WAV3_ARATH
ID WAV3_ARATH Reviewed; 740 AA.
AC Q9LTA6; Q0WLQ3;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase WAV3 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:22122664};
DE AltName: Full=Protein WAVY GROWTH 3 {ECO:0000303|PubMed:22122664};
DE AltName: Full=RING-type E3 ubiquitin transferase WAV3 {ECO:0000305};
GN Name=WAV3 {ECO:0000303|PubMed:22122664};
GN OrderedLocusNames=At5g49665 {ECO:0000312|Araport:AT5G49665};
GN ORFNames=K2I5.2 {ECO:0000312|EMBL:BAA98154.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP INTERACTION WITH SINAT1; SINAT2; SINAT3; SINAT4; SINAT5; TOR1/SPR2 AND
RP FIP2, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-740.
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.
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of
CC root growth. Acts as positive regulator of root gravitropism. Possesses
CC E3 protein ligase activity in vitro. {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:0000269|PubMed:22122664};
CC -!- SUBUNIT: Interacts with SINAT1, SINAT2, SINAT3, SINAT4, SINAT5,
CC TOR1/SPR2 and FIP2. {ECO:0000269|PubMed:22122664}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips and leaf primordia.
CC {ECO:0000269|PubMed:22122664}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings exhibit enhanced root wavy growth and
CC curvature in response to gravitropism. {ECO:0000269|PubMed:22122664}.
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DR EMBL; AB251345; BAL15672.1; -; Genomic_DNA.
DR EMBL; AB025613; BAA98154.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95843.1; -; Genomic_DNA.
DR EMBL; BT000441; AAN17418.1; -; mRNA.
DR EMBL; BT010337; AAQ56780.1; -; mRNA.
DR EMBL; AK230140; BAF01954.1; -; mRNA.
DR RefSeq; NP_680410.1; NM_148105.3.
DR AlphaFoldDB; Q9LTA6; -.
DR SMR; Q9LTA6; -.
DR STRING; 3702.AT5G49665.1; -.
DR iPTMnet; Q9LTA6; -.
DR PaxDb; Q9LTA6; -.
DR PRIDE; Q9LTA6; -.
DR ProteomicsDB; 242764; -.
DR EnsemblPlants; AT5G49665.1; AT5G49665.1; AT5G49665.
DR GeneID; 835029; -.
DR Gramene; AT5G49665.1; AT5G49665.1; AT5G49665.
DR KEGG; ath:AT5G49665; -.
DR Araport; AT5G49665; -.
DR TAIR; locus:504954897; AT5G49665.
DR eggNOG; ENOG502QRQC; Eukaryota.
DR HOGENOM; CLU_006228_3_0_1; -.
DR InParanoid; Q9LTA6; -.
DR OMA; FAKCIGG; -.
DR OrthoDB; 274565at2759; -.
DR PhylomeDB; Q9LTA6; -.
DR PRO; PR:Q9LTA6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTA6; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0010274; P:hydrotropism; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA: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; PF13519; VWA_2; 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..740
FT /note="E3 ubiquitin-protein ligase WAV3"
FT /id="PRO_0000443504"
FT DOMAIN 332..476
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 122..167
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 14..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 80236 MW; DB436FE8A8935501 CRC64;
MGTGWRRAFC TTAPRNSDAA APDLDKQRTG YNLTPSPSPR SCVKLAFLSG GSNPSTPRST
SSPSLRCRTA DAQTPTAEQT STPRSATKSP RLSLAAISNP SSPRSPLKLS LFRNSFKFRS
TCGICLNSVK TGQGTAKYTA ECSHAFHFPC IADYVRKQGK LVCPVCNSIW KDASLLVPHK
NATESPLDDS VSVIQEKRVV VTSSPRAKPR PKQSDYSRFY DDDEPLLSPR FVTIPEADEN
CGGEEEDDVP QFKGFVVDPN PSFAVKTNEI PVNGRDFGNV QVSLLPEAAV VSVGCGYETR
AVALRVKAPP PLTARGGVGR RLLDPSQRAP VDLVVVVDVG GTMNGAKLQM VKRAMRLVIS
SLGSADRLSI VAVVMTVPKR LLPLKRMTEH GKRSAGAVVD GLLCGQGSNT SEALKKASRV
LEDRRERNPV ASIVLLTDGQ GQLSKVHTNQ RSTITNVGST RFAHIEIPVT EHGFGESGGC
SNAPAEEAFA KCIGGLLSVV VQDLRIQIRV GSGSGPCEIS AIYLCNGRPT LVSSGSGSVR
LGDLYAGEER ELLVELRVPS TATRAYQILS VRGLFKDPST QEVVYGRDQS LRVPQAVRSS
SSPRIERLRS LFIATRAVAE SRRLVEYGEC TSAYHLLTSA RALLGQSGTV EAAEYIKVVE
AELVEVQWRG QQLMEYQSQH QQQHNQRRRG SERETTTTMT LMDENGEPLT PASAWRAAEK
LAKLAMMKKS DLHGFENARF
