WAVH2_ARATH
ID WAVH2_ARATH Reviewed; 717 AA.
AC Q0WQX9; O49548; Q8GY95;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Probable E3 ubiquitin-protein ligase WAVH2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Protein WAV3 homolog 2 {ECO:0000303|PubMed:22122664};
DE AltName: Full=RING-type E3 ubiquitin transferase WAVH2 {ECO:0000305};
GN Name=WAVH2 {ECO:0000303|PubMed:22122664};
GN OrderedLocusNames=At5g65683 {ECO:0000312|Araport:AT5G65683};
GN ORFNames=F6H11.200 {ECO:0000312|EMBL:CAA16691.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
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 [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 TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22122664; DOI=10.1111/j.1365-313x.2011.04870.x;
RA Sakai T., Mochizuki S., Haga K., Uehara Y., Suzuki A., Harada A., Wada T.,
RA Ishiguro S., Okada K.;
RT "The wavy growth 3 E3 ligase family controls the gravitropic response in
RT Arabidopsis roots.";
RL Plant J. 70:303-314(2012).
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase involved in the
CC regulation of root growth. Acts as positive regulator of root
CC gravitropism. {ECO:0000269|PubMed:22122664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305};
CC -!- INTERACTION:
CC Q0WQX9; Q17TI5: BRX; NbExp=3; IntAct=EBI-4426718, EBI-4426649;
CC Q0WQX9; Q8GXW1: RGL2; NbExp=3; IntAct=EBI-4426718, EBI-963665;
CC -!- TISSUE SPECIFICITY: Expressed in root tips, cotyledons, leaf primordia
CC and hypocotyls. {ECO:0000269|PubMed:22122664}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10674.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA16691.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB010075; BAB10674.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL021684; CAA16691.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98086.1; -; Genomic_DNA.
DR EMBL; AK117780; BAC42427.1; -; mRNA.
DR EMBL; BT005960; AAO64895.1; -; mRNA.
DR EMBL; AK228549; BAF00470.1; -; mRNA.
DR PIR; T05901; T05901.
DR RefSeq; NP_680467.1; NM_148162.4.
DR AlphaFoldDB; Q0WQX9; -.
DR SMR; Q0WQX9; -.
DR IntAct; Q0WQX9; 29.
DR STRING; 3702.AT5G65683.1; -.
DR iPTMnet; Q0WQX9; -.
DR PaxDb; Q0WQX9; -.
DR PRIDE; Q0WQX9; -.
DR ProteomicsDB; 242653; -.
DR EnsemblPlants; AT5G65683.1; AT5G65683.1; AT5G65683.
DR GeneID; 836695; -.
DR Gramene; AT5G65683.1; AT5G65683.1; AT5G65683.
DR KEGG; ath:AT5G65683; -.
DR Araport; AT5G65683; -.
DR TAIR; locus:504954891; AT5G65683.
DR eggNOG; ENOG502QVJZ; Eukaryota.
DR HOGENOM; CLU_006228_3_0_1; -.
DR InParanoid; Q0WQX9; -.
DR OMA; SIRAAYI; -.
DR OrthoDB; 274565at2759; -.
DR PhylomeDB; Q0WQX9; -.
DR PRO; PR:Q0WQX9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WQX9; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00092; VWA; 1.
DR Pfam; PF17123; zf-RING_11; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..717
FT /note="Probable E3 ubiquitin-protein ligase WAVH2"
FT /id="PRO_0000443506"
FT DOMAIN 326..456
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 140..184
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 13..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 42
FT /note="F -> L (in Ref. 4; BAC42427 and 5; AAO64895)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="S -> P (in Ref. 4; BAC42427 and 5; AAO64895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 717 AA; 78579 MW; 3C2EAA95EA330499 CRC64;
MVFGWRKAFC TSVSSNQDKP QQHSSLHTTD PPIPTPRFRS KFGFLSNPST PRLRSRGGSG
TGCRSSASTS VTIPSLPTSP KLHCRTTSNA TPRTSNSSSP KFFSNPSSPK SSSSSSSQGG
GGVSLLRATL LLNKSNSSRC AICLQRVNSN QSNSTAAIFT AECSHSFHLS CVNGLEDKRC
PFCSAAWNHA PKSNYPAVNN NFGSDPIRRP EIREIKTGKS LRVYNDDEPL AYSPVSLAQI
NTIHESDEND DVEDDDDFPG FFRDSSITSD MVPSISGNLE VKLLPESAVV ETGKKKETHV
VIMKLKASPS PSSITDAIKA RRPSIDLVTV LDLSNGGANL QTVKHAMRSV ISLLREMDRL
SIVVFSTGSK RLMPLRRMTA KGRRSARRMV DALGGMETTG GVGMSVNDAL KKAVKVVEDR
REKNPSTSIF VLSDGQDQPE AVLKAKLNAT RIPFVVSTTR FSRPEIPVHS VYIASPGALL
HAPLRDAFTE RIASLLNVTL HNVKLNLSLV NGSHLTEISS VYSLTGRLEN FGSGSVIQVG
DLFAEEEREF LVELKVPTSS SGSHQVMSVQ SSIVDQMTHQ PMTCPKEKRF LIPRPQSVRY
VSSSIERLRN LHSMCRAVAD SRRLIEREDL SGAYQVLTTA RSNASHSDDS LRSLEVELNE
LSRIKPRNSI LNRTEDKPEQ LTPTSAWRAA EKLAKVAIMR KHLNRVSDMH GLENARF
