WIT2_ARATH
ID WIT2_ARATH Reviewed; 627 AA.
AC A8MQR0; Q9CAB0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=WPP domain-interacting tail-anchored protein 2;
GN Name=WIT2; OrderedLocusNames=At1g68910; ORFNames=T6L1.9;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 PROTEIN SEQUENCE OF 236-253 (ISOFORM 1/2), FUNCTION, AND TISSUE
RP 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 [4]
RP INTERACTION WITH KAKU1.
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 [5]
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 [6]
RP FUNCTION, INTERACTION WITH WIP1; WIP2; WIP3 AND KAKU1, 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: Together with WIT1, required for the nuclear envelope docking
CC of RANGAP proteins in root tips (PubMed:18591351). Plays a role in
CC nuclear shape determination (PubMed:25759303). 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:18591351,
CC 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 KAKU1 (PubMed:23973298, PubMed:25759303). Core component of the
CC LINC 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 WIP1, WIP2 and WIP3
CC (PubMed:25759303). {ECO:0000250, ECO:0000269|PubMed:23973298,
CC ECO:0000269|PubMed:25759303}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A8MQR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8MQR0-2; Sequence=VSP_035069, VSP_035070;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18591351}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51595.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011665; AAG51595.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34858.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34859.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34860.1; -; Genomic_DNA.
DR PIR; F96713; F96713.
DR RefSeq; NP_001077797.1; NM_001084328.2. [A8MQR0-2]
DR RefSeq; NP_001185353.1; NM_001198424.2. [A8MQR0-2]
DR RefSeq; NP_177057.2; NM_105565.3. [A8MQR0-1]
DR AlphaFoldDB; A8MQR0; -.
DR SMR; A8MQR0; -.
DR BioGRID; 28445; 5.
DR IntAct; A8MQR0; 1.
DR STRING; 3702.AT1G68910.1; -.
DR PaxDb; A8MQR0; -.
DR PRIDE; A8MQR0; -.
DR ProteomicsDB; 242465; -. [A8MQR0-1]
DR EnsemblPlants; AT1G68910.1; AT1G68910.1; AT1G68910. [A8MQR0-1]
DR EnsemblPlants; AT1G68910.2; AT1G68910.2; AT1G68910. [A8MQR0-2]
DR EnsemblPlants; AT1G68910.3; AT1G68910.3; AT1G68910. [A8MQR0-2]
DR GeneID; 843224; -.
DR Gramene; AT1G68910.1; AT1G68910.1; AT1G68910. [A8MQR0-1]
DR Gramene; AT1G68910.2; AT1G68910.2; AT1G68910. [A8MQR0-2]
DR Gramene; AT1G68910.3; AT1G68910.3; AT1G68910. [A8MQR0-2]
DR KEGG; ath:AT1G68910; -.
DR Araport; AT1G68910; -.
DR TAIR; locus:2205470; AT1G68910.
DR eggNOG; ENOG502QPXD; Eukaryota.
DR InParanoid; A8MQR0; -.
DR OMA; IDNCIGQ; -.
DR OrthoDB; 701646at2759; -.
DR PhylomeDB; A8MQR0; -.
DR PRO; PR:A8MQR0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A8MQR0; baseline and differential.
DR Genevisible; A8MQR0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0080115; F:myosin XI tail binding; IDA:TAIR.
DR GO; GO:2000769; P:regulation of establishment or maintenance of cell polarity regulating cell shape; IMP:UniProtKB.
DR InterPro; IPR039976; WIT1/WIT2.
DR InterPro; IPR040061; WIT2.
DR PANTHER; PTHR35705; PTHR35705; 1.
DR PANTHER; PTHR35705:SF9; PTHR35705:SF9; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Direct protein sequencing; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..627
FT /note="WPP domain-interacting tail-anchored protein 2"
FT /id="PRO_0000347195"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 577..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 81..152
FT /evidence="ECO:0000255"
FT COILED 188..218
FT /evidence="ECO:0000255"
FT COILED 312..542
FT /evidence="ECO:0000255"
FT VAR_SEQ 580..582
FT /note="EDE -> AGG (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035069"
FT VAR_SEQ 583..627
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_035070"
SQ SEQUENCE 627 AA; 71852 MW; 02F0A683B36AC8D2 CRC64;
MEEIIREDYF EALSSRNEEE QEMLRMLTKL EIDSAYTSEK LMNLHVLLMH LLAWDNDLEG
MGTLDSSPAS FEKALTFDLL CGILESEVKE VDEVLDVLEA QIVDTSYKIS SCKHGNYIVI
EGKLGESAES LKQSRGQVSE ITLQLAQLRR TLHYIRNGTS ENEESVELRQ KYALKPSDLR
HKNALRMLEK SLSRELELEK KLMEFQQNEE QLKLKLHYTE EVSSRMEEAS EFIWGRFLEA
DNSSEVLTGI SKELVGRLQI LQFSLNGSAQ RESELKSKLE DCTVQLEAKD LLVQKLEGTI
SENSEIVSEV LTLREYVKSA EQKLKNTDLE LKSVNASKQE ILVHLAEMEN ANESVKENLF
EAESRAESGE AKIKELDAAN LELTEELNFL KDADDKKTKK VNSLEKQVRE LEVQVQNSKV
SSEANQEQQN MLYSAIWDME TLIEDLKSKA SKAESRTETV EEQCIVLSTT NSELNKDVSF
LRQKAKSLEA MLDLANNEKE RYAQEITTRN KVLMDMMLQL SSERERIQEQ LYSLAKENKI
LRVNQCSNTY QRNGSYAGDK ELSFHADGHE IEALAESLQE DERTREEPEK QSVSEKSSEI
RRAIKLKHIL VVALVFVLFC SFFGVTY
