
GLKESLQEAE EKLILLNTEN STLSEKVSSL EEQLNEYGIQ TEDADATSGA LITDLERINE
ELKDKLAKTE ARAEETESKC KILEESKKEL QDELGNFRDK GFTIHKLASL EKHLRDSDLQ
LEHAVAAVEA SKEKQNLLYS TVSDMEDVIE DLKSKVLKAE NRADITEEKL IMVSESNAEV
NEELKFFKGR LKEGEKYLQQ AEERKLRTAK DIGVHNKIMK KLVMQLAAER ERLHKQITNL
SRENCVLMVK LKKVGKTGYM ESGNGSEVSP KSDQNASSCH QGSRLQATFI SLTNPEEEET
GSKSDIGSVR RLDVGALRFK HILVAILVIL ISSIAYVISQ QNM
